Riboflavinase

From Wikipedia, the free encyclopedia

In enzymology, a riboflavinase (EC 3.5.99.1) is an enzyme that catalyzes the chemical reaction

riboflavin + H₂O ribitol + lumichrome

Thus, the two substrates of this enzyme are riboflavin and H₂O, whereas its two products are ribitol and lumichrome.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is riboflavin hydrolase. This enzyme participates in riboflavin metabolism.

[edit] References

• IUBMB entry for 3.5.99.1
• BRENDA references for 3.5.99.1 (Recommended.)
• PubMed references for 3.5.99.1
• PubMed Central references for 3.5.99.1
• Google Scholar references for 3.5.99.1
• Yanagita T and Foster JW (1956). "A bacterial riboflavin hydrolase". J. Biol. Chem. 221: 593–607. 

[edit] External links

The CAS registry number for this enzyme class is 9024-79-7.

• IUBMB entry for 3.5.99.1

• KEGG entry for 3.5.99.1

• BRENDA entry for 3.5.99.1

• NiceZyme view of 3.5.99.1

• EC2PDB: PDB structures for 3.5.99.1

• PRIAM entry for 3.5.99.1

• PUMA2 entry for 3.5.99.1

• IntEnz: Integrated Enzyme entry for 3.5.99.1

• MetaCyc entry for 3.5.99.1

• Atomic-resolution structures of enzymes belonging to this class

[edit] Gene Ontology (GO) codes

• EGO entry for GO code 0050258: riboflavinase

• AMIGO entry for GO code 0050258: riboflavinase