L-gulonolactone oxidase

GULOP
Identifiers
AliasesGULOP, GULO, SCURVY, gulonolactone (L-) oxidase, pseudogene
External IDsMGI: 1353434; GeneCards: GULOP; OMA:GULOP - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

NM_178747

RefSeq (protein)

n/a

NP_848862

Location (UCSC)n/aChr 14: 66.22 – 66.25 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse
L-gulonolactone oxidase
Identifiers
EC no.1.1.3.8
CAS no.9028-78-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

L-Gulonolactone oxidase (EC 1.1.3.8) is an enzyme that produces vitamin C. It is expressed in most mammals, but is non-functional in Haplorrhini (a suborder of primates, including humans), in some bats, and in guinea pigs. It catalyzes the reaction of L-gulono-1,4-lactone with oxygen to form L-xylo-hex-3-gulonolactone (2-keto-gulono-γ-lactone) and hydrogen peroxide. It uses FAD as a cofactor. The L-xylo-hex-3-gulonolactone then converts to ascorbic acid spontaneously, without enzymatic action. The structure of L-gulonolactone oxidase in rats helps identify characteristics of this enzyme.

  1. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000034450Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.