2.7.1.26: riboflavin kinase

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For detailed information about riboflavin kinase, go to the full flat file.

Reaction

Synonyms

AtFMN/FHy, ATP: riboflavin kinase, ATP:riboflavin kinase, bifunctional riboflavin kinase/FMN adenylyltransferase, CaFADS, FAD synthetase, FADS, FK, flavokinase, flavokinase/FAD synthetase, flavokinase/flavin adenine dinucleotide synthetase, FMN adenylyltransferase, FMNAT, HsRFK, kinase, riboflavin, More, RFK, RibC, ribF, riboflavin kinase, riboflavin kinase/FMN adenylyltransferase, riboflavine kinase, RibR

ECTree

     2 Transferases

         2.7 Transferring phosphorus-containing groups

             2.7.1 Phosphotransferases with an alcohol group as acceptor

                2.7.1.26 riboflavin kinase

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Results	in table
4	Activating Compound
43101	AA Sequence
3	Application
1	CAS Registry Number
15	Cloned(Commentary)
4	Cofactor
6	Crystallization (Commentary)
34	Disease/ Diagnostics
16	General Information
4	General Stability
59	Inhibitors
45	kcat/KM [mM/s]
44	Ki Value [mM]
75	KM Value [mM]
2	Localization
23	Metals/Ions
12	Molecular Weight [Da]
19	Natural Substrates/ Products (Substrates)
40	Organism
10	Pathway
33	PDB ID
10	pH Optimum
2	pH Range
35	Protein Variants
16	Purification (Commentary)
3	Reaction
1	Reaction Type
40	Reference
14	Source Tissue
9	Specific Activity [micromol/min/mg]
2	Storage Stability
111	Substrates and Products (Substrate)
14	Subunits
42	Synonyms
1	Systematic Name
9	Temperature Optimum [°C]
3	Temperature Range [°C]
2	Temperature Stability [°C]
52	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 2.7.1.26 - riboflavin kinase

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SYSTEMATIC NAME

IUBMB Comments

ATP:riboflavin 5'-phosphotransferase

The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates [5]. While monofunctional riboflavin kinase is found in eukaryotes, some bacteria have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.7.2, FMN adenylyltransferase [5]. A divalent metal cation is required for activity (with different species preferring Mg2+, Mn2+ or Zn2+). In Bacillus subtilis, ATP can be replaced by other phosphate donors but with decreasing enzyme activity in the order ATP > dATP > CTP > UTP [6].