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Literature summary for 2.7.7.23 extracted from

  • Honda, Y.; Zang, Q.; Shimizu, Y.; Dadashipour, M.; Zhang, Z.; Kawarabayasi, Y.
    Increasing the thermostable sugar-1-phosphate nucleotidylyltransferase activities of the archaeal ST0452 protein through site saturation mutagenesis of the 97th amino acid position (2017), Appl. Environ. Microbiol., 83, e02291 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.23

Protein Variants

Protein Variants Comment Organism
G9A/K147A specific GlcNAc-1-P UTase activity of the mutant enzyme is 71.8fold lower compared to specific activity of the wild-type enzyme Sulfurisphaera tokodaii
G9A/T80A specific GlcNAc-1-P UTase activity of the mutant enzyme is 35fold lower compared to specific activity of the wild-type enzyme Sulfurisphaera tokodaii
G9A/Y97A no activity Sulfurisphaera tokodaii
G9A/Y97F specific GlcNAc-1-P UTase activity of the mutant enzyme is 14.5fold lower compared to specific activity of the wild-type enzyme Sulfurisphaera tokodaii
T80A/K147A specific GlcNAc-1-P UTase activity of the mutant enzyme is 11.09fold lower compared to specific activity of the wild-type enzyme Sulfurisphaera tokodaii
T80A/Y97A specific GlcNAc-1-P UTase activity of the mutant enzyme is 31.4fold lower compared to specific activity of the wild-type enzyme Sulfurisphaera tokodaii
T80A/Y97F specific GlcNAc-1-P UTase activity of the mutant enzyme is 25.1fold lower compared to specific activity of the wild-type enzyme Sulfurisphaera tokodaii
Y103A mutant protein shows a 24% increase in activity compared to that of the wild-type enzyme Escherichia coli
Y103N mutant protein shows a 32% increase in activity compared to that of the wild-type enzyme Escherichia coli
Y103V mutant protein shows a 30% decrease in activity compared to that of the wild-type enzyme Escherichia coli
Y97A 1.82fold increase in GlcNAc-1-P UTase activity compared to that of the wild-type enzyme Sulfurisphaera tokodaii
Y97A/K147A specific GlcNAc-1-P UTase activity of the mutant enzyme is 11.9fold lower compared to specific activity of the wild-type enzyme Sulfurisphaera tokodaii
Y97F/K147A specific GlcNAc-1-P UTaseactivity of the mutant enzyme is 5.7fold lower compared to specific activity of the wild-type enzyme Sulfurisphaera tokodaii
Y97N 4.45fold increase in GlcNAc-1-P UTase activity compared to that of the wild-type enzyme Sulfurisphaera tokodaii
Y97V 3.56fold increase in GlcNAc-1-P UTase activity compared to that of the wild-type enzyme Sulfurisphaera tokodaii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.068
-
 N-acetyl-alpha-D-glucosamine 1-phosphate wild-type enzyme, pH 7.5, 80°C Sulfurisphaera tokodaii
0.097
-
 N-acetyl-alpha-D-glucosamine 1-phosphate mutant enzyme Y97M, pH 7.5, 80°C Sulfurisphaera tokodaii
0.147
-
 N-acetyl-alpha-D-glucosamine 1-phosphate mutant enzyme Y97N, pH 7.5, 80°C Sulfurisphaera tokodaii
0.861
-
 N-acetyl-alpha-D-glucosamine 1-phosphate mutant enzyme Y97V, pH 7.5, 80°C Sulfurisphaera tokodaii

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ACC7
-
-
Escherichia coli K12 P0ACC7
-
-
Sulfurisphaera tokodaii Q975F9
-
-
Sulfurisphaera tokodaii DSM 16993 Q975F9
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli
-
 Sulfurisphaera tokodaii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 Escherichia coli diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 Sulfurisphaera tokodaii diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 Sulfurisphaera tokodaii DSM 16993 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 Escherichia coli K12 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?

Synonyms

Synonyms Comment Organism
EcGlmU
-
 Escherichia coli
GlcNAc-1-P UTase
-
 Sulfurisphaera tokodaii
ST0452
-
 Sulfurisphaera tokodaii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli
80
-
 assay at Sulfurisphaera tokodaii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
9.97
-
 N-acetyl-alpha-D-glucosamine 1-phosphate wild-type enzyme, pH 7.5, 80°C Sulfurisphaera tokodaii
10.9
-
 N-acetyl-alpha-D-glucosamine 1-phosphate mutant enzyme Y97M, pH 7.5, 80°C Sulfurisphaera tokodaii
48.95
-
 N-acetyl-alpha-D-glucosamine 1-phosphate mutant enzyme Y97V, pH 7.5, 80°C Sulfurisphaera tokodaii
49.75
-
 N-acetyl-alpha-D-glucosamine 1-phosphate mutant enzyme Y97N, pH 7.5, 80°C Sulfurisphaera tokodaii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Sulfurisphaera tokodaii
7.5
-
 assay Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
56.9
-
 N-acetyl-alpha-D-glucosamine 1-phosphate mutant enzyme Y97V, pH 7.5, 80°C Sulfurisphaera tokodaii
112.4
-
 N-acetyl-alpha-D-glucosamine 1-phosphate mutant enzyme Y97M, pH 7.5, 80°C Sulfurisphaera tokodaii
146.6
-
 N-acetyl-alpha-D-glucosamine 1-phosphate wild-type enzyme, pH 7.5, 80°C Sulfurisphaera tokodaii
338.4
-
 N-acetyl-alpha-D-glucosamine 1-phosphate mutant enzyme Y97N, pH 7.5, 80°C Sulfurisphaera tokodaii