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
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galnac
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bifidobacteria
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uridyltransferase
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chemoenzymatic
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udp-glcnac
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longum
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galacto-n-biose
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milk
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pyrophosphatase
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5'-diphosphate
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three-enzyme
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uridine
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one-pot
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oligosaccharide
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infantis
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anomeric
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n-acetylgalactosamine
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glycosyltransferases
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utp
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4-epimerase
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n-acetylglucosamine-1-phosphate
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synthesis
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udp-n-acetylglucosamine
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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
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Metals Ions
Metals Ions on EC 2.7.1.162 - N-acetylhexosamine 1-kinase
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Co2+
Mg2+
additional information
requires a divalent cation, with Mg2+ resulting in the greatest stimulation of enzyme activity
Mg2+
requirement of the second magnesium ion, the enzyme has two magnesium binding sites, Mg1 and Mg2, structure overview
Mg2+
required for catalysis, optimum for wild-type enzyme is 5 mM, for mutants H31A and F247A 10 mM
Mg2+
required, bindin gstructure and analysis, one Mg2+ per subunit
additional information
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divalent cation required for activity