In enzymology, a 2-hydroxymethylglutarate dehydrogenase (EC 1.1.1.291) is an enzyme that catalyzes the chemical reaction
2-hydroxymethylglutarate dehydrogenase | |||||||||
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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 | ||||||||
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- (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
edit- 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. Bibcode:2006PNAS..10312341A. doi:10.1073/pnas.0601635103. PMC 1562527. PMID 16894175.12341-6&rft.date=2006&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1562527#id-name=PMC&rft_id=info:pmid/16894175&rft_id=info:doi/10.1073/pnas.0601635103&rft_id=info:bibcode/2006PNAS..10312341A&rft.aulast=Alhapel&rft.aufirst=A&rft.au=Darley, DJ&rft.au=Wagener, N&rft.au=Eckel, E&rft.au=Elsner, N&rft.au=Pierik, AJ&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1562527&rfr_id=info:sid/en.wikipedia.org:2-hydroxymethylglutarate dehydrogenase" class="Z3988">