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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

Reaction

ATP
+
N-acetyl-alpha-D-galactosamine
=
ADP
+
N-acetyl-alpha-D-galactosamine 1-phosphate

Synonyms

GALK2, GalNAc kinase, GalNAcK, GK2, More, N-acetylgalactosamine (GalNAc)-1-phosphate kinase

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.1 Phosphotransferases with an alcohol group as acceptor
                2.7.1.157 N-acetylgalactosamine kinase

Engineering

Engineering on EC 2.7.1.157 - N-acetylgalactosamine kinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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