2.7.1.171: protein-fructosamine 3-kinase
This is an abbreviated version!
For detailed information about protein-fructosamine 3-kinase, go to the full flat file.
Word Map on EC 2.7.1.171
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2.7.1.171
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deglycation
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erythrocyte
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fructoselysine
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protein-bound
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fn3krp
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non-enzymatic
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fn3k-related
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amadori
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endproducts
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dmf
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maillard
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protein-repairing
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glycemia
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ketoamine
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3-kinase-related
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3-deoxyglucosone
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medicine
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analysis
- 2.7.1.171
-
deglycation
- erythrocyte
- fructoselysine
-
protein-bound
- fn3krp
-
non-enzymatic
-
fn3k-related
-
amadori
-
endproducts
- dmf
-
maillard
-
protein-repairing
-
glycemia
-
ketoamine
-
3-kinase-related
- 3-deoxyglucosone
- medicine
- analysis
Reaction
Synonyms
AtFN3K, FL3P, FN3K, fructosamine 3 kinase, fructosamine 3-kinase, fructosamine-3-kinase, fructose-3-kinase, HsFN3K, ketosamine 3-kinase 1
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Subunits
Subunits on EC 2.7.1.171 - protein-fructosamine 3-kinase
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dimer
monomer
additional information
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the crystal structure of the FN3K homologue from Arabidopsis thaliana reveals that it forms an unexpected strand-exchange dimer in which the ATP-binding P-loop and adjoining beta-strands are swapped between two chains in the dimer. This dimeric configuration is characterized by strained interchain disulfide bonds that stabilize the P-loop in an extended conformation. In the AtFN3K dimer, the substrate-binding lobes are covalently tethered to create a unique interface, presumably for phosphorylating ketosamine and related substrates. AtFN3K can dimerize without the cysteines
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FN3K adopts a protein kinase fold. The wild-type and mutant enzymes show both dimeric and monomeric forms, structure-function analysis and comparisons, overview
additional information
FN3K adopts a protein kinase fold. Structure-function analysis and comparisons, overview