2.7.1.157: N-acetylgalactosamine kinase
This is an abbreviated version!
For detailed information about N-acetylgalactosamine kinase, go to the full flat file.
Word Map on EC 2.7.1.157
-
2.7.1.157
-
galactokinase
-
galactose
-
nalidixic
-
antimutator
-
proofreading
-
gale
-
papillation
-
mgatp
-
udp-galnac
-
udp-galactose
-
synthesis
- 2.7.1.157
- galactokinase
- galactose
-
nalidixic
-
antimutator
-
proofreading
-
gale
-
papillation
- mgatp
- udp-galnac
- udp-galactose
- synthesis
Reaction
Synonyms
GALK2, GalNAc kinase, GalNAcK, GK2, More, N-acetylgalactosamine (GalNAc)-1-phosphate kinase
ECTree
Advanced search results
Engineering
Engineering on EC 2.7.1.157 - N-acetylgalactosamine kinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
F444A
mutation in residue equivalent to residue Tyr379 of galactokinase, whose alteration dramatically enhances the substrate range of this enzyme. Mutation does not result in large changes to the specificity of the enzyme
F444C
mutation in residue equivalent to residue Tyr379 of galactokinase, whose alteration dramatically enhances the substrate range of this enzyme. Mutation does not result in large changes to the specificity of the enzyme but increases turnover rate with N-acetylgalactosamine
F444H
mutation in residue equivalent to residue Tyr379 of galactokinase, whose alteration dramatically enhances the substrate range of this enzyme. Mutation does not result in large changes to the specificity of the enzyme
F444K
mutation in residue equivalent to residue Tyr379 of galactokinase, whose alteration dramatically enhances the substrate range of this enzyme. Mutation does not result in large changes to the specificity of the enzyme
F444R
mutation in residue equivalent to residue Tyr379 of galactokinase, whose alteration dramatically enhances the substrate range of this enzyme. Mutation does not result in large changes to the specificity of the enzyme
F444S
mutation in residue equivalent to residue Tyr379 of galactokinase, whose alteration dramatically enhances the substrate range of this enzyme. Mutation does not result in large changes to the specificity of the enzyme but increases turnover rate with N-acetylgalactosamine
F444W
mutation in residue equivalent to residue Tyr379 of galactokinase, whose alteration dramatically enhances the substrate range of this enzyme. Mutation does not result in large changes to the specificity of the enzyme