2.7.1.162: N-acetylhexosamine 1-kinase
This is an abbreviated version!
For detailed information about N-acetylhexosamine 1-kinase, go to the full flat file.
Word Map on EC 2.7.1.162
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2.7.1.162
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n-acetylglucosamine
-
galnac
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bifidobacteria
-
uridyltransferase
-
chemoenzymatic
-
udp-glcnac
-
longum
-
galacto-n-biose
-
milk
-
pyrophosphatase
-
5'-diphosphate
-
three-enzyme
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uridine
-
one-pot
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oligosaccharide
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infantis
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anomeric
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n-acetylgalactosamine
-
glycosyltransferases
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utp
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4-epimerase
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n-acetylglucosamine-1-phosphate
-
synthesis
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udp-n-acetylglucosamine
-
glcnac-1-p
- 2.7.1.162
- n-acetylglucosamine
- galnac
-
bifidobacteria
- uridyltransferase
-
chemoenzymatic
- udp-glcnac
- longum
- galacto-n-biose
- milk
- pyrophosphatase
- 5'-diphosphate
-
three-enzyme
- uridine
-
one-pot
- oligosaccharide
- infantis
-
anomeric
- n-acetylgalactosamine
- glycosyltransferases
- utp
-
4-epimerase
- n-acetylglucosamine-1-phosphate
- synthesis
- udp-n-acetylglucosamine
-
glcnac-1-p
Reaction
Synonyms
BLLJ_1622, hexosamine kinase, lnpB, N-acetylhexosamine 1-kinase, N-acetylhexosamine 1-phosphate kinase, N-acetylhexosamine kinase, NahK, NahKATCC15697, NahK_15697
ECTree
2.7.1.162 N-acetylhexosamine 1-kinaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.7.1.162 - N-acetylhexosamine 1-kinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D208 A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
D208A
site-directed mutagenesis, the mutant shows altered activity and kinetics compared to the wild-type enzyme
D208A/K210A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
D208A/K210L
site-directed mutagenesis, the mutant shows highly reduced activity and altered substrate specificity compared to the wild-type
D208L
site-directed mutagenesis, the mutant shows highly reduced activity and altered substrate specificity compared to the wild-type
D228A
site-directed mutagenesis, the mutant shows altered activity and kinetics compared to the wild-type enzyme
I146E
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
I146E/T231E
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
K210A
K210E
site-directed mutagenesis, the mutant shows reduced highly activity and altered substrate specificity compared to the wild-type
K210L
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
N213A
site-directed mutagenesis, the mutant shows altered activity and kinetics compared to the wild-type enzyme
Q48A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
R306A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
R306A/Y317A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
R306E
site-directed mutagenesis, the mutant shows highly reduced activity but unaltered substrate specificity compared to the wild-type
R306E/Y317F
site-directed mutagenesis, the mutant shows highly reduced activity but unaltered substrate specificity compared to the wild-type
T231 E
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Y317A
site-directed mutagenesis, the mutant shows similar activity but slightly altered substrate specificity compared to the wild-type
Y317F
site-directed mutagenesis, the mutant shows similar activity but slightly altered substrate specificity compared to the wild-type
D208A
-
site-directed mutagenesis, the mutant shows altered activity and kinetics compared to the wild-type enzyme
-
D228A
-
site-directed mutagenesis, the mutant shows altered activity and kinetics compared to the wild-type enzyme
-
K210A
-
site-directed mutagenesis, the mutant shows altered activity and kinetics compared to the wild-type enzyme
-
N213A
-
site-directed mutagenesis, the mutant shows altered activity and kinetics compared to the wild-type enzyme
-
Q48A
-
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
-
R306A
-
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
-
R306E
-
site-directed mutagenesis, the mutant shows highly reduced activity but unaltered substrate specificity compared to the wild-type
-
Y317A
-
site-directed mutagenesis, the mutant shows similar activity but slightly altered substrate specificity compared to the wild-type
-
Y317F
-
site-directed mutagenesis, the mutant shows similar activity but slightly altered substrate specificity compared to the wild-type
-
D208A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
D208E
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
D208N
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
F247A
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
H31A
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
H31V
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
I24A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
I24V
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
D208A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
-
D208N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
-
F247A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31V
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
D208A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
-
D208N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
-
F247A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31V
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
D208A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
-
D208N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
-
F247A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31V
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
D208A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
-
D208N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
-
F247A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31V
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
D208A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
-
D208N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
-
F247A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31V
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
K210A
site-directed mutagenesis, the mutant shows altered activity and kinetics compared to the wild-type enzyme
K210A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
