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Riboflavinase

From Wikipedia, the free encyclopedia
riboflavinase
Identifiers
EC no.3.5.99.1
CAS no.9024-79-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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.

References

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  • Foster JW, Yanagita T (August 1956). "A bacterial riboflavin hydrolase". The Journal of Biological Chemistry. 221 (2): 593–607. PMID 13357454.