EC number:1.1.1.375
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.1 Acting on the CH-OH group of donors |
| 1.1.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.1.1.375 |
|---|---|
| Description: | L-2-hydroxycarboxylate dehydrogenase (NAD(P)(+)). |
| Alternative Name: |
Lactate/malate dehydrogenase. |
| Cath: | 3.40.50.720; 3.90.110.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.1.1.375 |
| BRENDA Enzyme Link: | BRENDA 1.1.1.375 |
| KEGG Enzyme Link: | KEGG1.1.1.375 |
| BioCyc Enzyme Link: | BioCyc 1.1.1.375 |
| ExPASy Enzyme Link: | ExPASy1.1.1.375 |
| EC2PDB Enzyme Link: | EC2PDB 1.1.1.375 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.1.1.375 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.1.1.375 |
| IntEnz Enzyme Link: | IntEnz 1.1.1.375 |
| MEDLINE Enzyme Link: | MEDLINE 1.1.1.375 |
EC number:1.1.1.375
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:42768 | a (2S)-2-hydroxycarboxylate + NADP(+) = a 2-oxocarboxylate + H(+) + NADPH |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1 |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Refolding, characterization and crystal structure of (S)-malate dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix. | Kawakami R, Sakuraba H, Goda S, Tsuge H, Ohshima T | 2009 Oct | 19555779 |
| Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases. | Lee BI, Chang C, Cho SJ, Eom SH, Kim KK, Yu YG, Suh SW | 2001 Apr 13 | 11292347 |
| The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase. | Madern D | 2000 Sep | 10998181 |
| Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea. | Graupner M, Xu H, White RH | 2000 Jul | 10850983 |
| RHEA:34555 | a (2S)-2-hydroxycarboxylate + NAD(+) = a 2-oxocarboxylate + H(+) + NADH |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1 |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Refolding, characterization and crystal structure of (S)-malate dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix. | Kawakami R, Sakuraba H, Goda S, Tsuge H, Ohshima T | 2009 Oct | 19555779 |
| The first examples of (S)-2-hydroxyacid dehydrogenases catalyzing the transfer of the pro-4S hydrogen of NADH are found in the archaea. | Graupner M, White RH | 2001 Jul 9 | 11451450 |
| The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase. | Madern D | 2000 Sep | 10998181 |
| Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea. | Graupner M, Xu H, White RH | 2000 Jul | 10850983 |
| Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA. | Rein U, Gueta R, Denger K, Ruff J, Hollemeyer K, Cook AM | 2005 Mar | 15758220 |
| Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics. | Graham DE, White RH | 2002 Apr | 12013276 |