2.7.1.26: riboflavin kinase
This is an abbreviated version!
For detailed information about riboflavin kinase, go to the full flat file.
Word Map on EC 2.7.1.26
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2.7.1.26
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mononucleotide
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ammoniagenes
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fadss
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isoalloxazine
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kyphoplasty
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flavocoenzyme
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flavinogenic
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ribityl
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davawensis
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roseoflavin
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famata
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ctp-dependent
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synthesis
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drug development
- 2.7.1.26
- mononucleotide
- ammoniagenes
-
fadss
- isoalloxazine
-
kyphoplasty
-
flavocoenzyme
-
flavinogenic
-
ribityl
- davawensis
- roseoflavin
- famata
-
ctp-dependent
- synthesis
- drug development
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
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Application
Application on EC 2.7.1.26 - riboflavin kinase
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drug development
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
synthesis
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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
synthesis
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