DB code: S00366
RLCP classification | 3.100.220195.81 : Transfer | |
---|---|---|
CATH domain | 3.40.50.1240 : Rossmann fold | Catalytic domain |
E.C. | 5.4.2.1 | |
CSA | 1qhf | |
M-CSA | 1qhf | |
MACiE |
CATH domain | Related DB codes (homologues) |
---|---|
3.40.50.1240 : Rossmann fold | S00365 S00363 D00460 D00514 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
---|---|---|---|---|
P62707 |
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
|
BPG-dependent PGAM
PGAM Phosphoglyceromutase dPGM EC 5.4.2.1 |
NP_415276.1
(Protein)
NC_000913.2 (DNA/RNA sequence) YP_489028.1 (Protein) NC_007779.1 (DNA/RNA sequence) |
PF00300
(His_Phos_1)
[Graphical View] |
P0A5R6 |
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
|
BPG-dependent PGAM
PGAM Phosphoglyceromutase dPGM EC 5.4.2.1 |
NP_334917.1
(Protein)
NC_002755.2 (DNA/RNA sequence) YP_006513819.1 (Protein) NC_018143.1 (DNA/RNA sequence) YP_177731.1 (Protein) NC_000962.3 (DNA/RNA sequence) |
PF00300
(His_Phos_1)
[Graphical View] |
Q6MWZ7 |
(Possible phosphoglycerate mutase Gpm2
|
Phosphoglyceromutase
PGAM) (BPG-dependent PGAM) |
YP_006516686.1
(Protein)
NC_018143.1 (DNA/RNA sequence) YP_177944.1 (Protein) NC_000962.3 (DNA/RNA sequence) |
PF00300
(His_Phos_1)
[Graphical View] |
P36623 |
Phosphoglycerate mutase
|
PGAM
EC 5.4.2.1 BPG-dependent PGAM MPGM Phosphoglyceromutase |
NP_594889.1
(Protein)
NM_001020318.2 (DNA/RNA sequence) |
PF00300
(His_Phos_1)
[Graphical View] |
P00950 |
Phosphoglycerate mutase 1
|
PGAM 1
EC 5.4.2.1 BPG-dependent PGAM 1 MPGM 1 Phosphoglyceromutase 1 |
NP_012770.1
(Protein)
NM_001179718.1 (DNA/RNA sequence) |
PF00300
(His_Phos_1)
[Graphical View] |
KEGG enzyme name |
---|
phosphoglycerate mutase
phosphoglycerate phosphomutase phosphoglyceromutase glycerate phosphomutase (diphosphoglycerate cofactor) monophosphoglycerate mutase monophosphoglyceromutase diphosphoglycomutase diphosphoglycerate mutase bisphosphoglyceromutase GriP mutase MPGM PGA mutase PGAM-i PGAM PGAM-d PGM |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
P62707 | GPMA_ECOLI | 2-phospho-D-glycerate = 3-phospho-D-glycerate. | Homodimer. | ||
P0A5R6 | GPMA_MYCTU | 2-phospho-D-glycerate = 3-phospho-D-glycerate. | |||
Q6MWZ7 | Q6MWZ7_MYCTU | ||||
P00950 | PMG1_YEAST | 2-phospho-D-glycerate = 3-phospho-D-glycerate. | Homotetramer. | ||
P36623 | PMGY_SCHPO | 2-phospho-D-glycerate = 3-phospho-D-glycerate. | Monomer. |
KEGG Pathways | Map code | Pathways | E.C. |
---|---|---|
MAP00010 | Glycolysis / Gluconeogenesis |
Compound table | |||||||||
---|---|---|---|---|---|---|---|---|---|
Cofactors | Substrates | Products | Intermediates | ||||||
KEGG-id | C01159 | C00631 | C00197 | C04262 | |||||
E.C. | |||||||||
Compound | 2,3-Bisphospho-D-glycerate | 2-Phospho-D-glycerate | 3-Phospho-D-glycerate | Protein N(tau)-phospho-L-histidine | |||||
Type | carboxyl group,phosphate group/phosphate ion | carbohydrate,carboxyl group,phosphate group/phosphate ion | carbohydrate,carboxyl group,phosphate group/phosphate ion | ||||||
ChEBI |
17720 17720 |
17835 17835 |
17794 17794 |
||||||
PubChem |
186004 186004 |
439278 439278 |
439183 439183 |
||||||
1e58A | Unbound | Unbound | Unbound | Intermediate-bound:HIS_10-NEP | |||||
1e59A | Analogue:VO3 | Unbound | Unbound | Unbound | |||||
1riiA | Unbound | Analogue:GOL | Unbound | Unbound | |||||
1riiB | Unbound | Analogue:GOL | Unbound | Unbound | |||||
1riiC | Unbound | Unbound | Unbound | Unbound | |||||
1riiD | Unbound | Analogue:GOL | Unbound | Unbound | |||||
2a6pA | Unbound | Analogue:GOL-SO4 | Unbound | Unbound | |||||
2a6pB | Unbound | Analogue:GOL-SO4 | Unbound | Unbound | |||||
1bq3A | Analogue:IHP | Unbound | Unbound | Unbound | |||||
1bq3B | Unbound | Unbound | Unbound | Unbound | |||||
1bq3C | Unbound | Unbound | Unbound | Unbound | |||||
1bq3D | Analogue:IHP | Unbound | Unbound | Unbound | |||||
1bq4A | Unbound | Unbound | Unbound | Unbound | |||||
1bq4B | Unbound | Unbound | Unbound | Unbound | |||||
1bq4C | Unbound | Unbound | Unbound | Unbound | |||||
1bq4D | Unbound | Unbound | Unbound | Unbound | |||||
1qhfA | Unbound | Unbound | Bound:3PG | Unbound | |||||
1qhfB | Unbound | Unbound | Bound:3PG | Unbound | |||||
3pgmA | Unbound | Unbound | Bound:3PG | Unbound | |||||
4pgmA | Unbound | Unbound | Unbound | Unbound | |||||
4pgmB | Unbound | Unbound | Unbound | Unbound | |||||
4pgmC | Unbound | Unbound | Unbound | Unbound | |||||
4pgmD | Unbound | Unbound | Unbound | Unbound | |||||
5pgmA | Unbound | Unbound | Unbound | Unbound | |||||
5pgmB | Unbound | Unbound | Unbound | Unbound | |||||
5pgmC | Unbound | Unbound | Unbound | Unbound | |||||
5pgmD | Unbound | Unbound | Unbound | Unbound | |||||
5pgmE | Unbound | Unbound | Unbound | Unbound | |||||
5pgmF | Unbound | Unbound | Unbound | Unbound | |||||
5pgmG | Unbound | Unbound | Unbound | Unbound | |||||
5pgmH | Unbound | Unbound | Unbound | Unbound | |||||
1fztA | Unbound | Unbound | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
Swiss-prot;P00950, P62707, P36623 & literature [18] |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1e58A | HIS 10;GLU 88;ARG 9;ASN 16;ARG 61;HIS 183 | HIS 10(Phosphorylation) | Modified residue H10-NEP | |||||||
1e59A | HIS 10;GLU 88;ARG 9;ASN 16;ARG 61;HIS 183 | HIS 10(Phosphorylation) | ||||||||
1riiA | HIS 12;GLU 90;ARG 11;ASN 18;ARG 63;HIS 183 | HIS 12(Phosphorylation) | ||||||||
1riiB | HIS 12;GLU 90;ARG 11;ASN 18;ARG 63;HIS 183 | HIS 12(Phosphorylation) | ||||||||
1riiC | HIS 12;GLU 90;ARG 11;ASN 18;ARG 63;HIS 183 | HIS 12(Phosphorylation) | ||||||||
1riiD | HIS 12;GLU 90;ARG 11;ASN 18;ARG 63;HIS 183 | HIS 12(Phosphorylation) | ||||||||
2a6pA | HIS 13;GLU 85;ARG 12; ;ARG 64;HIS 147 | HIS 13(Phosphorylation) | ||||||||
2a6pB | HIS 13;GLU 85;ARG 12; ;ARG 64;HIS 147 | HIS 13(Phosphorylation) | ||||||||
1bq3A | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
1bq3B | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
1bq3C | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
1bq3D | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
1bq4A | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
1bq4B | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
1bq4C | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
1bq4D | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
1qhfA | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
1qhfB | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
3pgmA | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 179 | HIS 8(Phosphorylation) | ||||||||
4pgmA | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
4pgmB | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
4pgmC | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
4pgmD | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
5pgmA | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
5pgmB | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
5pgmC | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
5pgmD | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
5pgmE | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
5pgmF | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
5pgmG | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
5pgmH | HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 | HIS 8(Phosphorylation) | ||||||||
1fztA | HIS 15;GLU 93;ARG 14;ASN 21;ARG 66;HIS 163 | HIS 15(Phosphorylation) |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[2]
|
Scheme II, p.741-742 | |
[4]
|
Fig.3, p.125-128 | |
[14]
|
p.455-457 | |
[15]
|
p.1825-1826 | |
[18]
|
Fig.5, p.1511-1515 | |
[23]
|
p.1076-1077 | |
[24]
|
p.1133-1137 | |
[26]
|
p.82-83 |
References | |
---|---|
[1] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 6251799 |
Journal | Biochem Biophys Res Commun |
Year | 1980 |
Volume | 95 |
Pages | 132-9 |
Authors | Hass LF, Miller KB |
Title | Human erythrocyte phosphoglycerate mutase: evidence for normal catalysis in the absence of added 2,3-bisphospho-D-glycerate. |
Related PDB | |
Related UniProtKB | |
[2] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 6243955 |
Journal | Biochemistry |
Year | 1980 |
Volume | 19 |
Pages | 738-43 |
Authors | Blattler WA, Knowles JR |
Title | Phosphoglycerate mutases: stereochemical course of the phosphoryl group transfers catalyzed by the cofactor-dependent enzyme from rabbit muscle and the cofactor-independent enzyme from wheat germ. |
Related PDB | |
Related UniProtKB | |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 6115417 |
Journal | Philos Trans R Soc Lond B Biol Sci |
Year | 1981 |
Volume | 293 |
Pages | 177-89 |
Authors | Sternberg MJ, Cohen FE, Taylor WR, Feldmann RJ |
Title | Analysis and predication of structural motifs in the glycolytic enzymes. |
Related PDB | |
Related UniProtKB | |
[4] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). |
Medline ID | 81273329 |
PubMed ID | 6115412 |
Journal | Philos Trans R Soc Lond B Biol Sci |
Year | 1981 |
Volume | 293 |
Pages | 121-30 |
Authors | Winn SI, Watson HC, Harkins RN, Fothergill LA |
Title | Structure and activity of phosphoglycerate mutase. |
Related PDB | 3pgm |
Related UniProtKB | P00950 |
[5] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 6282653 |
Journal | Fed Proc |
Year | 1982 |
Volume | 41 |
Pages | 2424-31 |
Authors | Knowles JR |
Title | Phospho transfer enzymes: lessons from stereochemistry. |
Related PDB | |
Related UniProtKB | |
[6] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 6318807 |
Journal | Biochemistry |
Year | 1983 |
Volume | 22 |
Pages | 6130-4 |
Authors | Hunt AG, Simplaceanu V, Hong JS, Ho C |
Title | Phosphorus-31 nuclear magnetic resonance investigation of membrane vesicles from Escherichia coli. |
Related PDB | |
Related UniProtKB | |
[7] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 6331428 |
Journal | Biochem Biophys Res Commun |
Year | 1984 |
Volume | 121 |
Pages | 826-33 |
Authors | Amato SV, Rose ZB, Liebman MN |
Title | Macro-structural organization of phosphoglycerate mutase. |
Related PDB | |
Related UniProtKB | |
[8] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 6331429 |
Journal | Biochem Biophys Res Commun |
Year | 1984 |
Volume | 121 |
Pages | 834-41 |
Authors | Rose ZB, Kaklij GS |
Title | The effects of anions on phosphoglycerate mutase. |
Related PDB | |
Related UniProtKB | |
[9] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1659318 |
Journal | Arch Biochem Biophys |
Year | 1991 |
Volume | 291 |
Pages | 201-11 |
Authors | Mendz GL |
Title | Stimulation of mutases and isomerases by vanadium. |
Related PDB | |
Related UniProtKB | |
[10] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8110200 |
Journal | Biochem J |
Year | 1994 |
Volume | 297 |
Pages | 603-8 |
Authors | Nairn J, Price NC, Fothergill-Gilmore LA, Walker GE, Fothergill JE, Dunbar B |
Title | The amino acid sequence of the small monomeric phosphoglycerate mutase from the fission yeast Schizosaccharomyces pombe. |
Related PDB | |
Related UniProtKB | |
[11] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8765231 |
Journal | Biochim Biophys Acta |
Year | 1996 |
Volume | 1296 |
Pages | 69-75 |
Authors | Nairn J, Price NC, Kelly SM, Rigden D, Fothergill-Gilmore LA, Krell T |
Title | Phosphoglycerate mutase from Schizosaccharomyces pombe: development of an expression system and characterisation of three histidine mutants of the enzyme. |
Related PDB | |
Related UniProtKB | |
[12] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9030753 |
Journal | Eur J Biochem |
Year | 1997 |
Volume | 243 |
Pages | 306-14 |
Authors | Seip S, Lanz R, Gutknecht R, Flukiger K, Erni B |
Title | The fructose transporter of Bacillus subtilis encoded by the lev operon: backbone assignment and secondary structure of the IIB(Lev) subunit. |
Related PDB | |
Related UniProtKB | |
[13] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9390410 |
Journal | J Biomol NMR |
Year | 1997 |
Volume | 10 |
Pages | 309-10 |
Authors | Uhrinova S, Uhrin D, Nairn J, Price NC, Fothergill-Gilmore LA, Barlow PN |
Title | Backbone assignment of double labelled 23.7 kDa phosphoglycerate mutase from Schizosaccharomyces pombe. |
Related PDB | |
Related UniProtKB | |
[14] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). |
Medline ID | 98173871 |
PubMed ID | 9512715 |
Journal | J Mol Biol |
Year | 1998 |
Volume | 276 |
Pages | 449-59 |
Authors | Rigden DJ, Alexeev D, Phillips SE, Fothergill-Gilmore LA |
Title |
The 2.3 A X-ray crystal structure of S. |
Related PDB | 4pgm |
Related UniProtKB | P00950 |
[15] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 10531478 |
Journal | Acta Crystallogr D Biol Crystallogr |
Year | 1999 |
Volume | 55 |
Pages | 1822-6 |
Authors | Crowhurst GS, Dalby AR, Isupov MN, Campbell JW, Littlechild JA |
Title | Structure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at 1.7 A. |
Related PDB | 1qhf |
Related UniProtKB | |
[16] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10437801 |
Journal | FEBS Lett |
Year | 1999 |
Volume | 455 |
Pages | 344-8 |
Authors | Fraser HI, Kvaratskhelia M, White MF |
Title | The two analogous phosphoglycerate mutases of Escherichia coli. |
Related PDB | |
Related UniProtKB | |
[17] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 10369755 |
Journal | J Mol Biol |
Year | 1999 |
Volume | 289 |
Pages | 691-9 |
Authors | Rigden DJ, Walter RA, Phillips SE, Fothergill-Gilmore LA |
Title | Polyanionic inhibitors of phosphoglycerate mutase: combined structural and biochemical analysis. |
Related PDB | 1bq3 1bq4 |
Related UniProtKB | |
[18] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 10064712 |
Journal | J Mol Biol |
Year | 1999 |
Volume | 286 |
Pages | 1507-17 |
Authors | Rigden DJ, Walter RA, Phillips SE, Fothergill-Gilmore LA |
Title |
Sulphate ions observed in the 2.12 A structure of a new crystal form of S. |
Related PDB | 5pgm |
Related UniProtKB | |
[19] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11106417 |
Journal | Eur J Biochem |
Year | 2000 |
Volume | 267 |
Pages | 7065-74 |
Authors | Nairn J, Duncan D, Price NE, Kelly SM, Fothergill-Gilmore LA, Uhrinova S, Barlow PN, Rigden DJ, Price NC |
Title |
Characterization of active-site mutants of Schizosaccharomyces pombe phosphoglycerate mutase. |
Related PDB | |
Related UniProtKB | |
[20] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 11038361 |
Journal | J Biol Chem |
Year | 2001 |
Volume | 276 |
Pages | 3247-53 |
Authors | Bond CS, White MF, Hunter WN |
Title | High resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase. |
Related PDB | 1e58 |
Related UniProtKB | P62707 |
[21] | |
Resource | |
Comments |
NMR, |
Medline ID | |
PubMed ID | 11237600 |
Journal | J Mol Biol |
Year | 2001 |
Volume | 306 |
Pages | 275-90 |
Authors | Uhrinova S, Uhrin D, Nairn J, Price NC, Fothergill-Gilmore LA, Barlow PN |
Title |
Solution structure and dynamics of an open beta-sheet, |
Related PDB | 1fzt |
Related UniProtKB | |
[22] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11514674 |
Journal | Protein Sci |
Year | 2001 |
Volume | 10 |
Pages | 1835-46 |
Authors | Rigden DJ, Bagyan I, Lamani E, Setlow P, Jedrzejas MJ |
Title | A cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus is actually a broad specificity phosphatase. |
Related PDB | |
Related UniProtKB | |
[23] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS). |
Medline ID | |
PubMed ID | 11884145 |
Journal | J Mol Biol |
Year | 2002 |
Volume | 316 |
Pages | 1071-81 |
Authors | Bond CS, White MF, Hunter WN |
Title | Mechanistic implications for Escherichia coli cofactor-dependent phosphoglycerate mutase based on the high-resolution crystal structure of a vanadate complex. |
Related PDB | 1e59 |
Related UniProtKB | P62707 |
[24] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11827481 |
Journal | J Mol Biol |
Year | 2002 |
Volume | 315 |
Pages | 1129-43 |
Authors | Rigden DJ, Mello LV, Setlow P, Jedrzejas MJ |
Title | Structure and mechanism of action of a cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus with broad specificity phosphatase activity. |
Related PDB | |
Related UniProtKB | |
[25] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11951058 |
Journal | Med Sci Monit |
Year | 2002 |
Volume | 8 |
Pages | BR123-35 |
Authors | Torshin IY |
Title | Functional maps of the junctions between interglobular contacts and active sites in glycolytic enzymes -- a comparative analysis of the biochemical and structural data. |
Related PDB | |
Related UniProtKB | |
[26] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12586342 |
Journal | FEBS Lett |
Year | 2003 |
Volume | 536 |
Pages | 77-84 |
Authors | Rigden DJ |
Title | Unexpected catalytic site variation in phosphoprotein phosphatase homologues of cofactor-dependent phosphoglycerate mutase. |
Related PDB | |
Related UniProtKB | |
[27] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15258155 |
Journal | J Biol Chem |
Year | 2004 |
Volume | 279 |
Pages | 39132-8 |
Authors | Wang Y, Wei Z, Bian Q, Cheng Z, Wan M, Liu L, Gong W |
Title | Crystal structure of human bisphosphoglycerate mutase. |
Related PDB | |
Related UniProtKB | |
[28] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15735341 |
Journal | Acta Crystallogr D Biol Crystallogr |
Year | 2005 |
Volume | 61 |
Pages | 309-15 |
Authors | Muller P, Sawaya MR, Pashkov I, Chan S, Nguyen C, Wu Y, Perry LJ, Eisenberg D |
Title | The 1.70 angstroms X-ray crystal structure of Mycobacterium tuberculosis phosphoglycerate mutase. |
Related PDB | 1rii |
Related UniProtKB | |
[29] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 16672613 |
Journal | J Bacteriol |
Year | 2006 |
Volume | 188 |
Pages | 3589-99 |
Authors | Watkins HA, Baker EN |
Title |
Structural and functional analysis of Rv3214 from Mycobacterium tuberculosis, |
Related PDB | 2a6p |
Related UniProtKB |
Comments |
---|
This enzyme is homologous to a phosphatase (E.C. This enzyme catalyzes a kind of intermolecular transfer reaction, (a) 2,3-BPG (cofactor) + enzyme => 3-PGA (or 2-PGA) (product) + phosphorylated enzyme (b) 2-PGA (or 3-PGA) (substrate) + phosphorylated enzyme => 2,3-BPG (cofactor) + enzyme Accoding to the literature [14], (a) 2,3-BPG (cofactor) + enzyme => 3-PGA (or 2-PGA) (product) + phosphorylated enzyme (1) Arg59 and His181 modulate the nucleophilicity of His8, (2) His8 makes a nucleophilic attack on one of the phosphoryl groups of 2,3-BPG, (3) The transition state seems to be stabilized by Arg7, (b) 2-PGA (or 3-PGA) (substrate) + phosphorylated enzyme => 2,3-BPG (cofactor) + enzyme (4) Glu86 now acts as a general base to deprotonate and activate another hydroxyl group of substrate. (5) The activated acceptor, (6) The transition state seems to be stabilized by Arg7, |
Created | Updated |
---|---|
2005-06-14 | 2015-10-27 |