L-2-hydroxycarboxylate dehydrogenase (NAD+) explained
| L-2-hydroxycarboxylate dehydrogenase (NAD+) |
| Ec Number: | 1.1.1.337 |
| Cas Number: | 81210-65-3 |
L-2-hydroxycarboxylate dehydrogenase (NAD+) ((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+
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.
Notes and References
- Graupner M, Xu H, White RH . 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 . 10850983 . 94539 . 10.1128/JB.182.13.3688-3692.2000 .
- Graupner M, White RH . 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 . 11451450 . 10.1016/S0167-4838(01)00220-5 .
- Graham DE, White RH . Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics . Natural Product Reports . 19 . 2 . 133–47 . April 2002 . 12013276 . 10.1039/b103714p .
- Rein U, Gueta R, Denger K, Ruff J, Hollemeyer K, Cook AM . Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA . Microbiology . 151 . Pt 3 . 737–47 . March 2005 . 15758220 . 10.1099/mic.0.27548-0 .
