D-arabinono-1,4-lactone oxidase

D-arabinono-1,4-lactone oxidase
Identifiers
EC number	1.1.3.37
CAS number	182372-12-9
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 / EGO
Search PMC articles PubMed articles

In enzymology, a D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) is an enzyme that catalyzes the chemical reaction

D-arabinono-1,4-lactone + O₂ $\rightleftharpoons$ D-erythro-ascorbate + H₂O₂

Thus, the two substrates of this enzyme are D-arabinono-1,4-lactone and O₂, whereas its two products are D-erythro-ascorbate and H₂O₂.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is D-arabinono-1,4-lactone:oxygen oxidoreductase. It employs one cofactor, FAD.

References

• Huh WK, Kim ST, Yang KS, Seok YJ, Hah YC, Kang SO (1994). "Characterisation of D-arabinono-1,4-lactone oxidase from Candida albicans ATCC 10231". Eur. J. Biochem. 225 (3): 1073–9. doi:10.1111/j.1432-1033.1994.1073b.x. PMID 7957197. 

This EC 1.1 enzyme-related article is a stub. You can help Wikipedia by expanding it.v · Categories: EC 1.1 stubs EC 1.1.3 Flavin enzymes Enzymes of unknown structure Wikimedia Foundation. 2010. Игры ⚽ Нужно решить контрольную? D-2-hydroxy-acid dehydrogenase Dehydrogluconate dehydrogenase Look at other dictionaries: List of EC numbers (EC 1) — This list contains a list of EC numbers for the first group, EC 1, oxidoreducatases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.EC 1.1 Acting on the CH OH …   Wikipedia 18+ © Academic, 2000-2024 Contact us: Technical Support, Advertising Dictionaries export, created on PHP, Joomla, Drupal, WordPress, MODx. Mark and share Search through all dictionaries Translate… Search Internet Share the article and excerpts Direct link … Do a right-click on the link above and select “Copy Link”