Riboflavin kinase

In enzymology, a riboflavin kinase (EC number|2.7.1.26) is an enzyme that catalyzes the chemical reaction

:ATP + riboflavin $ightleftharpoons$ ADP + FMN

Thus, the two substrates of this enzyme are ATP and riboflavin, whereas its two products are ADP 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 ATP:riboflavin 5'-phosphotransferase. This enzyme is also called flavokinase. This enzyme participates in riboflavin metabolism. However, archaeal riboflavin kinases are supposedly generally utilizing CTP rather than ATP as the donor nucleotide.

tructural studies

As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes PDB link|1N05, PDB link|1N06, PDB link|1N07, PDB link|1N08, PDB link|1NB0, PDB link|1NB9, PDB link|1P4M, PDB link|1Q9S, PDB link|2P3M, PDB link|2VBS, PDB link|2VBT, PDB link|2VBU and PDB link|2VBV.

References

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External links

::"The CAS registry number for this enzyme class is CAS registry|9032-82-0."

Gene Ontology (GO) codes