In enzymology, a L-idonate 5-dehydrogenase (EC 1.1.1.264) is an enzyme that catalyzes the chemical reaction
L-idonate 5-dehydrogenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.1.1.264 | ||||||||
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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- L-idonate NAD(P) 5-dehydrogluconate NAD(P)H H
The 3 substrates of this enzyme are L-idonate, NAD , and NADP , whereas its 4 products are 5-dehydrogluconate, NADH, NADPH, 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 L-idonate:NAD(P) oxidoreductase.
References
edit- Bausch C, Peekhaus N, Utz C, Blais T, Murray E, Lowary T, Conway T (1998). "Sequence analysis of the GntII (subsidiary) system for gluconate metabolism reveals a novel pathway for L-idonic acid catabolism in Escherichia coli". J. Bacteriol. 180 (14): 3704–10. doi:10.1128/JB.180.14.3704-3710.1998. PMC 107343. PMID 9658018.3704-10&rft.date=1998&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC107343#id-name=PMC&rft_id=info:pmid/9658018&rft_id=info:doi/10.1128/JB.180.14.3704-3710.1998&rft.aulast=Bausch&rft.aufirst=C&rft.au=Peekhaus, N&rft.au=Utz, C&rft.au=Blais, T&rft.au=Murray, E&rft.au=Lowary, T&rft.au=Conway, T&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC107343&rfr_id=info:sid/en.wikipedia.org:L-idonate 5-dehydrogenase" class="Z3988">