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]

Application

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Application on EC 2.7.1.26 - riboflavin kinase

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

drug development

Homo sapiens

Q969G6

HsRFK parameters differ from those of the so far evaluated bacterial counterparts, suggesting species-specific mechanisms in RFK catalysis. Thus, HsRFK is a potential therapeutic target because of its key functions, while bacterial RFK modules are potential antimicrobial targets

759167

synthesis

2 entries

synthesis

Rattus norvegicus

-

immobilized enzyme is effective for phosphorylating riboflavin and numerous riboflavin analogs and provides a facile method for preparing exclusively other synthetic methods, the 5'-phosphates

641244

synthesis

Corynebacterium ammoniagenes

Q59263

the enzyme is used for the preparation of flavin mononucleotide (FMN) and FMN analogues from their corresponding riboflavin precursors, which is performed in a two-step procedure. After initial enzymatic conversion of riboflavin to FAD by the bifunctional FAD synthetase, the adenyl moiety of FAD is hydrolyzed with snake venom phosphodiesterase to yield FMN. The engineered FAD synthetase from Corynebacterium ammoniagenes with deleted N-terminal adenylation domain is a biocatalyst that is stable and efficient for direct and quantitative phosphorylation of riboflavin and riboflavin analogues to their corresponding FMN cofactors at preparative-scale

739570