Biology:L-2-hydroxycarboxylate dehydrogenase (NAD+)
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Short description: Class of enzymes
| L-2-hydroxycarboxylate dehydrogenase (NAD+) | |||||||||
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| Identifiers | |||||||||
| EC number | 1.1.1.337 | ||||||||
| CAS number | 81210-65-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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L-2-hydroxycarboxylate dehydrogenase (NAD+) (EC 1.1.1.337, (R)-sulfolactate:NAD+ oxidoreductase, L-sulfolactate dehydrogenase, (R)-sulfolactate dehydrogenase, L-2-hydroxyacid dehydrogenase (NAD+), ComC) is an enzyme with systematic name (2S)-2-hydroxycarboxylate:NAD+ oxidoreductase.[1][2][3][4] This enzyme catalyses the following chemical reaction
- (2S)-2-hydroxycarboxylate + NAD+ [math]\displaystyle{ \rightleftharpoons }[/math] 2-oxocarboxylate + NADH + H+
The enzyme from the archaeon Methanocaldococcus jannaschii uses as a substrate multiple (S)-2-hydroxycarboxylates including (2R)-3-sulfolactate, (S)-malate, (S)-lactate, and (S)-2-hydroxyglutarate.
References
- ↑ "Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea". Journal of Bacteriology 182 (13): 3688–92. July 2000. doi:10.1128/JB.182.13.3688-3692.2000. PMID 10850983.
- ↑ "The first examples of (S)-2-hydroxyacid dehydrogenases catalyzing the transfer of the pro-4S hydrogen of NADH are found in the archaea". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1548 (1): 169–73. July 2001. doi:10.1016/S0167-4838(01)00220-5. PMID 11451450.
- ↑ "Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics". Natural Product Reports 19 (2): 133–47. April 2002. doi:10.1039/b103714p. PMID 12013276.
- ↑ "Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA". Microbiology 151 (Pt 3): 737–47. March 2005. doi:10.1099/mic.0.27548-0. PMID 15758220. https://kops.uni-konstanz.de/bitstream/123456789/8661/1/Dissimilation.pdf.
External links
- L-2-hydroxycarboxylate+dehydrogenase+(NAD+) at the US National Library of Medicine Medical Subject Headings (MeSH)
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