L-galactonolactone oxidase
From Wikipedia, the free encyclopedia
In enzymology, a L-galactonolactone oxidase (EC 1.3.3.12) is an enzyme that catalyzes the chemical reaction
- L-galactono-1,4-lactone + O2
L-ascorbate + H2O2
Thus, the two substrates of this enzyme are L-galactono-1,4-lactone and O2, whereas its two products are L-ascorbic acid and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is L-galactono-1,4-lactone:oxygen 3-oxidoreductase. This enzyme is also called L-galactono-1,4-lactone oxidase. This enzyme participates in ascorbic acid and aldaric acid metabolism. It employs one cofactor, FAD.
[edit] References
- IUBMB entry for 1.3.3.12
- BRENDA references for 1.3.3.12 (Recommended.)
- PubMed references for 1.3.3.12
- PubMed Central references for 1.3.3.12
- Google Scholar references for 1.3.3.12
- Bleeg HS, Christensen F (1982). "Biosynthesis of ascorbate in yeast. Purification of L-galactono-1,4-lactone oxidase with properties different from mammalian L-gulonolactone oxidase". Eur. J. Biochem. 127: 391–6. doi:. PMID 6754380.
[edit] External links
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- The CAS registry number for this enzyme class is 69403-13-0.

