2-hydroxymethylglutarate dehydrogenase
| 2-hydroxymethylglutarate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.291 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a 2-hydroxymethylglutarate dehydrogenase (EC 1.1.1.291) is an enzyme that catalyzes the chemical reaction
- (S)-2-hydroxymethylglutarate + NAD+ 2-formylglutarate + NADH + H+
Thus, the two substrates of this enzyme are (S)-2-hydroxymethylglutarate and NAD+, whereas its 3 products are 2-formylglutarate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-2-hydroxymethylglutarate:NAD+ oxidoreductase. This enzyme is also called HgD.
References
- Alhapel A, Darley DJ, Wagener N, Eckel E, Elsner N, Pierik AJ (2006). "Molecular and functional analysis of nicotinate catabolism in Eubacterium barkeri". Proc. Natl. Acad. Sci. U.S.A. 103 (33): 12341–6. doi:10.1073/pnas.0601635103. PMC 1562527. PMID 16894175.
