L-xylose 1-dehydrogenase

L-xylose 1-dehydrogenase
Identifiers
EC no.1.1.1.113
CAS no.37250-44-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, L-xylose 1-dehydrogenase (EC 1.1.1.113) is an enzyme that catalyzes the chemical reaction

 
 
 
H+
 
H+
 
L-Xylono-1,4-lactone
 

The two substrates of this enzyme are L-xylose and oxidised nicotinamide adenine dinucleotide phosphate (NADP+). Its products are L-xylono-1,4-lactone, reduced NADPH, and a proton.[1][2]

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-xylose:NADP+ 1-oxidoreductase. Other names in common use include L-xylose dehydrogenase, and NADPH-xylose reductase.

References

  1. ^ Enzyme 1.1.1.113 at KEGG Pathway Database.
  2. ^ Uehara K, Takeda M (1962). "L-Xylose dehydrogenase in bakers' yeast". J. Biochem. 52 (6). Tokyo: 461–463. doi:10.1093/oxfordjournals.jbchem.a127646. PMID 13995171.