DB code: S00225
RLCP classification | 8.131.42001.6 : Isomerization | |
---|---|---|
8.113.42001.5 : Isomerization | ||
CATH domain | 3.20.20.70 : TIM Barrel | Catalytic domain |
E.C. | 5.3.1.1 | |
CSA | 1hti 1tph | |
M-CSA | 1hti 1tph | |
MACiE |
CATH domain | Related DB codes (homologues) |
---|---|
3.20.20.70 : TIM Barrel | S00215 S00217 S00218 S00219 S00532 S00198 S00220 S00745 S00537 S00538 S00539 S00826 S00841 S00235 S00239 S00240 S00243 S00244 S00199 S00200 S00201 S00221 S00222 S00847 S00224 S00226 D00014 D00029 M00141 T00015 T00239 D00664 D00665 D00804 D00863 T00089 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Pfam | RefSeq |
---|---|---|---|---|
P00943 |
Triosephosphate isomerase
|
TIM
EC 5.3.1.1 Triose-phosphate isomerase |
PF00121
(TIM)
[Graphical View] |
|
P00940 |
Triosephosphate isomerase
|
TIM
EC 5.3.1.1 Triose-phosphate isomerase |
PF00121
(TIM)
[Graphical View] |
NP_990782.1
(Protein)
NM_205451.1 (DNA/RNA sequence) |
P0A858 |
Triosephosphate isomerase
|
TIM
EC 5.3.1.1 Triose-phosphate isomerase |
PF00121
(TIM)
[Graphical View] |
NP_418354.1
(Protein)
NC_000913.2 (DNA/RNA sequence) YP_491532.1 (Protein) NC_007779.1 (DNA/RNA sequence) |
P62002 |
Triosephosphate isomerase
|
TIM
EC 5.3.1.1 Triose-phosphate isomerase |
PF00121
(TIM)
[Graphical View] |
NP_579649.1
(Protein)
NC_003413.1 (DNA/RNA sequence) |
P62003 |
Triosephosphate isomerase
|
TIM
EC 5.3.1.1 Triose-phosphate isomerase |
PF00121
(TIM)
[Graphical View] |
|
P48499 |
Triosephosphate isomerase
|
TIM
EC 5.3.1.1 Triose-phosphate isomerase |
PF00121
(TIM)
[Graphical View] |
|
Q07412 |
Triosephosphate isomerase
|
TIM
EC 5.3.1.1 Triose-phosphate isomerase |
PF00121
(TIM)
[Graphical View] |
|
P60174 |
Triosephosphate isomerase
|
TIM
EC 5.3.1.1 Triose-phosphate isomerase |
PF00121
(TIM)
[Graphical View] |
NP_000356.1
(Protein)
NM_000365.5 (DNA/RNA sequence) NP_001152759.1 (Protein) NM_001159287.1 (DNA/RNA sequence) NP_001244955.1 (Protein) NM_001258026.1 (DNA/RNA sequence) |
P60175 |
Triosephosphate isomerase
|
TIM
EC 5.3.1.1 Triose-phosphate isomerase |
PF00121
(TIM)
[Graphical View] |
NP_001065250.1
(Protein)
NM_001071782.1 (DNA/RNA sequence) |
P04789 |
Triosephosphate isomerase, glycosomal
|
TIM
Triose-phosphate isomerase EC 5.3.1.1 |
PF00121
(TIM)
[Graphical View] |
|
P52270 |
Triosephosphate isomerase, glycosomal
|
TIM
Triose-phosphate isomerase EC 5.3.1.1 |
PF00121
(TIM)
[Graphical View] |
|
P50921 |
Triosephosphate isomerase
|
TIM
EC 5.3.1.1 Triose-phosphate isomerase |
PF00121
(TIM)
[Graphical View] |
|
P00942 |
Triosephosphate isomerase
|
TIM
EC 5.3.1.1 Triose-phosphate isomerase |
PF00121
(TIM)
[Graphical View] |
NP_010335.1
(Protein)
NM_001180358.1 (DNA/RNA sequence) |
KEGG enzyme name |
---|
triose-phosphate isomerase
phosphotriose isomerase triose phosphoisomerase triose phosphate mutase D-glyceraldehyde-3-phosphate ketol-isomerase |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
P00943 | TPIS_BACST | D-glyceraldehyde 3-phosphate = glycerone phosphate. | Homodimer. | Cytoplasm (Probable). | |
P00940 | TPIS_CHICK | D-glyceraldehyde 3-phosphate = glycerone phosphate. | Homodimer. | ||
P0A858 | TPIS_ECOLI | D-glyceraldehyde 3-phosphate = glycerone phosphate. | Homodimer. | Cytoplasm (Probable). | |
P62002 | TPIS_PYRFU | D-glyceraldehyde 3-phosphate = glycerone phosphate. | Homotetramer (By similarity). | Cytoplasm (Probable). | |
P62003 | TPIS_PYRWO | D-glyceraldehyde 3-phosphate = glycerone phosphate. | Homotetramer. | Cytoplasm (Probable). | |
P48499 | TPIS_LEIME | D-glyceraldehyde 3-phosphate = glycerone phosphate. | Homodimer. | Cytoplasm. Glycosome. | |
Q07412 | TPIS_PLAFA | D-glyceraldehyde 3-phosphate = glycerone phosphate. | Homodimer. | ||
P60174 | TPIS_HUMAN | D-glyceraldehyde 3-phosphate = glycerone phosphate. | Homodimer. | ||
P60175 | TPIS_PANTR | D-glyceraldehyde 3-phosphate = glycerone phosphate. | Homodimer (By similarity). | ||
P04789 | TPIS_TRYBB | D-glyceraldehyde 3-phosphate = glycerone phosphate. | Homodimer. | Glycosome. | |
P52270 | TPIS_TRYCR | D-glyceraldehyde 3-phosphate = glycerone phosphate. | Homodimer. | Glycosome. | |
P50921 | TPIS_VIBMA | D-glyceraldehyde 3-phosphate = glycerone phosphate. | Homodimer. | Cytoplasm (Probable). | |
P00942 | TPIS_YEAST | D-glyceraldehyde 3-phosphate = glycerone phosphate. | Homodimer. |
KEGG Pathways | Map code | Pathways | E.C. |
---|---|---|
MAP00010 | Glycolysis / Gluconeogenesis | |
MAP00031 | Inositol metabolism | |
MAP00051 | Fructose and mannose metabolism | |
MAP00710 | Carbon fixation in photosynthetic organisms |
Compound table | ||||||||
---|---|---|---|---|---|---|---|---|
Substrates | Products | Intermediates | ||||||
KEGG-id | C00118 | C00111 | I00178 | |||||
E.C. | ||||||||
Compound | D-Glyceraldehyde 3-phosphate | Glycerone phosphate | Enediol form of glycerone phosphate | |||||
Type | carbohydrate,phosphate group/phosphate ion | carbohydrate,phosphate group/phosphate ion | ||||||
ChEBI |
29052 29052 |
16108 16108 |
||||||
PubChem |
439168 439168 |
668 668 |
||||||
1ag1O | Unbound | Unbound | Unbound | |||||
1ag1T | Unbound | Unbound | Unbound | |||||
1amkA | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1aw1A | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1aw1B | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1aw1D | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1aw1E | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1aw1G | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1aw1H | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1aw1J | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1aw1K | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1aw2A | Unbound | Unbound | Unbound | |||||
1aw2B | Unbound | Unbound | Unbound | |||||
1aw2D | Unbound | Unbound | Unbound | |||||
1aw2E | Unbound | Unbound | Unbound | |||||
1aw2G | Unbound | Unbound | Unbound | |||||
1aw2H | Unbound | Unbound | Unbound | |||||
1aw2J | Unbound | Unbound | Unbound | |||||
1aw2K | Unbound | Unbound | Unbound | |||||
1btmA | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1btmB | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1ci1A | Unbound | Unbound | Unbound | |||||
1ci1B | Unbound | Unbound | Unbound | |||||
1dkwA | Unbound | Unbound | Unbound | |||||
1dkwB | Unbound | Unbound | Unbound | |||||
1hg3A | Unbound | Unbound | Intermediate-analogue:3PP | |||||
1hg3B | Unbound | Unbound | Intermediate-analogue:3PP | |||||
1hg3C | Unbound | Unbound | Intermediate-analogue:3PP | |||||
1hg3D | Unbound | Unbound | Intermediate-analogue:3PP | |||||
1hg3E | Unbound | Unbound | Intermediate-analogue:3PP | |||||
1hg3F | Unbound | Unbound | Intermediate-analogue:3PP | |||||
1hg3G | Unbound | Unbound | Intermediate-analogue:3PP | |||||
1hg3H | Unbound | Unbound | Intermediate-analogue:3PP | |||||
1htiA | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1htiB | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1i45A | Unbound | Unbound | Unbound | |||||
1i45B | Unbound | Unbound | Unbound | |||||
1if2A | Analogue:129 | Unbound | Unbound | |||||
1iigA | Unbound | Unbound | Unbound | |||||
1iigB | Unbound | Unbound | Intermediate-analogue:3PP | |||||
1iihA | Unbound | Unbound | Unbound | |||||
1iihB | Analogue:3PG | Unbound | Unbound | |||||
1kv5A | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1kv5B | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1lyxA | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1lzoA | Unbound | Unbound | Unbound | |||||
1lzoB | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1lzoC | Unbound | Unbound | Unbound | |||||
1lzoD | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1m7oA | Analogue:3PG | Unbound | Unbound | |||||
1m7oB | Analogue:3PG | Unbound | Unbound | |||||
1m7pA | Analogue:G3H | Unbound | Unbound | |||||
1m7pB | Analogue:G3H | Unbound | Unbound | |||||
1ml1A | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1ml1C | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1ml1E | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1ml1G | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1ml1I | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1ml1K | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1mssA | Unbound | Unbound | Unbound | |||||
1mssB | Unbound | Unbound | Unbound | |||||
1n55A | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1neyA | Unbound | Bound:13P | Unbound | |||||
1neyB | Unbound | Bound:13P | Unbound | |||||
1nf0A | Unbound | Bound:13P | Unbound | |||||
1nf0B | Unbound | Bound:13P | Unbound | |||||
1o5xA | Unbound | Unbound | Intermediate-analogue:3PY-PO3 | |||||
1o5xB | Unbound | Unbound | Intermediate-analogue:2PG | |||||
1qdsA | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1spqA | Unbound | Unbound | Unbound | |||||
1spqB | Unbound | Unbound | Unbound | |||||
1sq7A | Unbound | Unbound | Unbound | |||||
1sq7B | Unbound | Unbound | Unbound | |||||
1ssdA | Unbound | Unbound | Unbound | |||||
1ssdB | Unbound | Unbound | Unbound | |||||
1ssgA | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1ssgB | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1su5A | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1su5B | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1suxA | Unbound | Unbound | Unbound | |||||
1suxB | Unbound | Unbound | Unbound | |||||
1sw0A | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1sw0B | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1sw3A | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1sw3B | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1sw7A | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1sw7B | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1tcdA | Unbound | Unbound | Unbound | |||||
1tcdB | Unbound | Unbound | Unbound | |||||
1timA | Unbound | Unbound | Unbound | |||||
1timB | Unbound | Unbound | Unbound | |||||
1tmhA | Unbound | Unbound | Unbound | |||||
1tmhB | Unbound | Unbound | Unbound | |||||
1tmhC | Unbound | Unbound | Unbound | |||||
1tmhD | Unbound | Unbound | Unbound | |||||
1tpb1 | Unbound | Analogue:PGH | Unbound | |||||
1tpb2 | Unbound | Analogue:PGH | Unbound | |||||
1tpc1 | Unbound | Analogue:PGH | Unbound | |||||
1tpc2 | Unbound | Analogue:PGH | Unbound | |||||
1tpdA | Unbound | Unbound | Unbound | |||||
1tpdB | Unbound | Unbound | Unbound | |||||
1tpeA | Unbound | Unbound | Unbound | |||||
1tpfA | Unbound | Unbound | Unbound | |||||
1tpfB | Unbound | Unbound | Unbound | |||||
1tph1 | Unbound | Analogue:PGH | Unbound | |||||
1tph2 | Unbound | Analogue:PGH | Unbound | |||||
1tpuA | Unbound | Analogue:PGH | Unbound | |||||
1tpuB | Unbound | Analogue:PGH | Unbound | |||||
1tpvA | Unbound | Analogue:PGH | Unbound | |||||
1tpvB | Unbound | Analogue:PGH | Unbound | |||||
1tpwA | Unbound | Analogue:PGH | Unbound | |||||
1tpwB | Unbound | Analogue:PGH | Unbound | |||||
1trdA | Unbound | Analogue:PGH | Unbound | |||||
1trdB | Unbound | Analogue:PGH | Unbound | |||||
1treA | Unbound | Unbound | Unbound | |||||
1treB | Unbound | Unbound | Unbound | |||||
1triA | Unbound | Unbound | Unbound | |||||
1tsiA | Unbound | Analogue:4PB | Unbound | |||||
1tsiB | Unbound | Unbound | Unbound | |||||
1ttiA | Unbound | Unbound | Transition-state-analogue:PGA | |||||
1ttjA | Unbound | Analogue:PGH | Unbound | |||||
1vgaA | Unbound | Unbound | Unbound | |||||
1vgaB | Unbound | Unbound | Unbound | |||||
1vgaC | Unbound | Unbound | Unbound | |||||
1vgaD | Unbound | Unbound | Unbound | |||||
1woaA | Analogue:G2H | Unbound | Unbound | |||||
1woaB | Analogue:G2H | Unbound | Unbound | |||||
1woaC | Analogue:G2H | Unbound | Unbound | |||||
1woaD | Analogue:G2H | Unbound | Unbound | |||||
1wobA | Unbound | Unbound | Unbound | |||||
1wobB | Unbound | Unbound | Unbound | |||||
1wobC | Unbound | Unbound | Unbound | |||||
1wobD | Unbound | Unbound | Unbound | |||||
1ydvA | Unbound | Unbound | Unbound | |||||
1ydvB | Unbound | Unbound | Unbound | |||||
1ypiA | Unbound | Unbound | Unbound | |||||
1ypiB | Unbound | Unbound | Unbound | |||||
2btmA | Unbound | Unbound | Transition-state-analogue:PGA | |||||
2btmB | Unbound | Unbound | Transition-state-analogue:PGA | |||||
2ypiA | Unbound | Unbound | Transition-state-analogue:PGA | |||||
2ypiB | Unbound | Unbound | Transition-state-analogue:PGA | |||||
3timA | Unbound | Unbound | Unbound | |||||
3timB | Unbound | Unbound | Unbound | |||||
3ypiA | Unbound | Analogue:PGH | Unbound | |||||
3ypiB | Unbound | Analogue:PGH | Unbound | |||||
4timA | Unbound | Unbound | Unbound | |||||
4timB | Unbound | Unbound | Intermediate-analogue:2PG | |||||
5timA | Unbound | Unbound | Unbound | |||||
5timB | Unbound | Unbound | Unbound | |||||
6timA | Unbound | Unbound | Unbound | |||||
6timB | Analogue:G3P | Unbound | Unbound | |||||
7timA | Unbound | Analogue:PGH | Unbound | |||||
7timB | Unbound | Analogue:PGH | Unbound | |||||
8timA | Unbound | Unbound | Unbound | |||||
8timB | Unbound | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
literature [42], [58], [75] & [101] |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1ag1O | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1ag1T | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1amkA | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1aw1A | ASN 9;LYS 11;HIS 97;GLU 169 | |||||||||
1aw1B | ASN 9;LYS 11;HIS 97;GLU 169 | |||||||||
1aw1D | ASN 9;LYS 11;HIS 97;GLU 169 | |||||||||
1aw1E | ASN 9;LYS 11;HIS 97;GLU 169 | |||||||||
1aw1G | ASN 9;LYS 11;HIS 97;GLU 169 | |||||||||
1aw1H | ASN 9;LYS 11;HIS 97;GLU 169 | |||||||||
1aw1J | ASN 9;LYS 11;HIS 97;GLU 169 | |||||||||
1aw1K | ASN 9;LYS 11;HIS 97;GLU 169 | |||||||||
1aw2A | ASN 9;LYS 11;HIS 97;GLU 169 | |||||||||
1aw2B | ASN 9;LYS 11;HIS 97;GLU 169 | |||||||||
1aw2D | ASN 9;LYS 11;HIS 97;GLU 169 | |||||||||
1aw2E | ASN 9;LYS 11;HIS 97;GLU 169 | |||||||||
1aw2G | ASN 9;LYS 11;HIS 97;GLU 169 | |||||||||
1aw2H | ASN 9;LYS 11;HIS 97;GLU 169 | |||||||||
1aw2J | ASN 9;LYS 11;HIS 97;GLU 169 | |||||||||
1aw2K | ASN 9;LYS 11;HIS 97;GLU 169 | |||||||||
1btmA | ASN 8;LYS 10;HIS 94;GLU 166 | |||||||||
1btmB | ASN 8;LYS 10;HIS 94;GLU 166 | |||||||||
1ci1A | ASN 12;LYS 14;HIS 96;GLU 168 | |||||||||
1ci1B | ASN 12;LYS 14;HIS 96;GLU 168 | |||||||||
1dkwA | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1dkwB | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1hg3A | ASN 12;LYS 14;HIS 96;GLU 144 | |||||||||
1hg3B | ASN 12;LYS 14;HIS 96;GLU 144 | |||||||||
1hg3C | ASN 12;LYS 14;HIS 96;GLU 144 | |||||||||
1hg3D | ASN 12;LYS 14;HIS 96;GLU 144 | |||||||||
1hg3E | ASN 12;LYS 14;HIS 96;GLU 144 | |||||||||
1hg3F | ASN 12;LYS 14;HIS 96;GLU 144 | |||||||||
1hg3G | ASN 12;LYS 14;HIS 96;GLU 144 | |||||||||
1hg3H | ASN 12;LYS 14;HIS 96;GLU 144 | |||||||||
1htiA | ASN 11;LYS 13;HIS 95;GLU 165 | |||||||||
1htiB | ASN 11;LYS 13;HIS 95;GLU 165 | |||||||||
1i45A | ASN 10;LYS 12;HIS 95;GLU 165 | FTR 168 | mutant W90Y, W157F, W168FTR | |||||||
1i45B | ASN 10;LYS 12;HIS 95;GLU 165 | FTR 168 | mutant W90Y, W157F, W168FTR | |||||||
1if2A | ASN 11;LYS 13;HIS 95;GLU 167 | mutant E65Q | ||||||||
1iigA | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1iigB | ASN 311;LYS 313;HIS 395;GLU 467 | |||||||||
1iihA | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1iihB | ASN 311;LYS 313;HIS 395;GLU 467 | |||||||||
1kv5A | ASN 11;LYS 13;HIS 95;GLU 167 | mutant R191S | ||||||||
1kv5B | ASN 11;LYS 13;HIS 95;GLU 167 | mutant R191S | ||||||||
1lyxA | ASN 10;LYS 12;HIS 95;GLU 165 | |||||||||
1lzoA | ASN 10;LYS 12;HIS 95;GLU 165 | |||||||||
1lzoB | ASN 10;LYS 12;HIS 95;GLU 165 | |||||||||
1lzoC | ASN 10;LYS 12;HIS 95;GLU 165 | |||||||||
1lzoD | ASN 10;LYS 12;HIS 95;GLU 165 | |||||||||
1m7oA | ASN 10;LYS 12;HIS 95;GLU 165 | |||||||||
1m7oB | ASN 10;LYS 12;HIS 95;GLU 165 | |||||||||
1m7pA | ASN 10;LYS 12;HIS 95;GLU 165 | |||||||||
1m7pB | ASN 10;LYS 12;HIS 95;GLU 165 | |||||||||
1ml1A | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1ml1C | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1ml1E | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1ml1G | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1ml1I | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1ml1K | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1mssA | ASN 11;LYS 13;HIS 95;GLU 167 | mutant F45S, V46S, 68-72 GNADALAS | ||||||||
1mssB | ASN 11;LYS 13;HIS 95;GLU 167 | mutant F45S, V46S, 68-72 GNADALAS | ||||||||
1n55A | ASN 11;LYS 13;HIS 95;GLU 167 | mutant E65Q | ||||||||
1neyA | ASN 10;LYS 12;HIS 95;GLU 165 | FTR 168 | mutant W90Y, W157F, W168FTR | |||||||
1neyB | ASN 10;LYS 12;HIS 95;GLU 165 | FTR 168 | mutant W90Y, W157F, W168FTR | |||||||
1nf0A | ASN 10;LYS 12;HIS 95;GLU 165 | FTR 168 | mutant W90Y, W157F, W168FTR | |||||||
1nf0B | ASN 10;LYS 12;HIS 95;GLU 165 | FTR 168 | mutant W90Y, W157F, W168FTR | |||||||
1o5xA | ASN 10;LYS 12;HIS 95;GLU 165 | mutant A163V | ||||||||
1o5xB | ASN 10;LYS 12;HIS 95;GLU 165 | mutant A163V | ||||||||
1qdsA | ASN 11;LYS 13;HIS 95;GLU 167 | mutant E65Q | ||||||||
1spqA | ASN 11;LYS 13;HIS 95;GLU 165 | mutant A176K | ||||||||
1spqB | ASN 11;LYS 13;HIS 95;GLU 165 | mutant A176K | ||||||||
1sq7A | ASN 11;LYS 13;HIS 95;GLU 165 | mutant K174L, T175W | ||||||||
1sq7B | ASN 11;LYS 13;HIS 95;GLU 165 | mutant K174L, T175W | ||||||||
1ssdA | ASN 11;LYS 13;HIS 95;GLU 165 | mutant K174Y, T175S, A176L | ||||||||
1ssdB | ASN 11;LYS 13;HIS 95;GLU 165 | mutant K174Y, T175S, A176L | ||||||||
1ssgA | ASN 11;LYS 13;HIS 95;GLU 165 | mutant K174Y, T175S, A176L | ||||||||
1ssgB | ASN 11;LYS 13;HIS 95;GLU 165 | mutant K174Y, T175S, A176L | ||||||||
1su5A | ASN 11;LYS 13;HIS 95;GLU 165 | mutant K174N, T175P, A176N | ||||||||
1su5B | ASN 11;LYS 13;HIS 95;GLU 165 | mutant K174N, T175P, A176N | ||||||||
1suxA | ASN 12;LYS 14;HIS 96;GLU 168 | |||||||||
1suxB | ASN 12;LYS 14;HIS 96;GLU 168 | |||||||||
1sw0A | ASN 11;LYS 13;HIS 95;GLU 165 | mutant K174L, T175W | ||||||||
1sw0B | ASN 11;LYS 13;HIS 95;GLU 165 | mutant K174L, T175W | ||||||||
1sw3A | ASN 11;LYS 13;HIS 95;GLU 165 | mutant T175V | ||||||||
1sw3B | ASN 11;LYS 13;HIS 95;GLU 165 | mutant T175V | ||||||||
1sw7A | ASN 11;LYS 13;HIS 95;GLU 165 | mutant K174N, T175S, A176S | ||||||||
1sw7B | ASN 11;LYS 13;HIS 95;GLU 165 | mutant K174N, T175S, A176S | ||||||||
1tcdA | ASN 12;LYS 14;HIS 96;GLU 168 | |||||||||
1tcdB | ASN 12;LYS 14;HIS 96;GLU 168 | |||||||||
1timA | ASN 11;LYS 13;HIS 95;GLU 165 | |||||||||
1timB | ASN 11;LYS 13;HIS 95;GLU 165 | |||||||||
1tmhA | ASN 11;LYS 13;HIS 97;GLU 169 | mutant P227H, I229V, A232F, A241P, A243E, A245V, V246D, V248I, K249N, deletion D242 | ||||||||
1tmhB | ASN 11;LYS 13;HIS 97;GLU 169 | mutant P227H, I229V, A232F, A241P, A243E, A245V, V246D, V248I, K249N, deletion D242 | ||||||||
1tmhC | ASN 11;LYS 13;HIS 97;GLU 169 | mutant P227H, I229V, A232F, A241P, A243E, A245V, V246D, V248I, K249N, deletion D242 | ||||||||
1tmhD | ASN 11;LYS 13;HIS 97;GLU 169 | mutant P227H, I229V, A232F, A241P, A243E, A245V, V246D, V248I, K249N, deletion D242 | ||||||||
1tpb1 | ASN 11;LYS 13;HIS 95; | mutant E165D | ||||||||
1tpb2 | ASN 11;LYS 13;HIS 95; | mutant E165D | ||||||||
1tpc1 | ASN 11;LYS 13;HIS 95; | mutant S96P, E165D | ||||||||
1tpc2 | ASN 11;LYS 13;HIS 95; | mutant S96P, E165D | ||||||||
1tpdA | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1tpdB | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1tpeA | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1tpfA | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1tpfB | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1tph1 | ASN 11;LYS 13;HIS 95;GLU 165 | |||||||||
1tph2 | ASN 11;LYS 13;HIS 95;GLU 165 | |||||||||
1tpuA | ASN 11;LYS 13; ;GLU 165 | mutant H95N | ||||||||
1tpuB | ASN 11;LYS 13; ;GLU 165 | mutant H95N | ||||||||
1tpvA | ASN 11;LYS 13; ;GLU 165 | mutant H95N, S96P | ||||||||
1tpvB | ASN 11;LYS 13; ;GLU 165 | mutant H95N, S96P | ||||||||
1tpwA | ASN 11;LYS 13;HIS 95;GLU 165 | mutant S96P | ||||||||
1tpwB | ASN 11;LYS 13;HIS 95;GLU 165 | mutant S96P | ||||||||
1trdA | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1trdB | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1treA | ASN 11;LYS 13;HIS 97;GLU 169 | |||||||||
1treB | ASN 11;LYS 13;HIS 97;GLU 169 | |||||||||
1triA | ASN 11; ;HIS 95;GLU 167 | mutant 68-82 GNADALAS, invisible K13 | ||||||||
1tsiA | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1tsiB | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
1ttiA | ASN 11;LYS 13;HIS 95;GLU 167 | mutant I68G, A69N, K70A, S71D, P81A, A100W, deletion 73-79 | ||||||||
1ttjA | ASN 11; ;HIS 95;GLU 167 | mutant F45S, V46S, invisible K13 | ||||||||
1vgaA | ASN 10;LYS 12;HIS 95;GLU 165 | mutant W168F | ||||||||
1vgaB | ASN 10;LYS 12;HIS 95;GLU 165 | mutant W168F | ||||||||
1vgaC | ASN 10;LYS 12;HIS 95;GLU 165 | mutant W168F | ||||||||
1vgaD | ASN 10;LYS 12;HIS 95;GLU 165 | mutant W168F | ||||||||
1woaA | ASN 10;LYS 12;HIS 95;GLU 165 | mutant A163V, W168F | ||||||||
1woaB | ASN 10;LYS 12;HIS 95;GLU 165 | mutant A163V, W168F | ||||||||
1woaC | ASN 10;LYS 12;HIS 95;GLU 165 | mutant A163V, W168F | ||||||||
1woaD | ASN 10;LYS 12;HIS 95;GLU 165 | mutant A163V, W168F | ||||||||
1wobA | ASN 10;LYS 12;HIS 95;GLU 165 | mutant A163V, W168F | ||||||||
1wobB | ASN 10;LYS 12;HIS 95;GLU 165 | mutant A163V, W168F | ||||||||
1wobC | ASN 10;LYS 12;HIS 95;GLU 165 | mutant A163V, W168F | ||||||||
1wobD | ASN 10;LYS 12;HIS 95;GLU 165 | mutant A163V, W168F | ||||||||
1ydvA | ASN 10;LYS 12;HIS 95;GLU 165 | |||||||||
1ydvB | ASN 10;LYS 12;HIS 95;GLU 165 | |||||||||
1ypiA | ASN 10;LYS 12;HIS 95;GLU 165 | |||||||||
1ypiB | ASN 10;LYS 12;HIS 95;GLU 165 | |||||||||
2btmA | ASN 8;LYS 10;HIS 94;GLU 166 | |||||||||
2btmB | ASN 8;LYS 10;HIS 94;GLU 166 | |||||||||
2ypiA | ASN 10;LYS 12;HIS 95;GLU 165 | |||||||||
2ypiB | ASN 10;LYS 12;HIS 95;GLU 165 | |||||||||
3timA | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
3timB | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
3ypiA | ASN 10;LYS 12; ;GLU 165 | mutant H95Q | ||||||||
3ypiB | ASN 10;LYS 12; ;GLU 165 | mutant H95Q | ||||||||
4timA | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
4timB | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
5timA | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
5timB | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
6timA | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
6timB | ASN 11;LYS 13;HIS 95;GLU 167 | |||||||||
7timA | ASN 10;LYS 12;HIS 95;GLU 165 | |||||||||
7timB | ASN 10;LYS 12;HIS 95;GLU 165 | |||||||||
8timA | ASN 11;LYS 13;HIS 95;GLU 165 | |||||||||
8timB | ASN 11;LYS 13;HIS 95;GLU 165 |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[3]
|
Fig.1, p.159-161, p.168-170 | |
[4]
|
Fig.1, p.604, p.607-612 | |
[5]
|
p.120 | |
[7]
|
Fig.1 | |
[9]
|
Fig.1, Fig.4 | |
[10]
|
Scheme I, p.3187 | |
[11]
|
Fig.1, p.678 | |
[12]
|
Scheme I | |
[13]
|
Fig.1, Fig.2, Fig.4 | |
[14]
|
Scheme I, Scheme II, p.3016-3017 | |
[15]
|
Fig.1, Fig.2 | |
[21]
|
FIG.1 | |
[27]
|
Scheme I | |
[28]
|
Fig.3, p.241-243 | |
[29]
|
Fig.1 | |
[33]
|
Fig.1 | |
[34]
|
Fig.1 | |
[35]
|
Fig.1 | |
[40]
|
Fig.3, p.314 | |
[42]
|
Fig.2 | |
[43]
|
Fig.1 | |
[44]
|
||
[45]
|
Fig.1 | |
[50]
|
Fig.1 | |
[53]
|
Fig.1 | |
[54]
|
Fig.1 | |
[56]
|
Fig.1, p.232-234 | |
[58]
|
Scheme 1, Scheme 3, Fig.8 | |
[67]
|
Fig.1, p.4395-4396 | |
[69]
|
SCHEME 1 | |
[75]
|
Fig.1, p.5194 | |
[77]
|
Fig.1 | |
[86]
|
Scheme 1, Fig.1 | |
[87]
|
Scheme 1 | |
[89]
|
SCHEME I, SCHEME II, Fig.6 | |
[92]
|
FIG.1 | |
[93]
|
FIG.1, p.52468-52469 | |
[94]
|
Scheme 1, p.47 | |
[96]
|
Fig.1, Fig.3, p.52-54 | |
[98]
|
||
[101]
|
Fig.1, p.229-230 |
References | |
---|---|
[1] | |
Resource | |
Comments |
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), |
Medline ID | 75175220 |
PubMed ID | 1134550 |
Journal | Nature |
Year | 1975 |
Volume | 255 |
Pages | 609-14 |
Authors | Banner DW, Bloomer AC, Petsko GA, Phillips DC, Pogson CI, Wilson IA, Corran PH, Furth AJ, Milman JD, Offord RE, Priddle JD, Waley SG |
Title | Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 angstrom resolution using amino acid sequence data. |
Related PDB | |
Related UniProtKB | P00940 |
[2] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY. |
Medline ID | 77044751 |
PubMed ID | 985462 |
Journal | Biochem Biophys Res Commun |
Year | 1976 |
Volume | 72 |
Pages | 146-55 |
Authors | Banner DW, Bloomer A, Petsko GA, Phillips DC, Wilson IA |
Title | Atomic coordinates for triose phosphate isomerase from chicken muscle. |
Related PDB | 1tim |
Related UniProtKB | P00940 |
[3] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 6115415 |
Journal | Philos Trans R Soc Lond B Biol Sci |
Year | 1981 |
Volume | 293 |
Pages | 159-71 |
Authors | Alber T, Banner DW, Bloomer AC, Petsko GA, Phillips D, Rivers PS, Wilson IA |
Title | On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase. |
Related PDB | 1ml1 |
Related UniProtKB | |
[4] | |
Resource | |
Comments | REVIEW. |
Medline ID | 88295752 |
PubMed ID | 3331346 |
Journal | Cold Spring Harb Symp Quant Biol |
Year | 1987 |
Volume | 52 |
Pages | 603-13 |
Authors | Alber TC, Davenport RC Jr, Giammona DA, Lolis E, Petsko GA, Ringe D |
Title | Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme? |
Related PDB | |
Related UniProtKB | P00942 |
[5] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). |
Medline ID | 88118904 |
PubMed ID | 3430602 |
Journal | J Mol Biol |
Year | 1987 |
Volume | 198 |
Pages | 109-21 |
Authors | Wierenga RK, Kalk KH, Hol WG |
Title | Structure determination of the glycosomal triosephosphate isomerase from Trypanosoma brucei brucei at 2.4 A resolution. |
Related PDB | |
Related UniProtKB | P04789 |
[6] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2260979 |
Journal | Biochem Biophys Res Commun |
Year | 1990 |
Volume | 173 |
Pages | 736-40 |
Authors | Schnackerz KD, Kuan TK, Goux WJ, Gracy RW |
Title | Phosphorus-31 nuclear magnetic resonance spectroscopy reveals two conformational forms of chloroacetol phosphate-bound triosephosphate isomerase. |
Related PDB | |
Related UniProtKB | |
[7] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2361134 |
Journal | Biochemistry |
Year | 1990 |
Volume | 29 |
Pages | 4099-108 |
Authors | Blacklow SC, Knowles JR |
Title | How can a catalytic lesion be offset? The energetics of two pseudorevertant triosephosphate isomerases. |
Related PDB | |
Related UniProtKB | |
[8] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). |
Medline ID | 90373768 |
PubMed ID | 2204417 |
Journal | Biochemistry |
Year | 1990 |
Volume | 29 |
Pages | 6609-18 |
Authors | Lolis E, Alber T, Davenport RC, Rose D, Hartman FC, Petsko GA |
Title | Structure of yeast triosephosphate isomerase at 1.9-A resolution. |
Related PDB | 1ypi |
Related UniProtKB | P00942 |
[9] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH 2-P-GLYCOLATE. |
Medline ID | 90373769 |
PubMed ID | 2204418 |
Journal | Biochemistry |
Year | 1990 |
Volume | 29 |
Pages | 6619-25 |
Authors | Lolis E, Petsko GA |
Title | Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis. |
Related PDB | 2ypi |
Related UniProtKB | P00942 |
[10] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2185832 |
Journal | Biochemistry |
Year | 1990 |
Volume | 29 |
Pages | 3186-94 |
Authors | Pompliano DL, Peyman A, Knowles JR |
Title | Stabilization of a reaction intermediate as a catalytic device: definition of the functional role of the flexible loop in triosephosphate isomerase. |
Related PDB | |
Related UniProtKB | |
[11] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2217142 |
Journal | Protein Eng |
Year | 1990 |
Volume | 3 |
Pages | 677-90 |
Authors | Daggett V, Kollman PA |
Title | Molecular dynamics simulations of active site mutants of triosephosphate isomerase. |
Related PDB | |
Related UniProtKB | |
[12] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1883832 |
Journal | Biochemistry |
Year | 1991 |
Volume | 30 |
Pages | 8470-6 |
Authors | Blacklow SC, Liu KD, Knowles JR |
Title | Stepwise improvements in catalytic effectiveness: independence and interdependence in combinations of point mutations of a sluggish triosephosphate isomerase. |
Related PDB | |
Related UniProtKB | |
[13] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 2043623 |
Journal | Biochemistry |
Year | 1991 |
Volume | 30 |
Pages | 5821-6 |
Authors | Davenport RC, Bash PA, Seaton BA, Karplus M, Petsko GA, Ringe D |
Title | Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway. |
Related PDB | 7tim |
Related UniProtKB | |
[14] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 2007138 |
Journal | Biochemistry |
Year | 1991 |
Volume | 30 |
Pages | 3011-9 |
Authors | Komives EA, Chang LC, Lolis E, Tilton RF, Petsko GA, Knowles JR |
Title | Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95. |
Related PDB | 3ypi |
Related UniProtKB | |
[15] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2069953 |
Journal | Biochemistry |
Year | 1991 |
Volume | 30 |
Pages | 6948-56 |
Authors | Lodi PJ, Knowles JR |
Title | Neutral imidazole is the electrophile in the reaction catalyzed by triosephosphate isomerase: structural origins and catalytic implications. |
Related PDB | |
Related UniProtKB | |
[16] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1814699 |
Journal | Ciba Found Symp |
Year | 1991 |
Volume | 161 |
Pages | 91-103; discussion 103-7 |
Authors | Kollman PA, Daggett V, Dang LX |
Title | The application of computational methods to the study of enzyme catalysis by triose-phosphate isomerase and stabilities of variants of bacteriophage T4 lysozyme. |
Related PDB | |
Related UniProtKB | |
[17] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2065677 |
Journal | Eur J Biochem |
Year | 1991 |
Volume | 199 |
Pages | 231-8 |
Authors | Schnackerz KD, Gracy RW |
Title | Probing the catalytic sites of triosephosphate isomerase by 31P-NMR with reversibly and irreversibly binding substrate analogues. |
Related PDB | |
Related UniProtKB | |
[18] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 2040290 |
Journal | Eur J Biochem |
Year | 1991 |
Volume | 198 |
Pages | 53-7 |
Authors | Verlinde CL, Noble ME, Kalk KH, Groendijk H, Wierenga RK, Hol WG |
Title |
Anion binding at the active site of trypanosomal triosephosphate isomerase. |
Related PDB | 1ag1 |
Related UniProtKB | |
[19] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 1895291 |
Journal | J Med Chem |
Year | 1991 |
Volume | 34 |
Pages | 2709-18 |
Authors | Noble ME, Verlinde CL, Groendijk H, Kalk KH, Wierenga RK, Hol WG |
Title | Crystallographic and molecular modeling studies on trypanosomal triosephosphate isomerase: a critical assessment of the predicted and observed structures of the complex with 2-phosphoglycerate. |
Related PDB | 4tim |
Related UniProtKB | |
[20] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS). |
Medline ID | 91350193 |
PubMed ID | 1880808 |
Journal | J Mol Biol |
Year | 1991 |
Volume | 220 |
Pages | 995-1015 |
Authors | Wierenga RK, Noble ME, Vriend G, Nauche S, Hol WG |
Title |
Refined 1.83 A structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate. |
Related PDB | 5tim |
Related UniProtKB | P04789 |
[21] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2005961 |
Journal | Nature |
Year | 1991 |
Volume | 350 |
Pages | 121-4 |
Authors | Knowles JR |
Title |
Enzyme catalysis: not different, |
Related PDB | |
Related UniProtKB | |
[22] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 2062828 |
Journal | Proteins |
Year | 1991 |
Volume | 10 |
Pages | 50-69 |
Authors | Noble ME, Wierenga RK, Lambeir AM, Opperdoes FR, Thunnissen AM, Kalk KH, Groendijk H, Hol WG |
Title | The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes. |
Related PDB | 6tim 1iig 1iih |
Related UniProtKB | |
[23] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH 2-P-GLYCOLATE. |
Medline ID | |
PubMed ID | 2062827 |
Journal | Proteins |
Year | 1991 |
Volume | 10 |
Pages | 33-49 |
Authors | Wierenga RK, Noble ME, Postma JP, Groendijk H, Kalk KH, Hol WG, Opperdoes FR |
Title | The crystal structure of the "open" and the "closed" conformation of the flexible loop of trypanosomal triosephosphate isomerase. |
Related PDB | 3tim |
Related UniProtKB | |
[24] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1536574 |
Journal | Arch Biochem Biophys |
Year | 1992 |
Volume | 293 |
Pages | 382-90 |
Authors | Sun AQ, Yuksel KU, Gracy RW |
Title | Relationship between the catalytic center and the primary degradation site of triosephosphate isomerase: effects of active site modification and deamidation. |
Related PDB | |
Related UniProtKB | |
[25] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1586170 |
Journal | Arch Biochem Biophys |
Year | 1992 |
Volume | 295 |
Pages | 421-8 |
Authors | Sun AQ, Yuksel KU, Rao GS, Gracy RW |
Title | Effects of active site modification and reversible dissociation on the secondary structure of triosephosphate isomerase. |
Related PDB | |
Related UniProtKB | |
[26] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1390633 |
Journal | Biochemistry |
Year | 1992 |
Volume | 31 |
Pages | 8488-94 |
Authors | Sampson NS, Knowles JR |
Title | Segmental motion in catalysis: investigation of a hydrogen bond critical for loop closure in the reaction of triosephosphate isomerase. |
Related PDB | |
Related UniProtKB | |
[27] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1390632 |
Journal | Biochemistry |
Year | 1992 |
Volume | 31 |
Pages | 8482-7 |
Authors | Sampson NS, Knowles JR |
Title | Segmental movement: definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase. |
Related PDB | |
Related UniProtKB | |
[28] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1290934 |
Journal | Faraday Discuss |
Year | 1992 |
Volume | (93) |
Pages | 239-48 |
Authors | Karplus M, Evanseck JD, Joseph D, Bash PA, Field MJ |
Title | Simulation analysis of triose phosphate isomerase: conformational transition and catalysis. |
Related PDB | |
Related UniProtKB | |
[29] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1628747 |
Journal | FEBS Lett |
Year | 1992 |
Volume | 306 |
Pages | 80-4 |
Authors | Hennig M, Schlesier B, Dauter Z, Pfeffer S, Betzel C, Hohne WE, Wilson KS |
Title | A TIM barrel protein without enzymatic activity? Crystal-structure of narbonin at 1.8 A resolution. |
Related PDB | |
Related UniProtKB | |
[30] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1639191 |
Journal | FEBS Lett |
Year | 1992 |
Volume | 307 |
Pages | 34-9 |
Authors | Wierenga RK, Borchert TV, Noble ME |
Title | Crystallographic binding studies with triosephosphate isomerases: conformational changes induced by substrate and substrate-analogues. |
Related PDB | |
Related UniProtKB | |
[31] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1400336 |
Journal | J Biol Chem |
Year | 1992 |
Volume | 267 |
Pages | 20168-74 |
Authors | Sun AQ, Yuksel KU, Gracy RW |
Title |
Interactions between the catalytic centers and subunit interface of triosephosphate isomerase probed by refolding, |
Related PDB | |
Related UniProtKB | |
[32] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY. |
Medline ID | 92235847 |
PubMed ID | 1569570 |
Journal | J Mol Biol |
Year | 1992 |
Volume | 224 |
Pages | 1115-26 |
Authors | Wierenga RK, Noble ME, Davenport RC |
Title |
Comparison of the refined crystal structures of liganded and unliganded chicken, |
Related PDB | |
Related UniProtKB | P00940 P00942 P04789 |
[33] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 1304889 |
Journal | Protein Sci |
Year | 1992 |
Volume | 1 |
Pages | 1578-84 |
Authors | Verlinde CL, Witmans CJ, Pijning T, Kalk KH, Hol WG, Callens M, Opperdoes FR |
Title | Structure of the complex between trypanosomal triosephosphate isomerase and N-hydroxy-4-phosphono-butanamide: binding at the active site despite an "open" flexible loop conformation. |
Related PDB | 1tsi |
Related UniProtKB | |
[34] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). |
Medline ID | |
PubMed ID | 15299515 |
Journal | Acta Crystallogr D Biol Crystallogr |
Year | 1993 |
Volume | 49(Pt 4) |
Pages | 403-17 |
Authors | Noble ME.M, Zeelen JP, Wierenga RK, Mainfroid V, Goraj K, Gohimont A-C, Martial JA |
Title | Structure of triosephosphate isomerase from Escherichia coli determined at 2.6 A resolution. |
Related PDB | 1tre |
Related UniProtKB | P0A858 |
[35] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8476863 |
Journal | Biochemistry |
Year | 1993 |
Volume | 32 |
Pages | 4338-43 |
Authors | Lodi PJ, Knowles JR |
Title | Direct evidence for the exploitation of an alpha-helix in the catalytic mechanism of triosephosphate isomerase. |
Related PDB | |
Related UniProtKB | |
[36] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8431552 |
Journal | Biophys J |
Year | 1993 |
Volume | 64 |
Pages | 9-15 |
Authors | Wade RC, Davis ME, Luty BA, Madura JD, McCammon JA |
Title | Gating of the active site of triose phosphate isomerase: Brownian dynamics simulations of flexible peptide loops in the enzyme. |
Related PDB | |
Related UniProtKB | |
[37] | |
Resource | |
Comments |
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), |
Medline ID | 93170303 |
PubMed ID | 8436128 |
Journal | Eur J Biochem |
Year | 1993 |
Volume | 211 |
Pages | 703-10 |
Authors | Borchert TV, Pratt K, Zeelen JP, Callens M, Noble ME, Opperdoes FR, Michels PA, Wierenga RK |
Title | Overexpression of trypanosomal triosephosphate isomerase in Escherichia coli and characterisation of a dimer-interface mutant. |
Related PDB | |
Related UniProtKB | P04789 |
[38] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8262920 |
Journal | J Biol Chem |
Year | 1993 |
Volume | 268 |
Pages | 26872-8 |
Authors | Sun AQ, Yuksel KU, Gracy RW |
Title | Limited proteolysis of triose-phosphate isomerase and characterization of the catalytically active peptide complex. |
Related PDB | |
Related UniProtKB | |
[39] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). |
Medline ID | 94143343 |
PubMed ID | 8309937 |
Journal | Protein Eng |
Year | 1993 |
Volume | 6 |
Pages | 893-900 |
Authors | Mainfroid V, Goraj K, Rentier-Delrue F, Houbrechts A, Loiseau A, Gohimont AC, Noble ME, Borchert TV, Wierenga RK, Martial JA |
Title | Replacing the (beta alpha)-unit 8 of E.coli TIM with its chicken homologue leads to a stable and active hybrid enzyme. |
Related PDB | |
Related UniProtKB | P0A858 |
[40] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 8356028 |
Journal | Proteins |
Year | 1993 |
Volume | 16 |
Pages | 311-26 |
Authors | Noble ME, Zeelen JP, Wierenga RK |
Title |
Structures of the "open" and "closed" state of trypanosomal triosephosphate isomerase, |
Related PDB | 1tpd 1trd |
Related UniProtKB | |
[41] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8204630 |
Journal | Biochemistry |
Year | 1994 |
Volume | 33 |
Pages | 6960-5 |
Authors | Garza-Ramos G, Tuena de Gomez-Puyou M, Gomez-Puyou A, Yuksel KU, Gracy RW |
Title | Deamidation of triosephosphate isomerase in reverse micelles: effects of water on catalysis and molecular wear and tear. |
Related PDB | |
Related UniProtKB | |
[42] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8130194 |
Journal | Biochemistry |
Year | 1994 |
Volume | 33 |
Pages | 2815-23 |
Authors | Joseph-McCarthy D, Lolis E, Komives EA, Petsko GA |
Title | Crystal structure of the K12M/G15A triosephosphate isomerase double mutant and electrostatic analysis of the active site. |
Related PDB | |
Related UniProtKB | |
[43] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 7907502 |
Journal | Biochemistry |
Year | 1994 |
Volume | 33 |
Pages | 2824-9 |
Authors | Joseph-McCarthy D, Rost LE, Komives EA, Petsko GA |
Title | Crystal structure of the mutant yeast triosephosphate isomerase in which the catalytic base glutamic acid 165 is changed to aspartic acid. |
Related PDB | |
Related UniProtKB | |
[44] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8130193 |
Journal | Biochemistry |
Year | 1994 |
Volume | 33 |
Pages | 2809-14 |
Authors | Lodi PJ, Chang LC, Knowles JR, Komives EA |
Title | Triosephosphate isomerase requires a positively charged active site: the role of lysine-12. |
Related PDB | |
Related UniProtKB | |
[45] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). |
Medline ID | 94176473 |
PubMed ID | 8130195 |
Journal | Biochemistry |
Year | 1994 |
Volume | 33 |
Pages | 2830-7 |
Authors | Zhang Z, Sugio S, Komives EA, Liu KD, Knowles JR, Petsko GA, Ringe D |
Title | Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution. |
Related PDB | 1tph |
Related UniProtKB | P00940 |
[46] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 7906272 |
Journal | J Biol Chem |
Year | 1994 |
Volume | 269 |
Pages | 5005-8 |
Authors | Yuksel KU, Sun AQ, Gracy RW, Schnackerz KD |
Title |
The hinged lid of yeast triose-phosphate isomerase. |
Related PDB | |
Related UniProtKB | |
[47] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 7809033 |
Journal | Protein Eng |
Year | 1994 |
Volume | 7 |
Pages | 945-51 |
Authors | Kishan R, Zeelen JP, Noble ME, Borchert TV, Mainfroid V, Goraj K, Martial JA, Wierenga RK |
Title |
Modular mutagenesis of a TIM-barrel enzyme: the crystal structure of a chimeric E. |
Related PDB | 1tmh |
Related UniProtKB | |
[48] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 8061607 |
Journal | Protein Sci |
Year | 1994 |
Volume | 3 |
Pages | 779-87 |
Authors | Kishan KV, Zeelen JP, Noble ME, Borchert TV, Wierenga RK |
Title | Comparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms. |
Related PDB | 1tpe 1tpf |
Related UniProtKB | |
[49] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). |
Medline ID | 94339841 |
PubMed ID | 8061610 |
Journal | Protein Sci |
Year | 1994 |
Volume | 3 |
Pages | 810-21 |
Authors | Mande SC, Mainfroid V, Kalk KH, Goraj K, Martial JA, Hol WG |
Title |
Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. |
Related PDB | 1hti |
Related UniProtKB | P60174 |
[50] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 7577950 |
Journal | Biochemistry |
Year | 1995 |
Volume | 34 |
Pages | 13612-21 |
Authors | Komives EA, Lougheed JC, Liu K, Sugio S, Zhang Z, Petsko GA, Ringe D |
Title | The structural basis for pseudoreversion of the E165D lesion by the secondary S96P mutation in triosephosphate isomerase depends on the positions of active site water molecules. |
Related PDB | 1tpb 1tpc |
Related UniProtKB | |
[51] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). |
Medline ID | 96164392 |
PubMed ID | 8580851 |
Journal | Protein Sci |
Year | 1995 |
Volume | 4 |
Pages | 2594-604 |
Authors | Delboni LF, Mande SC, Rentier-Delrue F, Mainfroid V, Turley S, Vellieux FM, Martial JA, Hol WG |
Title |
Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. |
Related PDB | 1btm |
Related UniProtKB | P00943 |
[52] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANTS. |
Medline ID | 96000857 |
PubMed ID | 8591044 |
Journal | Structure |
Year | 1995 |
Volume | 3 |
Pages | 669-79 |
Authors | Borchert TV, Kishan KV, Zeelen JP, Schliebs W, Thanki N, Abagyan R, Jaenicke R, Wierenga RK |
Title |
Three new crystal structures of point mutation variants of monoTIM: conformational flexibility of loop-1, |
Related PDB | 1tri 1tti 1ttj |
Related UniProtKB | P04789 |
[53] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 8952501 |
Journal | Biochemistry |
Year | 1996 |
Volume | 35 |
Pages | 15474-84 |
Authors | Komives EA, Lougheed JC, Zhang Z, Sugio S, Narayana N, Xuong NH, Petsko GA, Ringe D |
Title | The structural basis for pseudoreversion of the H95N lesion by the secondary S96P mutation in triosephosphate isomerase. |
Related PDB | 1tpu 1tpv |
Related UniProtKB | |
[54] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8626554 |
Journal | J Biol Chem |
Year | 1996 |
Volume | 271 |
Pages | 10010-6 |
Authors | Aqvist J, Fothergill M |
Title | Computer simulation of the triosephosphate isomerase catalyzed reaction. |
Related PDB | |
Related UniProtKB | |
[55] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8745400 |
Journal | Protein Sci |
Year | 1996 |
Volume | 5 |
Pages | 229-39 |
Authors | Schliebs W, Thanki N, Eritja R, Wierenga R |
Title | Active site properties of monomeric triosephosphate isomerase (monoTIM) as deduced from mutational and structural studies. |
Related PDB | |
Related UniProtKB | |
[56] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8811738 |
Journal | Proteins |
Year | 1996 |
Volume | 25 |
Pages | 225-36 |
Authors | Perakyla M, Pakkanen TA |
Title |
Ab initio models for receptor-ligand interactions in proteins. |
Related PDB | |
Related UniProtKB | |
[57] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9126273 |
Journal | Arch Biochem Biophys |
Year | 1997 |
Volume | 340 |
Pages | 27-35 |
Authors | Talent JM, Zvaigzne AI, Agrawal N, Gracy RW |
Title | Effect of active-site modification on the terminal marking deamidation of triosephosphate isomerase. |
Related PDB | |
Related UniProtKB | |
[58] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9398185 |
Journal | Biochemistry |
Year | 1997 |
Volume | 36 |
Pages | 14661-75 |
Authors | Harris TK, Abeygunawardana C, Mildvan AS |
Title | NMR studies of the role of hydrogen bonding in the mechanism of triosephosphate isomerase. |
Related PDB | |
Related UniProtKB | |
[59] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9245397 |
Journal | Biochemistry |
Year | 1997 |
Volume | 36 |
Pages | 9655-62 |
Authors | Schliebs W, Thanki N, Jaenicke R, Wierenga RK |
Title | A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability. |
Related PDB | |
Related UniProtKB | |
[60] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9089815 |
Journal | Protein Eng |
Year | 1997 |
Volume | 10 |
Pages | 159-67 |
Authors | Thanki N, Zeelen JP, Mathieu M, Jaenicke R, Abagyan RA, Wierenga RK, Schliebs W |
Title | Protein engineering with monomeric triosephosphate isomerase (monoTIM): the modelling and structure verification of a seven-residue loop. |
Related PDB | |
Related UniProtKB | |
[61] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9144796 |
Journal | Proteins |
Year | 1997 |
Volume | 28 |
Pages | 109-16 |
Authors | Kobayashi N, Yamato T, Go N |
Title | Mechanical property of a TIM-barrel protein. |
Related PDB | |
Related UniProtKB | |
[62] | |
Resource | |
Comments |
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF PGK, |
Medline ID | 98046096 |
PubMed ID | 9384563 |
Journal | Structure |
Year | 1997 |
Volume | 5 |
Pages | 1475-83 |
Authors | Auerbach G, Huber R, Grattinger M, Zaiss K, Schurig H, Jaenicke R, Jacob U |
Title | Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability. |
Related PDB | |
Related UniProtKB | P36204 |
[63] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). |
Medline ID | 97410385 |
PubMed ID | 9261072 |
Journal | Structure |
Year | 1997 |
Volume | 5 |
Pages | 751-61 |
Authors | Velanker SS, Ray SS, Gokhale RS, Suma S, Balaram H, Balaram P, Murthy MR |
Title | Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design. |
Related PDB | 1ydv |
Related UniProtKB | Q07412 |
[64] | |
Resource | |
Comments |
NUCLEOTIDE SEQUENCE, |
Medline ID | |
PubMed ID | 9442062 |
Journal | J Biol Chem |
Year | 1998 |
Volume | 273 |
Pages | 2199-206 |
Authors | Alvarez M, Zeelen JP, Mainfroid V, Rentier-Delrue F, Martial JA, Wyns L, Wierenga RK, Maes D |
Title |
Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. |
Related PDB | 1aw1 1aw2 |
Related UniProtKB | P50921 |
[65] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS). |
Medline ID | 98437380 |
PubMed ID | 9761683 |
Journal | J Mol Biol |
Year | 1998 |
Volume | 283 |
Pages | 193-203 |
Authors | Maldonado E, Soriano-Garcia M, Moreno A, Cabrera N, Garza-Ramos G, de Gomez-Puyou M, Gomez-Puyou A, Perez-Montfort R |
Title | Differences in the intersubunit contacts in triosephosphate isomerase from two closely related pathogenic trypanosomes. |
Related PDB | 1tcd |
Related UniProtKB | P52270 |
[66] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10194326 |
Journal | Biochemistry |
Year | 1999 |
Volume | 38 |
Pages | 4114-20 |
Authors | Perez-Montfort R, Garza-Ramos G, Alcantara GH, Reyes-Vivas H, Gao XG, Maldonado E, de Gomez-Puyou MT, Gomez-Puyou A |
Title | Derivatization of the interface cysteine of triosephosphate isomerase from Trypanosoma brucei and Trypanosoma cruzi as probe of the interrelationship between the catalytic sites and the dimer interface. |
Related PDB | |
Related UniProtKB | |
[67] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10194358 |
Journal | Biochemistry |
Year | 1999 |
Volume | 38 |
Pages | 4389-97 |
Authors | Zhang Z, Komives EA, Sugio S, Blacklow SC, Narayana N, Xuong NH, Stock AM, Petsko GA, Ringe D |
Title | The role of water in the catalytic efficiency of triosephosphate isomerase. |
Related PDB | |
Related UniProtKB | |
[68] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). |
Medline ID | 99315861 |
PubMed ID | 10383424 |
Journal | J Biol Chem |
Year | 1999 |
Volume | 274 |
Pages | 19181-7 |
Authors | Alvarez M, Wouters J, Maes D, Mainfroid V, Rentier-Delrue F, Wyns L, Depiereux E, Martial JA |
Title | Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperatures. |
Related PDB | 2btm |
Related UniProtKB | P00943 |
[69] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10507008 |
Journal | Methods Enzymol |
Year | 1999 |
Volume | 308 |
Pages | 246-76 |
Authors | Shan SO, Herschlag D |
Title | Hydrogen bonding in enzymatic catalysis: analysis of energetic contributions. |
Related PDB | |
Related UniProtKB | |
[70] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). |
Medline ID | 99398662 |
PubMed ID | 10468562 |
Journal | Proc Natl Acad Sci U S A |
Year | 1999 |
Volume | 96 |
Pages | 10062-7 |
Authors | Gao XG, Maldonado E, Perez-Montfort R, Garza-Ramos G, de Gomez-Puyou MT, Gomez-Puyou A, Rodriguez-Romero A |
Title | Crystal structure of triosephosphate isomerase from Trypanosoma cruzi in hexane. |
Related PDB | 1ci1 |
Related UniProtKB | P52270 |
[71] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS). |
Medline ID | 99249704 |
PubMed ID | 10235625 |
Journal | Protein Eng |
Year | 1999 |
Volume | 12 |
Pages | 243-50 |
Authors | Williams JC, Zeelen JP, Neubauer G, Vriend G, Backmann J, Michels PA, Lambeir AM, Wierenga RK |
Title | Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power. |
Related PDB | 1amk |
Related UniProtKB | P48499 |
[72] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF TIM. |
Medline ID | 20058648 |
PubMed ID | 10591103 |
Journal | Proteins |
Year | 1999 |
Volume | 37 |
Pages | 441-53 |
Authors | Maes D, Zeelen JP, Thanki N, Beaucamp N, Alvarez M, Thi MH, Backmann J, Martial JA, Wyns L, Jaenicke R, Wierenga RK |
Title | The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures. |
Related PDB | 1b9b |
Related UniProtKB | P36204 |
[73] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10957646 |
Journal | Acta Crystallogr D Biol Crystallogr |
Year | 2000 |
Volume | 56 |
Pages | 1201-3 |
Authors | Wouters J, Maes D |
Title | Identification of a potential metal cation-pi binding site in the structure of a thermophilic Bacillus stearothermophilus triosephosphate isomerase mutant. |
Related PDB | |
Related UniProtKB | |
[74] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 10785370 |
Journal | Eur J Biochem |
Year | 2000 |
Volume | 267 |
Pages | 2516-24 |
Authors | Lambeir AM, Backmann J, Ruiz-Sanz J, Filimonov V, Nielsen JE, Kursula I, Norledge BV, Wierenga RK |
Title | The ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triose phosphate isomerase. |
Related PDB | 1qds |
Related UniProtKB | |
[75] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 11589711 |
Journal | Eur J Biochem |
Year | 2001 |
Volume | 268 |
Pages | 5189-96 |
Authors | Kursula I, Partanen S, Lambeir AM, Antonov DM, Augustyns K, Wierenga RK |
Title | Structural determinants for ligand binding and catalysis of triosephosphate isomerase. |
Related PDB | 1if2 |
Related UniProtKB | |
[76] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 11419952 |
Journal | J Mol Biol |
Year | 2001 |
Volume | 310 |
Pages | 271-80 |
Authors | Rozovsky S, Jogl G, Tong L, McDermott AE |
Title | Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics. |
Related PDB | 1i45 |
Related UniProtKB | |
[77] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11419951 |
Journal | J Mol Biol |
Year | 2001 |
Volume | 310 |
Pages | 259-70 |
Authors | Rozovsky S, McDermott AE |
Title | The time scale of the catalytic loop motion in triosephosphate isomerase. |
Related PDB | |
Related UniProtKB | |
[78] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 11243785 |
Journal | J Mol Biol |
Year | 2001 |
Volume | 306 |
Pages | 745-57 |
Authors | Walden H, Bell GS, Russell RJ, Siebers B, Hensel R, Taylor GL |
Title |
Tiny TIM: a small, |
Related PDB | 1hg3 |
Related UniProtKB | P62003 |
[79] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11286559 |
Journal | J Mol Biol |
Year | 2001 |
Volume | 307 |
Pages | 1103-12 |
Authors | Xiang J, Sun J, Sampson NS |
Title | The importance of hinge sequence for loop function and catalytic activity in the reaction catalyzed by triosephosphate isomerase. |
Related PDB | |
Related UniProtKB | |
[80] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11342710 |
Journal | Protein Eng |
Year | 2001 |
Volume | 14 |
Pages | 149-55 |
Authors | Saab-Rincon G, Juarez VR, Osuna J, Sanchez F, Soberon X |
Title | Different strategies to recover the activity of monomeric triosephosphate isomerase by directed evolution. |
Related PDB | |
Related UniProtKB | |
[81] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 11151009 |
Journal | Proteins |
Year | 2001 |
Volume | 42 |
Pages | 383-9 |
Authors | Norledge BV, Lambeir AM, Abagyan RA, Rottmann A, Fernandez AM, Filimonov VV, Peter MG, Wierenga RK |
Title |
Modeling, |
Related PDB | 1dkw |
Related UniProtKB | |
[82] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 12454456 |
Journal | Acta Crystallogr D Biol Crystallogr |
Year | 2002 |
Volume | 58 |
Pages | 1992-2000 |
Authors | Parthasarathy S, Balaram H, Balaram P, Murthy MR |
Title | Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: observation of the catalytic loop in the open conformation in the ligand-bound state. |
Related PDB | 1m7o 1m7p |
Related UniProtKB | |
[83] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11914068 |
Journal | Biochemistry |
Year | 2002 |
Volume | 41 |
Pages | 4230-8 |
Authors | Hernandez-Alcantara G, Garza-Ramos G, Hernandez GM, Gomez-Puyou A, Perez-Montfort R |
Title |
Catalysis and stability of triosephosphate isomerase from Trypanosoma brucei with different residues at position 14 of the dimer interface. |
Related PDB | |
Related UniProtKB | |
[84] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 12403619 |
Journal | Biochemistry |
Year | 2002 |
Volume | 41 |
Pages | 13178-88 |
Authors | Parthasarathy S, Ravindra G, Balaram H, Balaram P, Murthy MR |
Title | Structure of the Plasmodium falciparum triosephosphate isomerase-phosphoglycolate complex in two crystal forms: characterization of catalytic loop open and closed conformations in the ligand-bound state. |
Related PDB | 1lyx 1lzo |
Related UniProtKB | |
[85] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 11997014 |
Journal | FEBS Lett |
Year | 2002 |
Volume | 518 |
Pages | 39-42 |
Authors | Kursula I, Partanen S, Lambeir AM, Wierenga RK |
Title |
The importance of the conserved Arg191-Asp227 salt bridge of triosephosphate isomerase for folding, |
Related PDB | 1kv5 |
Related UniProtKB | |
[86] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11902900 |
Journal | J Am Chem Soc |
Year | 2002 |
Volume | 124 |
Pages | 3093-124 |
Authors | Cui Q, Karplus M |
Title | Quantum mechanics/molecular mechanics studies of triosephosphate isomerase-catalyzed reactions: effect of geometry and tunneling on proton-transfer rate constants. |
Related PDB | |
Related UniProtKB | |
[87] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12475328 |
Journal | J Am Chem Soc |
Year | 2002 |
Volume | 124 |
Pages | 14871-8 |
Authors | Zhang X, Harrison DH, Cui Q |
Title | Functional specificities of methylglyoxal synthase and triosephosphate isomerase: a combined QM/MM analysis. |
Related PDB | |
Related UniProtKB | |
[88] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12185208 |
Journal | J Biol Chem |
Year | 2002 |
Volume | 277 |
Pages | 30968-75 |
Authors | Silverman JA, Harbury PB |
Title |
Rapid mapping of protein structure, |
Related PDB | |
Related UniProtKB | |
[89] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 14631822 |
Journal | Adv Protein Chem |
Year | 2003 |
Volume | 66 |
Pages | 315-72 |
Authors | Cui Q, Karplus M |
Title | Catalysis and specificity in enzymes: a study of triosephosphate isomerase and comparison with methyl glyoxal synthase. |
Related PDB | |
Related UniProtKB | |
[90] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12472469 |
Journal | Biochem J |
Year | 2003 |
Volume | 370 |
Pages | 785-92 |
Authors | Najera H, Costas M, Fernandez-Velasco DA |
Title | Thermodynamic characterization of yeast triosephosphate isomerase refolding: insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme. |
Related PDB | |
Related UniProtKB | |
[91] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12627960 |
Journal | Biochemistry |
Year | 2003 |
Volume | 42 |
Pages | 2941-51 |
Authors | Desamero R, Rozovsky S, Zhadin N, McDermott A, Callender R |
Title | Active site loop motion in triosephosphate isomerase: T-jump relaxation spectroscopy of thermal activation. |
Related PDB | |
Related UniProtKB | |
[92] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 12522213 |
Journal | J Biol Chem |
Year | 2003 |
Volume | 278 |
Pages | 9544-51 |
Authors | Kursula I, Wierenga RK |
Title | Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution. |
Related PDB | 1n55 |
Related UniProtKB | |
[93] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 14563846 |
Journal | J Biol Chem |
Year | 2003 |
Volume | 278 |
Pages | 52461-70 |
Authors | Parthasarathy S, Eaazhisai K, Balaram H, Balaram P, Murthy MR |
Title | Structure of Plasmodium falciparum triose-phosphate isomerase-2-phosphoglycerate complex at 1.1-A resolution. |
Related PDB | 1o5x |
Related UniProtKB | |
[94] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12483674 |
Journal | J Comput Chem |
Year | 2003 |
Volume | 24 |
Pages | 46-56 |
Authors | Alagona G, Ghio C, Kollman PA |
Title | The intramolecular mechanism for the second proton transfer in triosephosphate isomerase (TIM): a QM/FE approach. |
Related PDB | |
Related UniProtKB | |
[95] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 14643664 |
Journal | J Mol Biol |
Year | 2003 |
Volume | 334 |
Pages | 1023-41 |
Authors | Aparicio R, Ferreira ST, Polikarpov I |
Title | Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity. |
Related PDB | |
Related UniProtKB | |
[96] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 12509510 |
Journal | Proc Natl Acad Sci U S A |
Year | 2003 |
Volume | 100 |
Pages | 50-5 |
Authors | Jogl G, Rozovsky S, McDermott AE, Tong L |
Title | Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution. |
Related PDB | 1ney 1nf0 |
Related UniProtKB | |
[97] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15023076 |
Journal | Biochemistry |
Year | 2004 |
Volume | 43 |
Pages | 3255-63 |
Authors | Gonzalez-Mondragon E, Zubillaga RA, Saavedra E, Chanez-Cardenas ME, Perez-Montfort R, Hernandez-Arana A |
Title | Conserved cysteine 126 in triosephosphate isomerase is required not for enzymatic activity but for proper folding and stability. |
Related PDB | |
Related UniProtKB | |
[98] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15350130 |
Journal | Biochemistry |
Year | 2004 |
Volume | 43 |
Pages | 11436-45 |
Authors | Xiang J, Jung JY, Sampson NS |
Title | Entropy effects on protein hinges: the reaction catalyzed by triosephosphate isomerase. |
Related PDB | |
Related UniProtKB | |
[99] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15324804 |
Journal | Chem Biol |
Year | 2004 |
Volume | 11 |
Pages | 1037-42 |
Authors | Tousignant A, Pelletier JN |
Title | Protein motions promote catalysis. |
Related PDB | |
Related UniProtKB | |
[100] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 15465054 |
Journal | J Mol Biol |
Year | 2004 |
Volume | 343 |
Pages | 671-84 |
Authors | Eaazhisai K, Balaram H, Balaram P, Murthy MR |
Title |
Structures of unliganded and inhibitor complexes of W168F, |
Related PDB | 1vga 1woa 1wob |
Related UniProtKB | |
[101] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15001364 |
Journal | J Mol Biol |
Year | 2004 |
Volume | 337 |
Pages | 227-39 |
Authors | Guallar V, Jacobson M, McDermott A, Friesner RA |
Title | Computational modeling of the catalytic reaction in triosephosphate isomerase. |
Related PDB | |
Related UniProtKB | |
[102] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 15321726 |
Journal | J Mol Biol |
Year | 2004 |
Volume | 341 |
Pages | 1355-1365 |
Authors | Tellez-Valencia A, Olivares-Illana V, Hernandez-Santoyo A, Perez-Montfort R, Costas M, Rodriguez-Romero A, Lopez-Calahorra F, Tuena de Gomez-Puyou M, Gomez-Puyou A |
Title | Inactivation of triosephosphate isomerase from Trypanosoma cruzi by an agent that perturbs its dimer interface |
Related PDB | 1sux |
Related UniProtKB | |
[103] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 15166315 |
Journal | Protein Eng Des Sel |
Year | 2004 |
Volume | 17 |
Pages | 375-82 |
Authors | Kursula I, Salin M, Sun J, Norledge BV, Haapalainen AM, Sampson NS, Wierenga RK |
Title | Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase. |
Related PDB | 1spq 1sq7 1ssd 1ssg 1su5 1sw0 1sw3 1sw7 |
Related UniProtKB | |
[104] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15103619 |
Journal | Proteins |
Year | 2004 |
Volume | 55 |
Pages | 548-57 |
Authors | Shukla A, Guptasarma P |
Title |
Folding of beta/alpha-unit scrambled forms of S. |
Related PDB | |
Related UniProtKB | |
[105] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15707966 |
Journal | Biochem Biophys Res Commun |
Year | 2005 |
Volume | 328 |
Pages | 922-8 |
Authors | Espinoza-Fonseca LM, Trujillo-Ferrara JG |
Title | Structural considerations for the rational design of selective anti-trypanosomal agents: the role of the aromatic clusters at the interface of triosephosphate isomerase dimer. |
Related PDB | |
Related UniProtKB |
Comments |
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According to the literature [4], (1) Glu165 (of 1ypi) acts as a general acid-base to transfer a (pro-R) proton from C1 to C2 (of substrate), (2) Intramolecular proton transfer from O1 to O2. (3) Glu165 acts as a general acid-base to transfer a (pro-R) proton from C1 to O2 (of substrate), According to the literature, According to the literature [42], (A) Isomerization; Shift of double-bond from carbonyl group to adjacent C=C. (A1) Glu165 acts as as a general base to deprotonate the C1 atom of substrate (G3P), (A2) Glu165 acts as a general acid to protonate the O1 atom, (B) Isomerization; Shift of double-bond from C=C to carbonyl group. (B1) Glu165 acts as a general base to deprotonate the O1 hydroxyl atom, (B2) Glu165 acts as a general acid to protonate the C2 atom, |
Created | Updated |
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2005-05-11 | 2021-03-26 |