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
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anomeric
- n-acetylgalactosamine
- glycosyltransferases
- utp
-
4-epimerase
- n-acetylglucosamine-1-phosphate
- synthesis
- udp-n-acetylglucosamine
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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
Advanced search results
Reaction
Reaction on EC 2.7.1.162 - N-acetylhexosamine 1-kinase
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ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
enzyme acts by a sequential bi bi (two substrates-two products) mechanism, with the reaction occurring after the binding of both ATP and N-acetylhexosamine
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
openclose conformational change at the active site, structure overview
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
regio- and stereoselectivity, catalytic mechanism, structure-function analysis, overview. Nucleophilic attack on the gamma-phosphate atom in a bond-breaking/bond formation manner of transfer (an SN2-like reaction). The carboxyl group of residue Asp208 within hydrogen-bond distance of C1 OH of GlcNAc/GalNAc is likely to serve as the active-site general base
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ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
regio- and stereoselectivity, catalytic mechanism, structure-function analysis, overview. Nucleophilic attack on the gamma-phosphate atom in a bond-breaking/bond formation manner of transfer (an SN2-like reaction). The carboxyl group of residue Asp208 within hydrogen-bond distance of C1 OH of GlcNAc/GalNAc is likely to serve as the active-site general base
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
the N-acetylhexosamine 1-kinase shows a concerted mechanism of two-magnesium-ion-assisted GlcNAc phosphorylation, flexibility behavior of lid motif upon substrate recognition, and water-assisted GlcNAc-1-P release
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
the N-acetylhexosamine 1-kinase shows a concerted mechanism of two-magnesium-ion-assisted GlcNAc phosphorylation, flexibility behavior of lid motif upon substrate recognition, and water-assisted GlcNAc-1-P release
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ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
the N-acetylhexosamine 1-kinase shows a concerted mechanism of two-magnesium-ion-assisted GlcNAc phosphorylation, flexibility behavior of lid motif upon substrate recognition, and water-assisted GlcNAc-1-P release
-
-
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
enzyme acts by a sequential bi bi (two substrates-two products) mechanism, with the reaction occurring after the binding of both ATP and N-acetylhexosamine
-
-
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
regio- and stereoselectivity, catalytic mechanism, structure-function analysis, overview. Nucleophilic attack on the gamma-phosphate atom in a bond-breaking/bond formation manner of transfer (an SN2-like reaction). The carboxyl group of residue Asp208 within hydrogen-bond distance of C1 OH of GlcNAc/GalNAc is likely to serve as the active-site general base
-
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ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
openclose conformational change at the active site, structure overview
-
-
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
the N-acetylhexosamine 1-kinase shows a concerted mechanism of two-magnesium-ion-assisted GlcNAc phosphorylation, flexibility behavior of lid motif upon substrate recognition, and water-assisted GlcNAc-1-P release
-
-
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
the N-acetylhexosamine 1-kinase shows a concerted mechanism of two-magnesium-ion-assisted GlcNAc phosphorylation, flexibility behavior of lid motif upon substrate recognition, and water-assisted GlcNAc-1-P release
-
-
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
regio- and stereoselectivity, catalytic mechanism, structure-function analysis, overview. Nucleophilic attack on the gamma-phosphate atom in a bond-breaking/bond formation manner of transfer (an SN2-like reaction). The carboxyl group of residue Asp208 within hydrogen-bond distance of C1 OH of GlcNAc/GalNAc is likely to serve as the active-site general base
-
-
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
the N-acetylhexosamine 1-kinase shows a concerted mechanism of two-magnesium-ion-assisted GlcNAc phosphorylation, flexibility behavior of lid motif upon substrate recognition, and water-assisted GlcNAc-1-P release
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