BRENDA - Enzyme Database
show all sequences of 2.7.1.162

Insights into the binding specificity and catalytic mechanism of N-acetylhexosamine 1-phosphate kinases through multiple reaction complexes

Wang, K.C.; Lyu, S.Y.; Liu, Y.C.; Chang, C.Y.; Wu, C.J.; Li, T.L.; Acta Crystallogr. Sect. D 70, 1401-1410 (2014)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
gene lnpB, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Bifidobacterium longum
gene lnpB, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Bifidobacterium longum subsp. infantis
Crystallization (Commentary)
Crystallization (Commentary)
Organism
purified recombinant His-tagged enzyme in complex with substrates GalNAc, GlcNAc-1P, GlcNAc/AMPPNP (a nonhydrolyzable ATP analogue) and GlcNAc-1P/ADP, hanging drop vapour diffusion method, pre-incubation of SeMet-substituted/wild-type NahK with GlcNAc (20fold excess), GalNAc (20fold excess) or GlcNAc-1P (10fold excess), and mixing of 20 mg/ml protein in 50 mM HEPES, pH 7.5, with a crystallization solution containing 20% w/v PEG 3350, 0.1 M Bis-Tris, pH 5.5, crystals of NahK-GlcNAc-AMPPNP are obtained by soaking NahK-GlcNAc crystals with 10 mM AMPPNP and 20 mM MgCl2 for 15 min, or the crystals of NahK-GlcNAc-1P-ADP by soaking NahK-GlcNAc-1P crystals with 5 mM ADP and 10 mM MgCl2 for 30 min, crystallization time is 10-14 days, 20C, X-ray diffraction structure determination and analysis at 1.72-2.15 A resolution, molecular replacement method, modelling
Bifidobacterium longum
purified recombinant His-tagged enzyme in complex with substrates GlcNAc, and GlcNAc/AMPPNP (a nonhydrolyzable ATP analogue), hanging drop vapour diffusion method, mixing of 20 mg/ml protein in 50 mM HEPES, pH 7.5, with crystallization solution containing 1.5 M Li2SO4, 0.1 M sodium acetate, pH 5.5, 2 days, crystals of the NahKATCC15697-GlcNAc-AMPPNP complex are obtained by soaking NahK-GlcNAc complex crystals with 5 mM AMPPNP and 10 mM MgCl2 for 1.5 h, 20C, X-ray diffraction structure determination and analysis at 1.47-1.90 A resolution, molecular replacement method, modelling
Bifidobacterium longum subsp. infantis
Engineering
Protein Variants
Commentary
Organism
D208 A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
D208A/K210A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
D208A/K210L
site-directed mutagenesis, the mutant shows highly reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
D208L
site-directed mutagenesis, the mutant shows highly reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
I146E
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
I146E/T231E
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
K210A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
K210E
site-directed mutagenesis, the mutant shows reduced highly activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
K210L
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
Q48A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
R306A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
R306A/Y317A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
R306E
site-directed mutagenesis, the mutant shows highly reduced activity but unaltered substrate specificity compared to the wild-type
Bifidobacterium longum
R306E/Y317F
site-directed mutagenesis, the mutant shows highly reduced activity but unaltered substrate specificity compared to the wild-type
Bifidobacterium longum
T231 E
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
Y317A
site-directed mutagenesis, the mutant shows similar activity but slightly altered substrate specificity compared to the wild-type
Bifidobacterium longum
Y317F
site-directed mutagenesis, the mutant shows similar activity but slightly altered substrate specificity compared to the wild-type
Bifidobacterium longum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
summary of ITC analysis of wild-type NahK and mutants
Bifidobacterium longum
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required, binding structure, overview
Bifidobacterium longum
Mg2+
required, binding structure, overview
Bifidobacterium longum subsp. infantis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42500
-
gel-filtration and analytical ultracentrifugation
Bifidobacterium longum
42500
-
gel-filtration and analytical ultracentrifugation
Bifidobacterium longum subsp. infantis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + N-acetyl-D-hexosamine
Bifidobacterium longum subsp. infantis
-
ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
-
-
?
ATP + N-acetyl-D-hexosamine
Bifidobacterium longum
-
ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
-
-
?
ATP + N-acetyl-D-hexosamine
Bifidobacterium longum subsp. infantis ATCC 15697
-
ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Bifidobacterium longum
E8MF12
gene lnpB
-
Bifidobacterium longum JCM 1217
E8MF12
gene lnpB
-
Bifidobacterium longum subsp. infantis
-
gene lnpB
-
Bifidobacterium longum subsp. infantis ATCC 15697
-
gene lnpB
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Bifidobacterium longum
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Bifidobacterium longum subsp. infantis
Reaction
Reaction
Commentary
Organism
Reaction ID
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
Bifidobacterium longum
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
Bifidobacterium longum subsp. infantis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
ATP + D-galactosamine
low activity
737343
Bifidobacterium longum
ADP + D-galactosamine 1-phosphate
-
-
-
?
ATP + D-galactosamine
low activity
737343
Bifidobacterium longum JCM 1217
ADP + D-galactosamine 1-phosphate
-
-
-
?
ATP + D-galactose
low activity
737343
Bifidobacterium longum
ADP + D-galactose 1-phosphate
-
-
-
?
ATP + D-galactose
low activity
737343
Bifidobacterium longum JCM 1217
ADP + D-galactose 1-phosphate
-
-
-
?
ATP + D-glucosamine
-
737343
Bifidobacterium longum
ADP + D-glucosamine 1-phosphate
-
-
-
?
ATP + D-glucose
low activity
737343
Bifidobacterium longum
ADP + D-glucose 1-phosphate
-
-
-
?
ATP + D-mannosamine
-
737343
Bifidobacterium longum
ADP + alpha-D-mannosamine 1-phosphate
-
-
-
?
ATP + mannose
-
737343
Bifidobacterium longum
ADP + mannose 1-phosphate
-
-
-
?
ATP + N-acetyl-D-galactosamine
-
737343
Bifidobacterium longum subsp. infantis
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-galactosamine
best substrate
737343
Bifidobacterium longum
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-galactosamine
best substrate
737343
Bifidobacterium longum JCM 1217
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-galactosamine
-
737343
Bifidobacterium longum subsp. infantis ATCC 15697
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
-
737343
Bifidobacterium longum subsp. infantis
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
high activity
737343
Bifidobacterium longum
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
high activity
737343
Bifidobacterium longum JCM 1217
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
-
737343
Bifidobacterium longum subsp. infantis ATCC 15697
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-hexosamine
-
737343
Bifidobacterium longum subsp. infantis
ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-hexosamine
-
737343
Bifidobacterium longum
ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-hexosamine
-
737343
Bifidobacterium longum subsp. infantis ATCC 15697
ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-mannosamine
low activity
737343
Bifidobacterium longum
ADP + N-acetyl-alpha-D-mannosamine 1-phosphate
-
-
-
?
additional information
substrate binding structures, overview
737343
Bifidobacterium longum subsp. infantis
?
-
-
-
-
additional information
substrate binding structures, overview. No activity with glucuronic acid, galacturonic acid, 6-azidoglucose, 6-GlcNAc, 3-glucosamine, 4-glucosamine, and 6-glucosamine
737343
Bifidobacterium longum
?
-
-
-
-
additional information
substrate binding structures, overview. No activity with glucuronic acid, galacturonic acid, 6-azidoglucose, 6-GlcNAc, 3-glucosamine, 4-glucosamine, and 6-glucosamine
737343
Bifidobacterium longum JCM 1217
?
-
-
-
-
additional information
substrate binding structures, overview
737343
Bifidobacterium longum subsp. infantis ATCC 15697
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
monomer
1 * 42500, SDS-PAGE
Bifidobacterium longum
monomer
1 * 42500, SDS-PAGE, enzyme NahK is a monomer in solution, and its polypeptide folds in a crescent-like architecture subdivided into two domains by a deep cleft. The N- and C-terminal domains of NahK comprise residues 1-103 and 117-359, respectively. The N-terminal domain contains a characteristic five-stranded antiparallel beta-sheet flanked by two alpha-helices
Bifidobacterium longum subsp. infantis
More
enzyme NahK is a monomer in solution, and its polypeptide folds in a crescent-like architecture subdivided into two domains by a deep cleft. The N- and C-terminal domains of NahK comprise residues 1-103 and 117-359, respectively. The N-terminal domain contains a characteristic five-stranded antiparallel beta-sheet flanked by two alpha-helices
Bifidobacterium longum
Synonyms
Synonyms
Commentary
Organism
hexosamine kinase
-
Bifidobacterium longum subsp. infantis
hexosamine kinase
-
Bifidobacterium longum
N-acetylhexosamine 1-phosphate kinase
-
Bifidobacterium longum subsp. infantis
N-acetylhexosamine 1-phosphate kinase
-
Bifidobacterium longum
NahK
-
Bifidobacterium longum subsp. infantis
NahK
-
Bifidobacterium longum
NahKATCC15697
-
Bifidobacterium longum subsp. infantis
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Bifidobacterium longum
37
-
assay at
Bifidobacterium longum subsp. infantis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Bifidobacterium longum
8
-
assay at
Bifidobacterium longum subsp. infantis
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
ATP/ADP binding structures, overview
Bifidobacterium longum
ATP
ATP/ADP binding structures, overview
Bifidobacterium longum subsp. infantis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene lnpB, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Bifidobacterium longum
gene lnpB, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Bifidobacterium longum subsp. infantis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
ATP/ADP binding structures, overview
Bifidobacterium longum
ATP
ATP/ADP binding structures, overview
Bifidobacterium longum subsp. infantis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant His-tagged enzyme in complex with substrates GalNAc, GlcNAc-1P, GlcNAc/AMPPNP (a nonhydrolyzable ATP analogue) and GlcNAc-1P/ADP, hanging drop vapour diffusion method, pre-incubation of SeMet-substituted/wild-type NahK with GlcNAc (20fold excess), GalNAc (20fold excess) or GlcNAc-1P (10fold excess), and mixing of 20 mg/ml protein in 50 mM HEPES, pH 7.5, with a crystallization solution containing 20% w/v PEG 3350, 0.1 M Bis-Tris, pH 5.5, crystals of NahK-GlcNAc-AMPPNP are obtained by soaking NahK-GlcNAc crystals with 10 mM AMPPNP and 20 mM MgCl2 for 15 min, or the crystals of NahK-GlcNAc-1P-ADP by soaking NahK-GlcNAc-1P crystals with 5 mM ADP and 10 mM MgCl2 for 30 min, crystallization time is 10-14 days, 20C, X-ray diffraction structure determination and analysis at 1.72-2.15 A resolution, molecular replacement method, modelling
Bifidobacterium longum
purified recombinant His-tagged enzyme in complex with substrates GlcNAc, and GlcNAc/AMPPNP (a nonhydrolyzable ATP analogue), hanging drop vapour diffusion method, mixing of 20 mg/ml protein in 50 mM HEPES, pH 7.5, with crystallization solution containing 1.5 M Li2SO4, 0.1 M sodium acetate, pH 5.5, 2 days, crystals of the NahKATCC15697-GlcNAc-AMPPNP complex are obtained by soaking NahK-GlcNAc complex crystals with 5 mM AMPPNP and 10 mM MgCl2 for 1.5 h, 20C, X-ray diffraction structure determination and analysis at 1.47-1.90 A resolution, molecular replacement method, modelling
Bifidobacterium longum subsp. infantis
Engineering (protein specific)
Protein Variants
Commentary
Organism
D208 A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
D208A/K210A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
D208A/K210L
site-directed mutagenesis, the mutant shows highly reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
D208L
site-directed mutagenesis, the mutant shows highly reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
I146E
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
I146E/T231E
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
K210A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
K210E
site-directed mutagenesis, the mutant shows reduced highly activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
K210L
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
Q48A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
R306A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
R306A/Y317A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
R306E
site-directed mutagenesis, the mutant shows highly reduced activity but unaltered substrate specificity compared to the wild-type
Bifidobacterium longum
R306E/Y317F
site-directed mutagenesis, the mutant shows highly reduced activity but unaltered substrate specificity compared to the wild-type
Bifidobacterium longum
T231 E
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Bifidobacterium longum
Y317A
site-directed mutagenesis, the mutant shows similar activity but slightly altered substrate specificity compared to the wild-type
Bifidobacterium longum
Y317F
site-directed mutagenesis, the mutant shows similar activity but slightly altered substrate specificity compared to the wild-type
Bifidobacterium longum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
summary of ITC analysis of wild-type NahK and mutants
Bifidobacterium longum
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required, binding structure, overview
Bifidobacterium longum
Mg2+
required, binding structure, overview
Bifidobacterium longum subsp. infantis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42500
-
gel-filtration and analytical ultracentrifugation
Bifidobacterium longum
42500
-
gel-filtration and analytical ultracentrifugation
Bifidobacterium longum subsp. infantis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + N-acetyl-D-hexosamine
Bifidobacterium longum subsp. infantis
-
ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
-
-
?
ATP + N-acetyl-D-hexosamine
Bifidobacterium longum
-
ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
-
-
?
ATP + N-acetyl-D-hexosamine
Bifidobacterium longum subsp. infantis ATCC 15697
-
ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Bifidobacterium longum
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Bifidobacterium longum subsp. infantis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
ATP + D-galactosamine
low activity
737343
Bifidobacterium longum
ADP + D-galactosamine 1-phosphate
-
-
-
?
ATP + D-galactosamine
low activity
737343
Bifidobacterium longum JCM 1217
ADP + D-galactosamine 1-phosphate
-
-
-
?
ATP + D-galactose
low activity
737343
Bifidobacterium longum
ADP + D-galactose 1-phosphate
-
-
-
?
ATP + D-galactose
low activity
737343
Bifidobacterium longum JCM 1217
ADP + D-galactose 1-phosphate
-
-
-
?
ATP + D-glucosamine
-
737343
Bifidobacterium longum
ADP + D-glucosamine 1-phosphate
-
-
-
?
ATP + D-glucose
low activity
737343
Bifidobacterium longum
ADP + D-glucose 1-phosphate
-
-
-
?
ATP + D-mannosamine
-
737343
Bifidobacterium longum
ADP + alpha-D-mannosamine 1-phosphate
-
-
-
?
ATP + mannose
-
737343
Bifidobacterium longum
ADP + mannose 1-phosphate
-
-
-
?
ATP + N-acetyl-D-galactosamine
-
737343
Bifidobacterium longum subsp. infantis
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-galactosamine
best substrate
737343
Bifidobacterium longum
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-galactosamine
best substrate
737343
Bifidobacterium longum JCM 1217
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-galactosamine
-
737343
Bifidobacterium longum subsp. infantis ATCC 15697
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
-
737343
Bifidobacterium longum subsp. infantis
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
high activity
737343
Bifidobacterium longum
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
high activity
737343
Bifidobacterium longum JCM 1217
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
-
737343
Bifidobacterium longum subsp. infantis ATCC 15697
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-hexosamine
-
737343
Bifidobacterium longum subsp. infantis
ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-hexosamine
-
737343
Bifidobacterium longum
ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-hexosamine
-
737343
Bifidobacterium longum subsp. infantis ATCC 15697
ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-mannosamine
low activity
737343
Bifidobacterium longum
ADP + N-acetyl-alpha-D-mannosamine 1-phosphate
-
-
-
?
additional information
substrate binding structures, overview
737343
Bifidobacterium longum subsp. infantis
?
-
-
-
-
additional information
substrate binding structures, overview. No activity with glucuronic acid, galacturonic acid, 6-azidoglucose, 6-GlcNAc, 3-glucosamine, 4-glucosamine, and 6-glucosamine
737343
Bifidobacterium longum
?
-
-
-
-
additional information
substrate binding structures, overview. No activity with glucuronic acid, galacturonic acid, 6-azidoglucose, 6-GlcNAc, 3-glucosamine, 4-glucosamine, and 6-glucosamine
737343
Bifidobacterium longum JCM 1217
?
-
-
-
-
additional information
substrate binding structures, overview
737343
Bifidobacterium longum subsp. infantis ATCC 15697
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 42500, SDS-PAGE
Bifidobacterium longum
monomer
1 * 42500, SDS-PAGE, enzyme NahK is a monomer in solution, and its polypeptide folds in a crescent-like architecture subdivided into two domains by a deep cleft. The N- and C-terminal domains of NahK comprise residues 1-103 and 117-359, respectively. The N-terminal domain contains a characteristic five-stranded antiparallel beta-sheet flanked by two alpha-helices
Bifidobacterium longum subsp. infantis
More
enzyme NahK is a monomer in solution, and its polypeptide folds in a crescent-like architecture subdivided into two domains by a deep cleft. The N- and C-terminal domains of NahK comprise residues 1-103 and 117-359, respectively. The N-terminal domain contains a characteristic five-stranded antiparallel beta-sheet flanked by two alpha-helices
Bifidobacterium longum
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Bifidobacterium longum
37
-
assay at
Bifidobacterium longum subsp. infantis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Bifidobacterium longum
8
-
assay at
Bifidobacterium longum subsp. infantis
General Information
General Information
Commentary
Organism
evolution
the enzyme belongs to the sugar kinase-Hsp70-actin superfamily
Bifidobacterium longum subsp. infantis
evolution
the enzyme belongs to the sugar kinase-Hsp70-actin superfamily
Bifidobacterium longum
metabolism
the enzyme is part of the LNB/GNB pathway in bifidobacteria, overview
Bifidobacterium longum subsp. infantis
metabolism
the enzyme is part of the LNB/GNB pathway in bifidobacteria, overview
Bifidobacterium longum
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzyme belongs to the sugar kinase-Hsp70-actin superfamily
Bifidobacterium longum
evolution
the enzyme belongs to the sugar kinase-Hsp70-actin superfamily
Bifidobacterium longum subsp. infantis
metabolism
the enzyme is part of the LNB/GNB pathway in bifidobacteria, overview
Bifidobacterium longum
metabolism
the enzyme is part of the LNB/GNB pathway in bifidobacteria, overview
Bifidobacterium longum subsp. infantis
Other publictions for EC 2.7.1.162
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
739523
Li
Efficient chemoenzymatic synth ...
Escherichia coli
Prep. Biochem. Biotechnol.
47
852-859
2017
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
737770
Sato
Open-close structural change u ...
Bifidobacterium longum, Bifidobacterium longum JCM 1217
Biochim. Biophys. Acta
1854
333-340
2015
-
-
1
1
4
-
-
8
-
1
-
2
-
5
-
-
1
1
-
-
-
-
4
2
3
1
-
-
8
1
-
-
-
-
-
-
-
-
1
-
1
4
-
-
-
-
8
-
1
-
2
-
-
-
1
-
-
-
-
4
2
1
-
-
8
1
-
-
-
-
1
1
-
-
-
737343
Wang
Insights into the binding spec ...
Bifidobacterium longum, Bifidobacterium longum JCM 1217, Bifidobacterium longum subsp. infantis, Bifidobacterium longum subsp. infantis ATCC 15697
Acta Crystallogr. Sect. D
70
1401-1410
2014
-
-
2
2
17
-
-
1
-
2
2
3
-
12
-
-
2
2
-
-
-
-
24
3
7
2
-
-
-
2
-
-
2
-
-
-
-
-
2
2
2
17
-
-
-
-
1
-
2
2
3
-
-
-
2
-
-
-
-
24
3
2
-
-
-
2
-
-
-
-
4
4
-
-
-
726089
Li
Efficient enzymatic synthesis ...
Bifidobacterium longum subsp. infantis
Org. Lett.
15
5528-5530
2013
-
1
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
723238
Li
Substrate promiscuity of N-ace ...
Bifidobacterium longum, Bifidobacterium longum ATCC 55813, Bifidobacterium longum subsp. infantis, Bifidobacterium longum subsp. infantis ATCC 15697
Molecules
16
6396-6407
2011
-
-
2
-
-
-
-
8
-
4
-
-
-
11
-
-
-
-
-
-
-
-
36
-
2
-
-
-
8
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
8
-
4
-
-
-
-
-
-
-
-
-
-
36
-
-
-
-
8
2
-
-
-
-
-
-
-
8
8
702588
Cai
Substrate specificity of N-ace ...
Bifidobacterium longum
Bioorg. Med. Chem. Lett.
19
5433-5435
2009
-
-
-
-
-
-
-
-
-
1
-
1
-
1
-
-
-
-
-
-
-
-
11
-
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
11
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
703179
Cai
A chemoenzymatic route to N-ac ...
Bifidobacterium longum
Chem. Commun. (Camb. )
2009
2944-2946
2009
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
11
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
11
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
677700
Nishimoto
Identification of N-acetylhexo ...
Bifidobacterium longum, Bifidobacterium longum JCM 1217
Appl. Environ. Microbiol.
73
6444-6449
2007
1
-
1
-
-
1
-
3
-
6
-
6
-
7
-
-
1
1
-
1
13
-
17
-
4
1
-
1
3
1
-
1
3
-
-
-
1
-
1
3
-
-
1
-
-
-
3
-
6
-
6
-
-
-
1
-
1
13
-
17
-
1
-
1
3
1
-
1
-
-
-
-
-
-
-