Jump to content

Riboflavin phosphotransferase

From Wikipedia, the free encyclopedia
riboflavin phosphotransferase
Identifiers
EC no.2.7.1.42
CAS no.9026-26-0
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 riboflavin phosphotransferase (EC 2.7.1.42) is an enzyme that catalyzes the chemical reaction

alpha-D-glucose 1-phosphate + riboflavin D-glucose + FMN

Thus, the two substrates of this enzyme are alpha-D-glucose 1-phosphate and riboflavin, whereas its two products are D-glucose and FMN.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is alpha-D-glucose-1-phosphate:riboflavin 5'-phosphotransferase. Other names in common use include riboflavine phosphotransferase, glucose-1-phosphate phosphotransferase, G-1-P phosphotransferase, and D-glucose-1-phosphate:riboflavin 5'-phosphotransferase.

References

[edit]
  • Katagiri H, Yamada H, Imai K. "The transphosphorylation reactions catalyzed by glucose 1-phosphate phosphotransferases of Escherichia coli. I. Enzymic phosphorylation of riboflavine". J. Biochem. Tokyo: 1119–1126.