IPR023468
Riboflavin kinase
InterPro entry
Short name | Riboflavin_kinase |
Overlapping homologous superfamilies | |
family relationships |
Description
Riboflavin is converted into catalytically active cofactors (FAD and FMN) by the actions of riboflavin kinase (
2.7.1.26), which converts it into FMN, and FAD synthetase (
2.7.7.2), which adenylates FMN to FAD. Eukaryotes usually have two separate enzymes, while most prokaryotes have a single bifunctional protein that can carry out both catalyses, although exceptions occur in both cases. While eukaryotic monofunctional riboflavin kinase is orthologous to the bifunctional prokaryotic enzyme
[2], the monofunctional FAD synthetase differs from its prokaryotic counterpart, and is instead related to the PAPS-reductase family
[3]. The bacterial FAD synthetase that is part of the bifunctional enzyme has remote similarity to nucleotidyl transferases and, hence, it may be involved in the adenylylation reaction of FAD synthetases
[1].
This entry represents riboflavin kinase, which occurs as part of a bifunctional enzyme or a stand-alone enzyme.
References
1.A conserved domain in prokaryotic bifunctional FAD synthetases can potentially catalyze nucleotide transfer. Krupa A, Sandhya K, Srinivasan N, Jonnalagadda S. Trends Biochem. Sci. 28, 9-12, (2003). View articlePMID: 12517446
2.Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism. Karthikeyan S, Zhou Q, Osterman AL, Zhang H. Biochemistry 42, 12532-8, (2003). View articlePMID: 14580199
3.Over-expression in Escherichia coli, purification and characterization of isoform 2 of human FAD synthetase. Galluccio M, Brizio C, Torchetti EM, Ferranti P, Gianazza E, Indiveri C, Barile M. Protein Expr. Purif. 52, 175-81, (2007). View articlePMID: 17049878
Cross References
Contributing Member Database Entry
- PANTHER:PTHR22749
Representative structure
1nb0: Crystal Structure of Human Riboflavin Kinase