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Literature summary for 2.7.1.162 extracted from

  • Zhao, Y.; She, N.; Ma, Y.; Wang, C.; Cao, Z.
    A description of enzymatic catalysis in N-acetylhexosamine 1-kinase concerted mechanism of two-magnesium-ion-assisted GlcNAc phosphorylation, flexibility behavior of lid motif upon substrate recognition, and water-assisted GlcNAc-1-P release (2018), ACS Catal., 8, 4143-4159 .
No PubMed abstract available
Search for more literature for 2.7.1.162

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, bindin gstructure and analysis, one Mg2+ per subunit Bifidobacterium longum subsp. Longum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + N-acetyl-D-galactosamine Bifidobacterium longum subsp. Longum
-
 ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-galactosamine Bifidobacterium longum subsp. Longum JCM 1217
-
 ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-galactosamine Bifidobacterium longum subsp. Longum ATCC 15707
-
 ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-galactosamine Bifidobacterium longum subsp. Longum DSM 20219
-
 ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-galactosamine Bifidobacterium longum subsp. Longum NCTC 11818
-
 ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-galactosamine Bifidobacterium longum subsp. Longum E194b
-
 ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-glucosamine Bifidobacterium longum subsp. Longum
-
 ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-glucosamine Bifidobacterium longum subsp. Longum JCM 1217
-
 ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-glucosamine Bifidobacterium longum subsp. Longum ATCC 15707
-
 ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-glucosamine Bifidobacterium longum subsp. Longum DSM 20219
-
 ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-glucosamine Bifidobacterium longum subsp. Longum NCTC 11818
-
 ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-glucosamine Bifidobacterium longum subsp. Longum E194b
-
 ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Bifidobacterium longum subsp. Longum E8MF12
-
-
Bifidobacterium longum subsp. Longum ATCC 15707 E8MF12
-
-
Bifidobacterium longum subsp. Longum DSM 20219 E8MF12
-
-
Bifidobacterium longum subsp. Longum E194b E8MF12
-
-
Bifidobacterium longum subsp. Longum JCM 1217 E8MF12
-
-
Bifidobacterium longum subsp. Longum NCTC 11818 E8MF12
-
-

Reaction

Reaction Comment Organism Reaction ID
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 Bifidobacterium longum subsp. Longum
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + N-acetyl-D-galactosamine
-
 Bifidobacterium longum subsp. Longum ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-galactosamine
-
 Bifidobacterium longum subsp. Longum JCM 1217 ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-galactosamine
-
 Bifidobacterium longum subsp. Longum ATCC 15707 ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-galactosamine
-
 Bifidobacterium longum subsp. Longum DSM 20219 ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-galactosamine
-
 Bifidobacterium longum subsp. Longum NCTC 11818 ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-galactosamine
-
 Bifidobacterium longum subsp. Longum E194b ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-glucosamine
-
 Bifidobacterium longum subsp. Longum ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-glucosamine
-
 Bifidobacterium longum subsp. Longum JCM 1217 ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-glucosamine
-
 Bifidobacterium longum subsp. Longum ATCC 15707 ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-glucosamine
-
 Bifidobacterium longum subsp. Longum DSM 20219 ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-glucosamine
-
 Bifidobacterium longum subsp. Longum NCTC 11818 ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
ATP + N-acetyl-D-glucosamine
-
 Bifidobacterium longum subsp. Longum E194b ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?

Synonyms

Synonyms Comment Organism
BLLJ_1622 locus name Bifidobacterium longum subsp. Longum
NahK
-
 Bifidobacterium longum subsp. Longum

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Bifidobacterium longum subsp. Longum

General Information

General Information Comment Organism
additional information ab initio QM/MM MD and MM MD simulations and one-dimensional and two-dimensional free energy profiles to descript catalytic process, substrate binding structure determination and analysis, overview Bifidobacterium longum subsp. Longum
physiological function the N-acetylhexosamine 1-kinase (NahK) is the typical example of anomeric kinases acting on gluco-type substrate, which catalyzes the phosphorylation of GlcNAc or GalNAc at anomeric C1 position with ATP, playing a crucial role in Bifidobacteria metabolic pathway and biosynthesis of sugar 1-phosphates and oligosaccharides Bifidobacterium longum subsp. Longum