Riboflavin phosphotransferase

In enzymology, a riboflavin phosphotransferase (EC 2.7.1.42) is an enzyme that catalyzes the chemical reaction

alpha-D-glucose 1-phosphate + riboflavin ${\displaystyle \rightleftharpoons }$ D-glucose + FMN

riboflavin phosphotransferase
Identifiers
EC no.	2.7.1.42
CAS no.	9026-26-0
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
Search PMC articles PubMed articles NCBI proteins

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.