D-arabinono-1,4-lactone oxidase | |||||||||
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Identifiers | |||||||||
EC no. | 1.1.3.37 | ||||||||
CAS no. | 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 / QuickGO | ||||||||
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In enzymology, a D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) is an enzyme that catalyzes the chemical reaction
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.
The glucose oxidase enzyme also known as notatin is an oxidoreductase that catalyses the oxidation of glucose to hydrogen peroxide and D-glucono-δ-lactone. This enzyme is produced by certain species of fungi and insects and displays antibacterial activity when oxygen and glucose are present.
L-Gulonolactone oxidase is an enzyme that produces vitamin C. It is expressed in most mammals, but is non-functional in Haplorrhini, 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.
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