BRENDA - Enzyme Database
show all sequences of 2.3.1.157

Characterization of the amino acid residues mediating the unique amino-sugar-1-phosphate acetyltransferase activity of the archaeal ST0452 protein

Zhang, Z.; Shimizu, Y.; Kawarabayasi, Y.; Extremophiles 19, 417-427 (2015)

Data extracted from this reference:

Application
Application
Commentary
Organism
additional information
the increase in activity induced by some substitutions and truncations may be a useful feature that can be exploited for commercial application of this enzyme
Sulfurisphaera tokodaii
Cloned(Commentary)
Cloned (Commentary)
Organism
expressed in Escherichia coli strain BL21-Codon Plus(DE3)-RIL; gene ST0452, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-Codon Plus(DE3)-RIL
Sulfurisphaera tokodaii
Engineering
Protein Variants
Commentary
Organism
H308A
site-directed mutagenesis, the mutation diminishes both amino-sugar-1-P AcTase activities of the ST0452 protein. The mutant shows 7.7% and 0.7% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively; specific activity is 0.7% compared to the wild-type enzyme
Sulfurisphaera tokodaii
K337A
site-directed mutagenesis, the mutant enzyme shows slightly decreasing GalN-1-P AcTase activity and slightly increasing GlcN-1-P AcTase activity compared to the wild-type enzyme. The mutant shows 82.6% and 137.7% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively
Sulfurisphaera tokodaii
K340A
site-directed mutagenesis, the mutant enzyme shows moderately decreasing GalN-1-P AcTase activity and moderately increasing GlcN-1-P AcTase activity compared to the wild-type enzyme. The mutant shows 63.3% and 147.1% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively; specific activity is 147.1% compared to the wild-type enzyme
Sulfurisphaera tokodaii
K377A
specific activity is 137.7% compared to the wild-type enzyme
Sulfurisphaera tokodaii
additional information
construction of expression vectors encoding a series of ST0452 C-terminal deletion mutants with hexahistidine tags at their C-termini, designated pST0452(DC005)H, pST0452(DC011)H, pST0452(DC021)H, pST0452(DC031)H, pST0452(DC041) H, pST0452(DC051)H, pST0452(DC071)H, pST0452 (DC121)H and pST0452(DC171)H. The deletion mutants retain the same tertiary structures as the wild-type ST0452 protein, but some show an altered thermostability, overview; glucosamine-1-phosphate acetyltransferase activity of C-terminal deletion mutants DC005 and DC011 (deletion of the C-terminal 5 or 11 residues of the ST0452 protein) are respectively, 4.8 and 16.8 times higher than that of the wild-type ST0452 protein. The mutant enzyme DC011 (deletion of the C-terminal 11 residues of the ST0452 protein) shows little thermal stability at 80°C. The C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein. The deletion mutant enzymes DC021, DC031, DC041, DC071 and DC121, are produced in an insoluble form or aggregated immediately after purification. Mutant enzymes DC051 and DC171 can be expressed in a soluble form. Mutant enzyme DC051 becomes completely insoluble after 5 min treatment at 60°C, while mutant enzyme DC171 is insoluble after 5 min treatment at 70 °C
Sulfurisphaera tokodaii
N331A
site-directed mutagenesis, the mutant enzyme shows highly decreasing GalN-1-P AcTase activity and decreasing GlcN-1-P AcTase activity compared to the wild-type enzyme. The mutant shows 3.1% and 46.1% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively; specific activity is 46.1% compared to the wild-type enzyme
Sulfurisphaera tokodaii
Y311A
site-directed mutagenesis, the mutant enzyme shows highly decreasing GalN-1-P AcTase activity and increasing GlcN-1-P AcTase activity compared to the wild-type enzyme. The mutant shows 3.3% and 118.4% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively; specific activity is 118.4% compared to the wild-type enzyme
Sulfurisphaera tokodaii
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
residues Tyr311, Lys337 and Lys340 plus C-terminal 11-residue region of the ST0452 protein enhance its GalN-1-P AcTase activity and suppress its GlcN-1-P AcTase activity, this function might be lost in bacterial enzymes
Sulfurisphaera tokodaii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.52
-
acetyl-CoA
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
Sulfurisphaera tokodaii
0.56
-
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
Sulfurisphaera tokodaii
0.59
-
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, wild-type enzyme; pH 7.5, 80°C, wild-type ST0452 protein
Sulfurisphaera tokodaii
0.63
-
acetyl-CoA
pH 7.5, 80°C, wild-type enzyme; pH 7.5, 80°C, wild-type ST0452 protein
Sulfurisphaera tokodaii
0.66
-
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
Sulfurisphaera tokodaii
0.84
-
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
Sulfurisphaera tokodaii
1.55
-
acetyl-CoA
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein
Sulfurisphaera tokodaii
1.69
-
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein
Sulfurisphaera tokodaii
1.71
-
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, wild-type ST0452 protein
Sulfurisphaera tokodaii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Sulfurisphaera tokodaii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
acetyl-CoA + alpha-D-galactosamine 1-phosphate
Sulfurisphaera tokodaii
-
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
?
acetyl-CoA + alpha-D-galactosamine 1-phosphate
Sulfurisphaera tokodaii 7
-
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
?
acetyl-CoA + alpha-D-galactosamine 1-phosphate
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
Sulfurisphaera tokodaii
-
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
Sulfurisphaera tokodaii 7
-
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Sulfurisphaera tokodaii
Q975F9
-
-
Sulfurisphaera tokodaii 7
Q975F9
-
-
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
Q975F9
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Sulfurisphaera tokodaii
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.35
-
pH 7.5, 80°C, mutant enzyme H308A
Sulfurisphaera tokodaii
3
8
alpha-D-galactosamine 1-phosphate substrate, pH 7.5, 80°C, recombinant mutant D005 protein
Sulfurisphaera tokodaii
23.1
-
pH 7.5, 80°C, mutant enzyme N331A
Sulfurisphaera tokodaii
29.6
-
alpha-D-galactosamine 1-phosphate aubstrate, pH 7.5, 80°C, recombinant mutant D011 protein
Sulfurisphaera tokodaii
47.6
-
alpha-D-galactosamine 1-phosphate aubstrate, pH 7.5, 80°C, recombinant wild-type ST0452 protein
Sulfurisphaera tokodaii
50
-
pH 7.5, 80°C, wild-type enzyme enzyme
Sulfurisphaera tokodaii
59.2
-
pH 7.5, 80°C, mutant enzyme Y311A
Sulfurisphaera tokodaii
67.4
-
alpha-D-glucosamine 1-phosphate substrate, pH 7.5, 80°C, recombinant wild-type ST0452 protein
Sulfurisphaera tokodaii
68.9
-
pH 7.5, 80°C, mutant enzyme K337A
Sulfurisphaera tokodaii
73.5
-
pH 7.5, 80°C, mutant enzyme K340A
Sulfurisphaera tokodaii
323.5
-
alpha-D-glucosamine 1-phosphate substrate, pH 7.5, 80°C, recombinant mutant D005 protein
Sulfurisphaera tokodaii
1131
-
alpha-D-glucosamine 1-phosphate aubstrate, pH 7.5, 80°C, recombinant mutant D011 protein
Sulfurisphaera tokodaii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
acetyl-CoA + alpha-D-galactosamine 1-phosphate
-
729696
Sulfurisphaera tokodaii
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-galactosamine 1-phosphate
-
729696
Sulfurisphaera tokodaii 7
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-galactosamine 1-phosphate
-
729696
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
-
729696
Sulfurisphaera tokodaii
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
-
729696
Sulfurisphaera tokodaii 7
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
-
729696
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
additional information
the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity. The ST0452 protein can catalyze the acetylation of both GlcN-1-P and GalN-1-P, while GalN-1-P AcTase activity is not detected in bacterial enzymes
729696
Sulfurisphaera tokodaii
?
-
-
-
-
additional information
the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity. The ST0452 protein can catalyze the acetylation of both GlcN-1-P and GalN-1-P, while GalN-1-P AcTase activity is not detected in bacterial enzymes
729696
Sulfurisphaera tokodaii 7
?
-
-
-
-
additional information
the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity. The ST0452 protein can catalyze the acetylation of both GlcN-1-P and GalN-1-P, while GalN-1-P AcTase activity is not detected in bacterial enzymes
729696
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
More
the enzyme contains the the N-terminal nucleotidylyltransferase domain (residues 1–210) and the C-terminal acetyltransferase domain (residues 211–401), respectively. Comparisons of the crystal structures of the ST0452 protein, PDB ID GGO, and Escherichia coli protein EcGlmU2, PDB ID 2OI5, comparison with ST0452 mutant enzymes, overview. Despite the structural similarities between the N- and C-termini of the ST0452 protein and those of Escherichia coli EcGlmU, the thermostabilities of the two proteins differ greatly, as EcGlmU is a mesophilic enzyme. The structures of these proteins do not correlate directly with their thermostability. The distance between the GlcN-1-P AcTase and GlcNAc-1-P UTase catalytic centers is smaller in the ST0452 protein than the mesophilic bacterial GlmU
Sulfurisphaera tokodaii
trimer
the C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein
Sulfurisphaera tokodaii
Synonyms
Synonyms
Commentary
Organism
amino-sugar-1-P AcTase
-
Sulfurisphaera tokodaii
amino-sugar-1-phosphate acetyltransferase
-
Sulfurisphaera tokodaii
galactosamine-1-phosphate acetyltransferase
-
Sulfurisphaera tokodaii
GalN-1-P AcTase
-
Sulfurisphaera tokodaii
GlcN-1-P AcTase
-
Sulfurisphaera tokodaii
glucosamine-1-phosphate acetyltransferase
-
Sulfurisphaera tokodaii
ST0452
-
Sulfurisphaera tokodaii
ST0452 protein
-
Sulfurisphaera tokodaii
STK_04520
locus name
Sulfurisphaera tokodaii
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
80
-
assay at
Sulfurisphaera tokodaii
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
80
-
mutant enzyme DC005 shows the same thermostability as wild-type ST0452 protein, whereas mutant enzyme DC011 denatures and becomes insoluble by 5-min treatment at 80 °C. The C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein
Sulfurisphaera tokodaii
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
12.6
-
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
Sulfurisphaera tokodaii
17.9
-
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
Sulfurisphaera tokodaii
69.7
-
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, wild-type ST0452 protein
Sulfurisphaera tokodaii
123.2
-
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, wild-type enzyme; pH 7.5, 80°C, wild-type ST0452 protein
Sulfurisphaera tokodaii
490.6
-
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
Sulfurisphaera tokodaii
2311
-
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein
Sulfurisphaera tokodaii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Sulfurisphaera tokodaii
Cofactor
Cofactor
Commentary
Organism
Structure
acetyl-CoA
-
Sulfurisphaera tokodaii
Application (protein specific)
Application
Commentary
Organism
additional information
the increase in activity induced by some substitutions and truncations may be a useful feature that can be exploited for commercial application of this enzyme
Sulfurisphaera tokodaii
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli strain BL21-Codon Plus(DE3)-RIL; gene ST0452, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-Codon Plus(DE3)-RIL
Sulfurisphaera tokodaii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
acetyl-CoA
-
Sulfurisphaera tokodaii
Engineering (protein specific)
Protein Variants
Commentary
Organism
H308A
site-directed mutagenesis, the mutation diminishes both amino-sugar-1-P AcTase activities of the ST0452 protein. The mutant shows 7.7% and 0.7% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively; specific activity is 0.7% compared to the wild-type enzyme
Sulfurisphaera tokodaii
K337A
site-directed mutagenesis, the mutant enzyme shows slightly decreasing GalN-1-P AcTase activity and slightly increasing GlcN-1-P AcTase activity compared to the wild-type enzyme. The mutant shows 82.6% and 137.7% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively
Sulfurisphaera tokodaii
K340A
site-directed mutagenesis, the mutant enzyme shows moderately decreasing GalN-1-P AcTase activity and moderately increasing GlcN-1-P AcTase activity compared to the wild-type enzyme. The mutant shows 63.3% and 147.1% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively; specific activity is 147.1% compared to the wild-type enzyme
Sulfurisphaera tokodaii
K377A
specific activity is 137.7% compared to the wild-type enzyme
Sulfurisphaera tokodaii
additional information
construction of expression vectors encoding a series of ST0452 C-terminal deletion mutants with hexahistidine tags at their C-termini, designated pST0452(DC005)H, pST0452(DC011)H, pST0452(DC021)H, pST0452(DC031)H, pST0452(DC041) H, pST0452(DC051)H, pST0452(DC071)H, pST0452 (DC121)H and pST0452(DC171)H. The deletion mutants retain the same tertiary structures as the wild-type ST0452 protein, but some show an altered thermostability, overview; glucosamine-1-phosphate acetyltransferase activity of C-terminal deletion mutants DC005 and DC011 (deletion of the C-terminal 5 or 11 residues of the ST0452 protein) are respectively, 4.8 and 16.8 times higher than that of the wild-type ST0452 protein. The mutant enzyme DC011 (deletion of the C-terminal 11 residues of the ST0452 protein) shows little thermal stability at 80°C. The C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein. The deletion mutant enzymes DC021, DC031, DC041, DC071 and DC121, are produced in an insoluble form or aggregated immediately after purification. Mutant enzymes DC051 and DC171 can be expressed in a soluble form. Mutant enzyme DC051 becomes completely insoluble after 5 min treatment at 60°C, while mutant enzyme DC171 is insoluble after 5 min treatment at 70 °C
Sulfurisphaera tokodaii
N331A
site-directed mutagenesis, the mutant enzyme shows highly decreasing GalN-1-P AcTase activity and decreasing GlcN-1-P AcTase activity compared to the wild-type enzyme. The mutant shows 3.1% and 46.1% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively; specific activity is 46.1% compared to the wild-type enzyme
Sulfurisphaera tokodaii
Y311A
site-directed mutagenesis, the mutant enzyme shows highly decreasing GalN-1-P AcTase activity and increasing GlcN-1-P AcTase activity compared to the wild-type enzyme. The mutant shows 3.3% and 118.4% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively; specific activity is 118.4% compared to the wild-type enzyme
Sulfurisphaera tokodaii
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
residues Tyr311, Lys337 and Lys340 plus C-terminal 11-residue region of the ST0452 protein enhance its GalN-1-P AcTase activity and suppress its GlcN-1-P AcTase activity, this function might be lost in bacterial enzymes
Sulfurisphaera tokodaii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.52
-
acetyl-CoA
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
Sulfurisphaera tokodaii
0.56
-
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
Sulfurisphaera tokodaii
0.59
-
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, wild-type enzyme; pH 7.5, 80°C, wild-type ST0452 protein
Sulfurisphaera tokodaii
0.63
-
acetyl-CoA
pH 7.5, 80°C, wild-type enzyme; pH 7.5, 80°C, wild-type ST0452 protein
Sulfurisphaera tokodaii
0.66
-
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
Sulfurisphaera tokodaii
0.84
-
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
Sulfurisphaera tokodaii
1.55
-
acetyl-CoA
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein
Sulfurisphaera tokodaii
1.69
-
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein
Sulfurisphaera tokodaii
1.71
-
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, wild-type ST0452 protein
Sulfurisphaera tokodaii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Sulfurisphaera tokodaii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
acetyl-CoA + alpha-D-galactosamine 1-phosphate
Sulfurisphaera tokodaii
-
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
?
acetyl-CoA + alpha-D-galactosamine 1-phosphate
Sulfurisphaera tokodaii 7
-
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
?
acetyl-CoA + alpha-D-galactosamine 1-phosphate
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
Sulfurisphaera tokodaii
-
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
Sulfurisphaera tokodaii 7
-
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Sulfurisphaera tokodaii
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.35
-
pH 7.5, 80°C, mutant enzyme H308A
Sulfurisphaera tokodaii
3
8
alpha-D-galactosamine 1-phosphate substrate, pH 7.5, 80°C, recombinant mutant D005 protein
Sulfurisphaera tokodaii
23.1
-
pH 7.5, 80°C, mutant enzyme N331A
Sulfurisphaera tokodaii
29.6
-
alpha-D-galactosamine 1-phosphate aubstrate, pH 7.5, 80°C, recombinant mutant D011 protein
Sulfurisphaera tokodaii
47.6
-
alpha-D-galactosamine 1-phosphate aubstrate, pH 7.5, 80°C, recombinant wild-type ST0452 protein
Sulfurisphaera tokodaii
50
-
pH 7.5, 80°C, wild-type enzyme enzyme
Sulfurisphaera tokodaii
59.2
-
pH 7.5, 80°C, mutant enzyme Y311A
Sulfurisphaera tokodaii
67.4
-
alpha-D-glucosamine 1-phosphate substrate, pH 7.5, 80°C, recombinant wild-type ST0452 protein
Sulfurisphaera tokodaii
68.9
-
pH 7.5, 80°C, mutant enzyme K337A
Sulfurisphaera tokodaii
73.5
-
pH 7.5, 80°C, mutant enzyme K340A
Sulfurisphaera tokodaii
323.5
-
alpha-D-glucosamine 1-phosphate substrate, pH 7.5, 80°C, recombinant mutant D005 protein
Sulfurisphaera tokodaii
1131
-
alpha-D-glucosamine 1-phosphate aubstrate, pH 7.5, 80°C, recombinant mutant D011 protein
Sulfurisphaera tokodaii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
acetyl-CoA + alpha-D-galactosamine 1-phosphate
-
729696
Sulfurisphaera tokodaii
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-galactosamine 1-phosphate
-
729696
Sulfurisphaera tokodaii 7
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-galactosamine 1-phosphate
-
729696
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
-
729696
Sulfurisphaera tokodaii
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
-
729696
Sulfurisphaera tokodaii 7
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
-
729696
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
additional information
the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity. The ST0452 protein can catalyze the acetylation of both GlcN-1-P and GalN-1-P, while GalN-1-P AcTase activity is not detected in bacterial enzymes
729696
Sulfurisphaera tokodaii
?
-
-
-
-
additional information
the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity. The ST0452 protein can catalyze the acetylation of both GlcN-1-P and GalN-1-P, while GalN-1-P AcTase activity is not detected in bacterial enzymes
729696
Sulfurisphaera tokodaii 7
?
-
-
-
-
additional information
the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity. The ST0452 protein can catalyze the acetylation of both GlcN-1-P and GalN-1-P, while GalN-1-P AcTase activity is not detected in bacterial enzymes
729696
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
the enzyme contains the the N-terminal nucleotidylyltransferase domain (residues 1–210) and the C-terminal acetyltransferase domain (residues 211–401), respectively. Comparisons of the crystal structures of the ST0452 protein, PDB ID GGO, and Escherichia coli protein EcGlmU2, PDB ID 2OI5, comparison with ST0452 mutant enzymes, overview. Despite the structural similarities between the N- and C-termini of the ST0452 protein and those of Escherichia coli EcGlmU, the thermostabilities of the two proteins differ greatly, as EcGlmU is a mesophilic enzyme. The structures of these proteins do not correlate directly with their thermostability. The distance between the GlcN-1-P AcTase and GlcNAc-1-P UTase catalytic centers is smaller in the ST0452 protein than the mesophilic bacterial GlmU
Sulfurisphaera tokodaii
trimer
the C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein
Sulfurisphaera tokodaii
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
80
-
assay at
Sulfurisphaera tokodaii
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
80
-
mutant enzyme DC005 shows the same thermostability as wild-type ST0452 protein, whereas mutant enzyme DC011 denatures and becomes insoluble by 5-min treatment at 80 °C. The C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein
Sulfurisphaera tokodaii
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
12.6
-
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
Sulfurisphaera tokodaii
17.9
-
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
Sulfurisphaera tokodaii
69.7
-
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, wild-type ST0452 protein
Sulfurisphaera tokodaii
123.2
-
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, wild-type enzyme; pH 7.5, 80°C, wild-type ST0452 protein
Sulfurisphaera tokodaii
490.6
-
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
Sulfurisphaera tokodaii
2311
-
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein
Sulfurisphaera tokodaii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Sulfurisphaera tokodaii
General Information
General Information
Commentary
Organism
additional information
the C-terminal tail region of the ST0452 protein might be important for recognition of the multiple substrates for amino-sugar-1-P AcTase activity. The ST0452 protein contains only two Cys residues, it is unlikely that Cys-Cys bonds contribute to its thermostability. Residue Asn331 in the ST0452 protein is essential for the GalN-1-P AcTase activity, but it is much less important and not essential for the GlcN-1-P AcTase activity. The C-terminal residues of the ST0452 protein enhance the turnover rate of its GalN-1-P AcTase catalytic activity and slightly suppress substrate binding. Residue H308 is essential for both amino-sugar-1-P AcTase activities of the ST0452 protein
Sulfurisphaera tokodaii
physiological function
the archaeal enzyme's high GalN-1-P AcTase activity, which is not detected on the bacterial and eukaryotic similar enzymes, supports the production of the UDP-GalNAc in archaeal cells
Sulfurisphaera tokodaii
General Information (protein specific)
General Information
Commentary
Organism
additional information
the C-terminal tail region of the ST0452 protein might be important for recognition of the multiple substrates for amino-sugar-1-P AcTase activity. The ST0452 protein contains only two Cys residues, it is unlikely that Cys-Cys bonds contribute to its thermostability. Residue Asn331 in the ST0452 protein is essential for the GalN-1-P AcTase activity, but it is much less important and not essential for the GlcN-1-P AcTase activity. The C-terminal residues of the ST0452 protein enhance the turnover rate of its GalN-1-P AcTase catalytic activity and slightly suppress substrate binding. Residue H308 is essential for both amino-sugar-1-P AcTase activities of the ST0452 protein
Sulfurisphaera tokodaii
physiological function
the archaeal enzyme's high GalN-1-P AcTase activity, which is not detected on the bacterial and eukaryotic similar enzymes, supports the production of the UDP-GalNAc in archaeal cells
Sulfurisphaera tokodaii
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
19.6
-
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
Sulfurisphaera tokodaii
21.5
-
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
Sulfurisphaera tokodaii
40.8
-
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, wild-type ST0452 protein
Sulfurisphaera tokodaii
211
-
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, wild-type enzyme; pH 7.5, 80°C, wild-type ST0452 protein
Sulfurisphaera tokodaii
869.2
-
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
Sulfurisphaera tokodaii
1489
-
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein
Sulfurisphaera tokodaii
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
19.6
-
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
Sulfurisphaera tokodaii
21.5
-
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
Sulfurisphaera tokodaii
40.8
-
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, wild-type ST0452 protein
Sulfurisphaera tokodaii
211
-
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, wild-type enzyme; pH 7.5, 80°C, wild-type ST0452 protein
Sulfurisphaera tokodaii
869.2
-
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
Sulfurisphaera tokodaii
1489
-
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein
Sulfurisphaera tokodaii
Other publictions for EC 2.3.1.157
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)
746844
Honda
Improvement of ST0452 N-acety ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993
Appl. Environ. Microbiol.
84
e002213-18
2018
-
-
1
1
2
-
-
-
-
-
-
-
-
10
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
736517
Sharma
Escherichia coli N-acetylgluco ...
Escherichia coli, Escherichia coli ATCC 25922
J. Biomol. Screen.
21
342-353
2016
-
-
1
-
-
-
3
-
-
1
-
2
-
10
-
-
1
-
-
-
-
-
2
-
2
1
-
-
-
1
-
-
1
4
-
2
-
-
1
1
-
-
-
2
4
4
-
-
1
-
2
-
-
-
1
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
737096
Dziadek
Mycobacterium tuberculosis Ats ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618, Mycobacterium tuberculosis H37Rv
PLoS ONE
11
e0148030
2016
-
1
1
-
1
-
-
-
-
-
-
3
-
15
-
-
1
-
-
-
-
-
6
-
3
-
-
-
-
-
-
-
1
-
-
-
-
1
1
1
-
1
-
-
-
-
-
-
-
-
3
-
-
-
1
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
729696
Zhang
Characterization of the amino ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7, Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
Extremophiles
19
417-427
2015
-
1
1
-
7
-
1
9
-
1
-
6
-
8
-
-
1
-
-
-
12
-
9
2
9
1
-
1
6
1
-
-
1
-
-
-
-
1
1
1
-
7
-
-
1
-
9
-
1
-
6
-
-
-
1
-
-
12
-
9
2
1
-
1
6
1
-
-
-
-
2
2
-
6
6
735518
Sharma
Identification and characteriz ...
Escherichia coli, Escherichia coli ATCC 25922, Haemophilus influenzae, Haemophilus influenzae ATCC 51907
Appl. Microbiol. Biotechnol.
100
3071-3085
2015
-
-
1
-
-
-
15
-
-
-
-
8
-
12
-
-
1
-
-
-
-
-
10
-
5
2
-
-
-
2
-
-
2
2
-
11
-
-
1
2
-
-
-
12
17
2
-
-
-
-
8
-
-
-
1
-
-
-
-
10
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
735569
Patin
Purification and biochemical c ...
Yersinia pestis, Yersinia pestis YPIII, Yersinia pseudotuberculosis, Yersinia pseudotuberculosis YPIII
Arch. Microbiol.
197
371-378
2015
1
-
2
-
1
-
2
4
-
2
-
2
-
6
-
-
1
-
-
-
-
-
4
2
5
1
-
-
4
1
-
-
1
-
-
-
1
-
2
1
-
1
-
-
2
-
4
-
2
-
2
-
-
-
1
-
-
-
-
4
2
1
-
-
4
1
-
-
-
-
2
2
-
-
-
737150
Soni
Depletion of M. tuberculosis G ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618, Mycobacterium tuberculosis H37Rv
PLoS Pathog.
11
e1005235
2015
-
1
1
1
-
-
2
-
-
-
-
6
-
12
-
-
-
-
-
-
-
-
6
-
2
1
-
-
-
1
-
-
1
-
-
1
-
1
1
1
1
-
-
1
2
-
-
-
-
-
6
-
-
-
-
-
-
-
-
6
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
737291
Rani
High-throughput screen identif ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Tuberculosis
95
664-677
2015
-
-
1
-
-
-
6
3
-
1
-
4
-
11
-
-
1
-
-
-
-
-
5
-
1
1
-
-
-
1
-
-
1
5
-
10
-
-
1
1
-
-
-
10
8
5
5
-
1
-
4
-
-
-
1
-
-
-
-
5
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
735396
Vithani
GlmU (N-acetylglucosamine-1-ph ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618
Acta Crystallogr. Sect. F
70
703-708
2014
-
-
1
1
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
736058
Mehra
Identification and optimizatio ...
Escherichia coli, Escherichia coli ATCC 25922
Eur. J. Med. Chem.
92
78-90
2014
-
-
-
-
-
-
12
-
-
-
-
2
-
5
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
1
-
-
1
-
-
2
-
-
-
1
-
-
-
2
14
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
719064
Green
Inhibitors of acetyltransferas ...
Escherichia coli, Haemophilus influenzae, Staphylococcus aureus, Streptococcus pneumoniae
Bioorg. Med. Chem. Lett.
22
1510-1519
2012
-
-
-
2
-
-
156
-
-
-
-
4
-
4
-
-
-
-
-
-
-
-
4
4
8
4
-
-
-
4
-
-
-
-
-
150
-
-
-
-
2
-
-
150
156
-
-
-
-
-
4
-
-
-
-
-
-
-
-
4
4
4
-
-
-
4
-
-
-
-
4
4
-
-
-
719070
Stokes
Inhibitors of the acetyltransf ...
Escherichia coli, Haemophilus influenzae, Streptococcus pneumoniae
Bioorg. Med. Chem. Lett.
22
7019-7023
2012
-
-
-
-
-
-
54
-
-
-
-
3
-
5
-
-
-
-
-
-
-
-
3
-
6
-
-
-
-
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