DB code: D00457
| CATH domain | 3.40.50.720 : Rossmann fold | |
|---|---|---|
| 3.40.50.720 : Rossmann fold | Catalytic domain | |
| E.C. | 1.1.1.29 | |
| CSA | 1gdh | |
| M-CSA | 1gdh | |
| 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 D00458 S00324 S00320 S00325 S00326 S00327 D00459 S00335 S00336 S00334 T00219 S00339 D00513 D00001 D00002 D00003 D00005 D00007 D00008 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 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Pfam |
|---|---|---|---|
| P36234 |
Glycerate dehydrogenase
|
GDH
EC 1.1.1.29 NADH-dependent hydroxypyruvate reductase HPR Hydroxypyruvate dehydrogenase Glyoxylate reductase |
PF00389
(2-Hacid_dh)
PF02826 (2-Hacid_dh_C) [Graphical View] |
| KEGG enzyme name |
|---|
|
glycerate dehydrogenase
D-glycerate dehydrogenase hydroxypyruvate reductase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P36234 | DHGY_HYPME | (R)-glycerate + NAD(+) = hydroxypyruvate + NADH. | Homodimer. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00260 | Glycine, serine and threonine metabolism | |
| MAP00630 | Glyoxylate and dicarboxylate metabolism |
| Compound table | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Substrates | Products | Intermediates | ||||||||
| KEGG-id | C00258 | C00003 | C00168 | C00004 | ||||||
| E.C. | ||||||||||
| Compound | (R)-Glycerate | NAD+ | Hydroxypyruvate | NADH | ||||||
| Type | carbohydrate,carboxyl group | amide group,amine group,nucleotide | carbohydrate,carboxyl group | amide group,amine group,nucleotide | ||||||
| ChEBI |
32398 32398 |
15846 15846 |
30841 30841 |
16908 16908 |
||||||
| PubChem |
439194 439194 |
5893 5893 |
964 964 |
439153 439153 |
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| 1gdhA01 |
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Unbound | Unbound | Unbound | Unbound | |
| 1gdhB01 |
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Unbound | Unbound | Unbound | Unbound | |
| 1gdhA02 |
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Unbound | Unbound | Unbound | Unbound | |
| 1gdhB02 |
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Unbound | Unbound | Unbound | Unbound | |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P36234 | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1gdhA01 |
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| 1gdhB01 |
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| 1gdhA02 |
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|
ARG 240;GLU 269;HIS 287 | ||||
| 1gdhB02 |
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ARG 240;GLU 269;HIS 287 | ||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[1]
|
p.1549-1551 | |
|
[5]
|
p.1133-1136, Fig.12 | 2 |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 14154 |
| Journal | J Biol Chem |
| Year | 1977 |
| Volume | 252 |
| Pages | 1539-51 |
| Authors | Dubrow R, Pizer LI |
| Title | Transient kinetic and deuterium isotope effect studies on the catalytic mechanism of phosphoglycerate dehydrogenase. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2689175 |
| Journal | Eur J Biochem |
| Year | 1989 |
| Volume | 186 |
| Pages | 355-9 |
| Authors | Van Schaftingen E, Draye JP, Van Hoof F |
| Title | Coenzyme specificity of mammalian liver D-glycerate dehydrogenase. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | CHARACTERIZATION |
| Medline ID | 90306024 |
| PubMed ID | 2114287 |
| Journal | Eur J Biochem |
| Year | 1990 |
| Volume | 190 |
| Pages | 279-84 |
| Authors | Izumi Y, Yoshida T, Kanzaki H, Toki S, Miyazaki SS, Yamada H |
| Title |
Purification and characterization of hydroxypyruvate reductase from a serine-producing methylotroph, |
| Related PDB | |
| Related UniProtKB | P36234 |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1567457 |
| Journal | Biochem Biophys Res Commun |
| Year | 1992 |
| Volume | 184 |
| Pages | 60-6 |
| Authors | Kochhar S, Hunziker PE, Leong-Morgenthaler P, Hottinger H |
| Title | Evolutionary relationship of NAD(+)-dependent D-lactate dehydrogenase: comparison of primary structure of 2-hydroxy acid dehydrogenases. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) |
| Medline ID | 94166078 |
| PubMed ID | 8120891 |
| Journal | J Mol Biol |
| Year | 1994 |
| Volume | 236 |
| Pages | 1123-40 |
| Authors | Goldberg JD, Yoshida T, Brick P |
| Title | Crystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4 A resolution. |
| Related PDB | 1gdh |
| Related UniProtKB | P36234 |
| Comments |
|---|
|
This enzyme may have a similar catalytic mechanism to that of lactate dehydrogenase (D00456 in EzCatDB), |
| Created | Updated |
|---|---|
| 2004-03-25 | 2009-02-26 |