DB code: D00008
| CATH domain | 3.40.50.720 : Rossmann fold | |
|---|---|---|
| 3.90.110.10 : L-2-Hydroxyisocaproate Dehydrogenase; Chain A, domain 2 | Catalytic domain | |
| E.C. | 1.1.1.37 | |
| CSA | 1emd | |
| M-CSA | 1emd | |
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.40.50.720 : Rossmann fold | S00543 S00551 S00552 S00553 S00602 S00604 S00605 S00608 S00610 S00625 S00319 S00328 S00329 S00330 S00331 S00332 D00456 D00457 D00458 S00324 S00320 S00325 S00326 S00327 D00459 S00335 S00336 S00334 T00219 S00339 D00513 D00001 D00002 D00003 D00005 D00007 D00010 D00012 D00017 D00018 D00023 D00027 D00028 D00031 D00032 D00033 D00034 D00035 D00037 D00048 D00071 D00476 D00481 D00482 D00490 D00492 D00494 D00545 D00601 D00603 D00604 D00605 D00615 D00845 D00857 D00858 M00161 M00171 M00210 T00002 T00010 T00011 T00015 T00227 T00247 T00408 T00414 D00827 D00262 D00274 D00275 M00035 T00109 |
| 3.90.110.10 : L-2-Hydroxyisocaproate Dehydrogenase; Chain A, domain 2 | D00005 M00171 D00827 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P61889 |
Malate dehydrogenase
|
EC
1.1.1.37
|
NP_417703.1
(Protein)
NC_000913.2 (DNA/RNA sequence) YP_491420.1 (Protein) NC_007779.1 (DNA/RNA sequence) |
PF02866
(Ldh_1_C)
PF00056 (Ldh_1_N) [Graphical View] |
| P00346 |
Malate dehydrogenase, mitochondrial
|
EC
1.1.1.37
|
PF02866
(Ldh_1_C)
PF00056 (Ldh_1_N) [Graphical View] |
|
| Q07841 |
Malate dehydrogenase
|
EC
1.1.1.37
|
YP_137180.1
(Protein)
NC_006396.1 (DNA/RNA sequence) |
PF02866
(Ldh_1_C)
PF00056 (Ldh_1_N) [Graphical View] |
| P10584 |
Malate dehydrogenase
|
EC
1.1.1.37
|
PF02866
(Ldh_1_C)
PF00056 (Ldh_1_N) [Graphical View] |
|
| P11708 |
Malate dehydrogenase, cytoplasmic
|
EC
1.1.1.37
Cytosolic malate dehydrogenase |
NP_999039.1
(Protein)
NM_213874.1 (DNA/RNA sequence) |
PF02866
(Ldh_1_C)
PF00056 (Ldh_1_N) [Graphical View] |
| KEGG enzyme name |
|---|
|
malate dehydrogenase
malic dehydrogenase L-malate dehydrogenase NAD-L-malate dehydrogenase malic acid dehydrogenase NAD-dependent malic dehydrogenase NAD-malate dehydrogenase NAD-malic dehydrogenase malate (NAD) dehydrogenase NAD-dependent malate dehydrogenase NAD-specific malate dehydrogenase NAD-linked malate dehydrogenase MDH L-malate-NAD+ oxidoreductase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P61889 | MDH_ECOLI | (S)-malate + NAD(+) = oxaloacetate + NADH. | Homodimer. | ||
| P00346 | MDHM_PIG | (S)-malate + NAD(+) = oxaloacetate + NADH. | Homodimer. | Mitochondrion matrix. | |
| Q07841 | MDH_HALMA | (S)-malate + NAD(+) = oxaloacetate + NADH. | Homotetramer, arranged as a dimer of dimers. | Cytoplasm. | |
| P10584 | MDH_THETH | (S)-malate + NAD(+) = oxaloacetate + NADH. | Homodimer. | ||
| P11708 | MDHC_PIG | (S)-malate + NAD(+) = oxaloacetate + NADH. | Homodimer. | Cytoplasm. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00020 | Citrate cycle (TCA cycle) | |
| MAP00620 | Pyruvate metabolism | |
| MAP00630 | Glyoxylate and dicarboxylate metabolism | |
| MAP00710 | Carbon fixation in photosynthetic organisms | |
| MAP00720 | Reductive carboxylate cycle (CO2 fixation) |
| Compound table | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Substrates | Products | Intermediates | |||||||||
| KEGG-id | C00149 | C00003 | C00036 | C00004 | C00080 | ||||||
| E.C. | |||||||||||
| Compound | (S)-Malate | NAD+ | Oxaloacetate | NADH | H+ | ||||||
| Type | carbohydrate,carboxyl group | amide group,amine group,nucleotide | carbohydrate,carboxyl group | amide group,amine group,nucleotide | others | ||||||
| ChEBI |
30797 30797 |
15846 15846 |
30744 30744 |
16908 16908 |
15378 15378 |
||||||
| PubChem |
222656 222656 |
5893 5893 |
970 970 |
439153 439153 |
1038 1038 |
||||||
| 1emdA01 |
|
|
|
|
|
Unbound | Bound:NAD | Unbound | Unbound | ||
| 1ib6A01 |
|
|
|
|
|
Unbound | Bound:NAD | Unbound | Unbound | ||
| 1ib6B01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ib6C01 |
|
|
|
|
|
Unbound | Bound:NAD | Unbound | Unbound | ||
| 1ib6D01 |
|
|
|
|
|
Unbound | Bound:NAD | Unbound | Unbound | ||
| 1ie3A01 |
|
|
|
|
|
Unbound | Bound:NAD | Unbound | Unbound | ||
| 1ie3B01 |
|
|
|
|
|
Unbound | Bound:NAD | Unbound | Unbound | ||
| 1ie3C01 |
|
|
|
|
|
Unbound | Bound:NAD | Unbound | Unbound | ||
| 1ie3D01 |
|
|
|
|
|
Unbound | Bound:NAD | Unbound | Unbound | ||
| 2cmdA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1mldA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1mldB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1mldC01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1mldD01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1d3aA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1d3aB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1gt2A02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Bound:NAD | ||
| 1gt2B02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Bound:NAD | ||
| 1hlpA02 |
|
|
|
|
|
Unbound | Bound:NAD | Unbound | Unbound | ||
| 1hlpB02 |
|
|
|
|
|
Unbound | Bound:NAD | Unbound | Unbound | ||
| 1o6zA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Bound:NAD | ||
| 1o6zB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Bound:NAD | ||
| 1o6zC02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Bound:NAD | ||
| 1o6zD02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Bound:NAD | ||
| 2hlpA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2hlpB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1bdmA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Analogue:NAX | ||
| 1bdmB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Analogue:NAX | ||
| 1bmdA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Bound:NAD | ||
| 1bmdB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Bound:NAD | ||
| 1iz9A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1iz9B01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 4mdhA01 |
|
|
|
|
|
Unbound | Bound:NAD | Unbound | Unbound | ||
| 4mdhB01 |
|
|
|
|
|
Unbound | Bound:NAD | Unbound | Unbound | ||
| 5mdhA01 |
|
|
|
|
|
Unbound | Bound:NAD | Unbound | Unbound | ||
| 5mdhB01 |
|
|
|
|
|
Unbound | Bound:NAD | Unbound | Unbound | ||
| 1emdA02 |
|
|
|
|
|
Analogue:CIT | Unbound | Unbound | Unbound | ||
| 1ib6A02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ib6B02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ib6C02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ib6D02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ie3A02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ie3B02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ie3C02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ie3D02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2cmdA02 |
|
|
|
|
|
Analogue:CIT | Unbound | Unbound | Unbound | ||
| 1mldA02 |
|
|
|
|
|
Analogue:CIT | Unbound | Unbound | Unbound | ||
| 1mldB02 |
|
|
|
|
|
Analogue:CIT | Unbound | Unbound | Unbound | ||
| 1mldC02 |
|
|
|
|
|
Analogue:CIT | Unbound | Unbound | Unbound | ||
| 1mldD02 |
|
|
|
|
|
Analogue:CIT | Unbound | Unbound | Unbound | ||
| 1d3aA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1d3aB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1gt2A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1gt2B01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1hlpA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1hlpB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1o6zA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1o6zB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1o6zC01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1o6zD01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2hlpA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2hlpB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1bdmA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1bdmB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1bmdA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1bmdB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1iz9A02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1iz9B02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 4mdhA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 4mdhB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 5mdhA02 |
|
|
|
|
|
Unbound | Unbound | Analogue:MAK | Unbound | ||
| 5mdhB02 |
|
|
|
|
|
Unbound | Unbound | Analogue:MAK | Unbound | ||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P11708, P00346, P61889, Q07841, P10584 & literature [25] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1emdA01 |
|
|
|
|
|
|||||
| 1ib6A01 |
|
|
|
|
|
|||||
| 1ib6B01 |
|
|
|
|
|
|||||
| 1ib6C01 |
|
|
|
|
|
|||||
| 1ib6D01 |
|
|
|
|
|
|||||
| 1ie3A01 |
|
|
|
|
|
|||||
| 1ie3B01 |
|
|
|
|
|
|||||
| 1ie3C01 |
|
|
|
|
|
|||||
| 1ie3D01 |
|
|
|
|
|
|||||
| 2cmdA01 |
|
|
|
|
|
|||||
| 1mldA01 |
|
|
|
|
|
|||||
| 1mldB01 |
|
|
|
|
|
|||||
| 1mldC01 |
|
|
|
|
|
|||||
| 1mldD01 |
|
|
|
|
|
|||||
| 1d3aA02 |
|
|
|
|
|
|||||
| 1d3aB02 |
|
|
|
|
|
|||||
| 1gt2A02 |
|
|
|
|
|
|||||
| 1gt2B02 |
|
|
|
|
|
|||||
| 1hlpA02 |
|
|
|
|
|
|||||
| 1hlpB02 |
|
|
|
|
|
|||||
| 1o6zA02 |
|
|
|
|
|
|||||
| 1o6zB02 |
|
|
|
|
|
|||||
| 1o6zC02 |
|
|
|
|
|
|||||
| 1o6zD02 |
|
|
|
|
|
|||||
| 2hlpA02 |
|
|
|
|
|
|||||
| 2hlpB02 |
|
|
|
|
|
|||||
| 1bdmA01 |
|
|
|
|
|
|||||
| 1bdmB01 |
|
|
|
|
|
|||||
| 1bmdA01 |
|
|
|
|
|
|||||
| 1bmdB01 |
|
|
|
|
|
|||||
| 1iz9A01 |
|
|
|
|
|
|||||
| 1iz9B01 |
|
|
|
|
|
|||||
| 4mdhA01 |
|
|
|
|
|
|||||
| 4mdhB01 |
|
|
|
|
|
|||||
| 5mdhA01 |
|
|
|
|
|
|||||
| 5mdhB01 |
|
|
|
|
|
|||||
| 1emdA02 |
|
|
|
|
|
ASP 150;ARG 153;HIS 177 | ||||
| 1ib6A02 |
|
|
|
|
|
ASP 150;;HIS 177 | mutant R153C | |||
| 1ib6B02 |
|
|
|
|
|
ASP 150;;HIS 177 | mutant R153C | |||
| 1ib6C02 |
|
|
|
|
|
ASP 150;;HIS 177 | mutant R153C | |||
| 1ib6D02 |
|
|
|
|
|
ASP 150;;HIS 177 | mutant R153C | |||
| 1ie3A02 |
|
|
|
|
|
ASP 150;;HIS 177 | mutant R153C | |||
| 1ie3B02 |
|
|
|
|
|
ASP 150;;HIS 177 | mutant R153C | |||
| 1ie3C02 |
|
|
|
|
|
ASP 150;;HIS 177 | mutant R153C | |||
| 1ie3D02 |
|
|
|
|
|
ASP 150;;HIS 177 | mutant R153C | |||
| 2cmdA02 |
|
|
|
|
|
ASP 150;ARG 153;HIS 177 | ||||
| 1mldA02 |
|
|
|
|
|
ASP 149;ARG 152;HIS 176 | ||||
| 1mldB02 |
|
|
|
|
|
ASP 149;ARG 152;HIS 176 | ||||
| 1mldC02 |
|
|
|
|
|
ASP 149;ARG 152;HIS 176 | ||||
| 1mldD02 |
|
|
|
|
|
ASP 149;ARG 152;HIS 176 | ||||
| 1d3aA01 |
|
|
|
|
|
ASP 168;ARG 171;HIS 195 | ||||
| 1d3aB01 |
|
|
|
|
|
ASP 168;ARG 171;HIS 195 | ||||
| 1gt2A01 |
|
|
|
|
|
ASP 168;ARG 171;HIS 195 | mutant R207S, R292S | |||
| 1gt2B01 |
|
|
|
|
|
ASP 168;ARG 171;HIS 195 | mutant R207S, R292S | |||
| 1hlpA01 |
|
|
|
|
|
ASP 166;ARG 169;HIS 193 | ||||
| 1hlpB01 |
|
|
|
|
|
ASP 166;ARG 169;HIS 193 | ||||
| 1o6zA01 |
|
|
|
|
|
ASP 168;ARG 171;HIS 195 | mutant R207S, R292S | |||
| 1o6zB01 |
|
|
|
|
|
ASP 168;ARG 171;HIS 195 | mutant R207S, R292S | |||
| 1o6zC01 |
|
|
|
|
|
ASP 168;ARG 171;HIS 195 | mutant R207S, R292S | |||
| 1o6zD01 |
|
|
|
|
|
ASP 168;ARG 171;HIS 195 | mutant R207S, R292S | |||
| 2hlpA01 |
|
|
|
|
|
ASP 168;ARG 171;HIS 195 | mutant E267R | |||
| 2hlpB01 |
|
|
|
|
|
ASP 168;ARG 171;HIS 195 | mutant E267R | |||
| 1bdmA02 |
|
|
|
|
|
ASP 158;ARG 161;HIS 186 | mutant T189I | |||
| 1bdmB02 |
|
|
|
|
|
ASP 158;ARG 161;HIS 186 | mutant T189I | |||
| 1bmdA02 |
|
|
|
|
|
ASP 158;ARG 161;HIS 186 | ||||
| 1bmdB02 |
|
|
|
|
|
ASP 158;ARG 161;HIS 186 | ||||
| 1iz9A02 |
|
|
|
|
|
ASP 159;ARG 162;HIS 187 | ||||
| 1iz9B02 |
|
|
|
|
|
ASP 159;ARG 162;HIS 187 | ||||
| 4mdhA02 |
|
|
|
|
|
ASP 158;ARG 161;HIS 186 | ||||
| 4mdhB02 |
|
|
|
|
|
ASP 158;ARG 161;HIS 186 | ||||
| 5mdhA02 |
|
|
|
|
|
ASP 158;ARG 161;HIS 186 | ||||
| 5mdhB02 |
|
|
|
|
|
ASP 158;ARG 161;HIS 186 | ||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[4]
|
p.6077-6078 | |
|
[7]
|
p.876-877 | |
|
[13]
|
p.2084 | |
|
[19]
|
p.4811-4815 | |
|
[20]
|
||
|
[22]
|
||
|
[29]
|
Fig.3, p.261-263 | |
|
[30]
|
p.711-712 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 6239374 |
| Journal | Science |
| Year | 1984 |
| Volume | 226 |
| Pages | 969-71 |
| Authors | Parthasarathy R, Fridey SM |
| Title | Conformational variability of NAD+ in the free and bound states: a nicotinamide sandwich in NAD+ crystals. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments |
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), |
| Medline ID | 87271560 |
| PubMed ID | 3606987 |
| Journal | Biochemistry |
| Year | 1987 |
| Volume | 26 |
| Pages | 2722-34 |
| Authors | Birktoft JJ, Bradshaw RA, Banaszak LJ |
| Title | Structure of porcine heart cytoplasmic malate dehydrogenase: combining X-ray diffraction and chemical sequence data in structural studies. |
| Related PDB | |
| Related UniProtKB | P11708 |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 3398050 |
| Journal | J Mol Biol |
| Year | 1988 |
| Volume | 200 |
| Pages | 609-10 |
| Authors | Harel M, Shoham M, Frolow F, Eisenberg H, Mevarech M, Yonath A, Sussman JL |
| Title | Crystallization of halophilic malate dehydrogenase from Halobacterium marismortui. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). |
| Medline ID | 89375338 |
| PubMed ID | 2775751 |
| Journal | Biochemistry |
| Year | 1989 |
| Volume | 28 |
| Pages | 6065-81 |
| Authors | Birktoft JJ, Rhodes G, Banaszak LJ |
| Title | Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-A resolution. |
| Related PDB | 4mdh |
| Related UniProtKB | P11708 |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1678537 |
| Journal | Philos Trans R Soc Lond B Biol Sci |
| Year | 1991 |
| Volume | 332 |
| Pages | 177-84 |
| Authors | Dunn CR, Wilks HM, Halsall DJ, Atkinson T, Clarke AR, Muirhead H, Holbrook JJ |
| Title | Design and synthesis of new enzymes based on the lactate dehydrogenase framework. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1445401 |
| Journal | Biochem Soc Symp |
| Year | 1992 |
| Volume | 58 |
| Pages | 113-25 |
| Authors | Eisenberg H |
| Title |
Halophilic malate dehydrogenase--a case history of biophysical investigations: ultracentrifugation, |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS). |
| Medline ID | 92373767 |
| PubMed ID | 1507230 |
| Journal | J Mol Biol |
| Year | 1992 |
| Volume | 226 |
| Pages | 867-82 |
| Authors | Hall MD, Levitt DG, Banaszak LJ |
| Title |
Crystal structure of Escherichia coli malate dehydrogenase. |
| Related PDB | 1cmd 2cmd 1cme |
| Related UniProtKB | P61889 |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8476859 |
| Journal | Biochemistry |
| Year | 1993 |
| Volume | 32 |
| Pages | 4308-13 |
| Authors | Cendrin F, Chroboczek J, Zaccai G, Eisenberg H, Mevarech M |
| Title |
Cloning, |
| Related PDB | |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). |
| Medline ID | |
| PubMed ID | 8471603 |
| Journal | Biochemistry |
| Year | 1993 |
| Volume | 32 |
| Pages | 3913-22 |
| Authors | Kelly CA, Nishiyama M, Ohnishi Y, Beppu T, Birktoft JJ |
| Title | Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus. |
| Related PDB | 1bdm 1bmd |
| Related UniProtKB | P10584 |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8444839 |
| Journal | J Biol Chem |
| Year | 1993 |
| Volume | 268 |
| Pages | 4656-60 |
| Authors | Nishiyama M, Birktoft JJ, Beppu T |
| Title | Alteration of coenzyme specificity of malate dehydrogenase from Thermus flavus by site-directed mutagenesis. |
| Related PDB | |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD AND CITRATE. |
| Medline ID | |
| PubMed ID | 8331658 |
| Journal | J Mol Biol |
| Year | 1993 |
| Volume | 232 |
| Pages | 213-22 |
| Authors | Hall MD, Banaszak LJ |
| Title | Crystal structure of a ternary complex of Escherichia coli malate dehydrogenase citrate and NAD at 1.9 A resolution. |
| Related PDB | 1emd |
| Related UniProtKB | P61889 |
| [12] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7849634 |
| Journal | Biochem Mol Biol Int |
| Year | 1994 |
| Volume | 34 |
| Pages | 239-50 |
| Authors | Wani JH, Srivastava VM |
| Title | Effect of cations and anthelmintics on enzymes of respiratory chains of the cestode Hymenolepis diminuta. |
| Related PDB | |
| Related UniProtKB | |
| [13] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). |
| Medline ID | |
| PubMed ID | 8117664 |
| Journal | Biochemistry |
| Year | 1994 |
| Volume | 33 |
| Pages | 2078-88 |
| Authors | Gleason WB, Fu Z, Birktoft J, Banaszak L |
| Title | Refined crystal structure of mitochondrial malate dehydrogenase from porcine heart and the consensus structure for dicarboxylic acid oxidoreductases. |
| Related PDB | 1mld |
| Related UniProtKB | P00346 |
| [14] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). |
| Medline ID | 94162212 |
| PubMed ID | 8011596 |
| Journal | J Mol Graph |
| Year | 1994 |
| Volume | 12 |
| Pages | 14-21, 34 |
| Authors | Duffield ML, Nicholls DJ, Atkinson T, Scawen MD |
| Title | An investigation of the thermal stabilities of two malate dehydrogenases by comparison of their three-dimensional structures. |
| Related PDB | |
| Related UniProtKB | P00346 |
| [15] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7703849 |
| Journal | Protein Sci |
| Year | 1994 |
| Volume | 3 |
| Pages | 2023-32 |
| Authors | Breiter DR, Resnik E, Banaszak LJ |
| Title | Engineering the quaternary structure of an enzyme: construction and analysis of a monomeric form of malate dehydrogenase from Escherichia coli. |
| Related PDB | |
| Related UniProtKB | |
| [16] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7601139 |
| Journal | Eur J Biochem |
| Year | 1995 |
| Volume | 230 |
| Pages | 1088-95 |
| Authors | Madern D, Pfister C, Zaccai G |
| Title | Mutation at a single acidic amino acid enhances the halophilic behaviour of malate dehydrogenase from Haloarcula marismortui in physiological salts. |
| Related PDB | |
| Related UniProtKB | |
| [17] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7476321 |
| Journal | Metabolism |
| Year | 1995 |
| Volume | 44 |
| Pages | 1380-3 |
| Authors | Petersen KF, Blair JB, Shulman GI |
| Title | Triiodothyronine treatment increases substrate cycling between pyruvate carboxylase and malic enzyme in perfused rat liver. |
| Related PDB | |
| Related UniProtKB | |
| [18] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8901548 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 1996 |
| Volume | 93 |
| Pages | 12150-4 |
| Authors | Plochocka D, Welnicki M, Zielenkiewicz P, Ostoja-Zagorski W |
| Title | Three-dimensional model of the potyviral genome-linked protein. |
| Related PDB | |
| Related UniProtKB | |
| [19] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9125501 |
| Journal | Biochemistry |
| Year | 1997 |
| Volume | 36 |
| Pages | 4800-16 |
| Authors | Cunningham MA, Ho LL, Nguyen DT, Gillilan RE, Bash PA |
| Title | Simulation of the enzyme reaction mechanism of malate dehydrogenase. |
| Related PDB | |
| Related UniProtKB | |
| [20] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9692968 |
| Journal | Biochemistry |
| Year | 1998 |
| Volume | 37 |
| Pages | 10780-91 |
| Authors | Jairajpuri MA, Azam N, Baburaj K, Bulliraju E, Durani S |
| Title | Charge and solvation effects in anion recognition centers: an inquiry exploiting reactive arginines. |
| Related PDB | |
| Related UniProtKB | |
| [21] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 10206992 |
| Journal | J Biol Chem |
| Year | 1999 |
| Volume | 274 |
| Pages | 11761-7 |
| Authors | Kim SY, Hwang KY, Kim SH, Sung HC, Han YS, Cho Y |
| Title |
Structural basis for cold adaptation. |
| Related PDB | 1b8p |
| Related UniProtKB | |
| [22] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). |
| Medline ID | 99173114 |
| PubMed ID | 10075524 |
| Journal | J Mol Biol |
| Year | 1999 |
| Volume | 285 |
| Pages | 703-12 |
| Authors | Chapman AD, Cortes A, Dafforn TR, Clarke AR, Brady RL |
| Title |
Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, |
| Related PDB | 5mdh |
| Related UniProtKB | P11708 |
| [23] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10653644 |
| Journal | Biochemistry |
| Year | 2000 |
| Volume | 39 |
| Pages | 1001-10 |
| Authors | Madern D, Ebel C, Mevarech M, Richard SB, Pfister C, Zaccai G |
| Title | Insights into the molecular relationships between malate and lactate dehydrogenases: structural and biochemical properties of monomeric and dimeric intermediates of a mutant of tetrameric L-[LDH-like] malate dehydrogenase from the halophilic archaeon Haloarcula marismortui. |
| Related PDB | |
| Related UniProtKB | |
| [24] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 10653643 |
| Journal | Biochemistry |
| Year | 2000 |
| Volume | 39 |
| Pages | 992-1000 |
| Authors | Richard SB, Madern D, Garcin E, Zaccai G |
| Title | Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 A resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui. |
| Related PDB | 1d3a 2hlp |
| Related UniProtKB | |
| [25] | |
| Resource | |
| Comments |
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NAD AND PYRUVATE, |
| Medline ID | |
| PubMed ID | 11389141 |
| Journal | J Biol Chem |
| Year | 2001 |
| Volume | 276 |
| Pages | 31156-62 |
| Authors | Bell JK, Yennawar HP, Wright SK, Thompson JR, Viola RE, Banaszak LJ |
| Title | Structural analyses of a malate dehydrogenase with a variable active site. |
| Related PDB | 1ib6 1ie3 |
| Related UniProtKB | P61889 |
| [26] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11292347 |
| Journal | J Mol Biol |
| Year | 2001 |
| Volume | 307 |
| Pages | 1351-62 |
| Authors | Lee BI, Chang C, Cho SJ, Eom SH, Kim KK, Yu YG, Suh SW |
| Title |
Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, |
| Related PDB | |
| Related UniProtKB | |
| [27] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11473265 |
| Journal | Nat Struct Biol |
| Year | 2001 |
| Volume | 8 |
| Pages | 721-8 |
| Authors | Chen J, Walter S, Horwich AL, Smith DL |
| Title | Folding of malate dehydrogenase inside the GroEL-GroES cavity. |
| Related PDB | |
| Related UniProtKB | |
| [28] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11742111 |
| Journal | Protein Eng |
| Year | 2001 |
| Volume | 14 |
| Pages | 911-7 |
| Authors | Trejo F, Gelpi JL, Ferrer A, Boronat A, Busquets M, Cortes A |
| Title | Contribution of engineered electrostatic interactions to the stability of cytosolic malate dehydrogenase. |
| Related PDB | |
| Related UniProtKB | |
| [29] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12537350 |
| Journal | Gen Physiol Biophys |
| Year | 2002 |
| Volume | 21 |
| Pages | 257-65 |
| Authors | Minarik P, Tomaskova N, Kollarova M, Antalik M |
| Title | Malate dehydrogenases--structure and function. |
| Related PDB | |
| Related UniProtKB | |
| [30] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12054817 |
| Journal | J Mol Biol |
| Year | 2002 |
| Volume | 318 |
| Pages | 707-21 |
| Authors | Dalhus B, Saarinen M, Sauer UH, Eklund P, Johansson K, Karlsson A, Ramaswamy S, Bjork A, Synstad B, Naterstad K, Sirevag R, Eklund H |
| Title | Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenases. |
| Related PDB | |
| Related UniProtKB | |
| [31] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 14572663 |
| Journal | FEBS Lett |
| Year | 2003 |
| Volume | 553 |
| Pages | 423-6 |
| Authors | Bjork A, Mantzilas D, Sirevag R, Eijsink VG |
| Title | Electrostatic interactions across the dimer-dimer interface contribute to the pH-dependent stability of a tetrameric malate dehydrogenase. |
| Related PDB | |
| Related UniProtKB | |
| [32] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 12581646 |
| Journal | J Mol Biol |
| Year | 2003 |
| Volume | 326 |
| Pages | 859-73 |
| Authors | Irimia A, Ebel C, Madern D, Richard SB, Cosenza LW, Zaccai G, Vellieux FM |
| Title | The Oligomeric states of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies. |
| Related PDB | 1gt2 1o6z |
| Related UniProtKB | |
| [33] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 14659762 |
| Journal | J Mol Biol |
| Year | 2004 |
| Volume | 335 |
| Pages | 343-56 |
| Authors | Irimia A, Vellieux FM, Madern D, Zaccai G, Karshikoff A, Tibbelin G, Ladenstein R, Lien T, Birkeland NK |
| Title | The 2.9A resolution crystal structure of malate dehydrogenase from Archaeoglobus fulgidus: mechanisms of oligomerisation and thermal stabilisation. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme catalyzes the following reaction:
(A) Hydride transfer from substrate, |
| Created | Updated |
|---|---|
| 2004-03-24 | 2009-02-26 |