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
ECTree
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Subunits
Subunits on EC 2.7.1.26 - riboflavin kinase
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monomer
oligomer
the enzyme forms transient oligomers during catalysis stabilized by several interactions between the RFK and FMNAT sites from neighboring protomers, which otherwise are separated in themonomeric enzyme
additional information
monomer
x * 16600, recombinant truncated C-terminal RF kinase domain, SDS-PAGE
prokaryotic FAD synthetases (FADSs) are bifunctional enzymes composed of two modules, the C-terminal module with RFK activity, and the N-terminus with FMNAT activity
additional information
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prokaryotic FAD synthetases (FADSs) are bifunctional enzymes composed of two modules, the C-terminal module with RFK activity, and the N-terminus with FMNAT activity
additional information
the RFK module is formed by residues 187-338 and shows a globular shape with a beta-barrel formed by six antiparallel strands, a terminal alpha-helix that is perpendicular to the barrel and seven loops connecting them
additional information
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the RFK module is formed by residues 187-338 and shows a globular shape with a beta-barrel formed by six antiparallel strands, a terminal alpha-helix that is perpendicular to the barrel and seven loops connecting them
additional information
structure-function analysis, apo-HsRFK structural model
additional information
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structure-function analysis, apo-HsRFK structural model
additional information
the enzyme contains a core domain with a modified Rossman-fold topology and a C-terminal extension. The substrate binding and catalytic site is located at the interface of the two domains