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Literature summary 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

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.9 Y97A specific Glc-1-P UTase activity of the mutant enzyme is 2.3fold lower than the specific activity of the mutant enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97C specific Glc-1-P UTase activity of the mutant enzyme is 1.9fold lower than the specific activity of the mutant enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97D specific Glc-1-P UTase activity of the mutant enzyme is 6.2fold lower than the specific activity of the mutant enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97E mutant enzyme shows mutant enzyme shows no activity Sulfurisphaera tokodaii
2.7.7.9 Y97F specific Glc-1-P UTase activity of the mutant enzyme is 1.2fold lower than the specific activity of the mutant enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97G specific Glc-1-P UTase activity of the mutant enzyme is 4.2fold lower than the specific activity of the mutant enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97H specific Glc-1-P UTase activity of the mutant enzyme is 2.6fold higher than the specific activity of the mutant enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97I mutant enzyme shows no activity Sulfurisphaera tokodaii
2.7.7.9 Y97K specific Glc-1-P UTase activity of the mutant enzyme is 3.7fold lower than the specific activity of the mutant enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97L specific Glc-1-P UTase activity of the mutant enzyme is 2.4fold higher than the specific activity of the mutant enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97M specific Glc-1-P UTase activity of the mutant enzyme is 2.8fold higher than the specific activity of the mutant enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97N specific Glc-1-P UTase activity of the mutant enzyme is 4.1fold higher than the specific activity of the mutant enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97Q specific Glc-1-P UTase activity of the mutant enzyme is 1.04fold higher than the specific activity of the mutant enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97R mutant enzyme shows no activity Sulfurisphaera tokodaii
2.7.7.9 Y97S specific Glc-1-P UTase activity of the mutant enzyme is 1.1fold higher than the specific activity of the mutant enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97T specific Glc-1-P UTase activity of the mutant enzyme is 4fold lower than the specific activity of the mutant enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97V specific Glc-1-P UTase activity of the mutant enzyme is 3.34fold lower than the specific activity of the mutant enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97W mutant enzyme shows no activity Sulfurisphaera tokodaii
2.7.7.23 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
2.7.7.23 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
2.7.7.23 G9A/Y97A no activity Sulfurisphaera tokodaii
2.7.7.23 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
2.7.7.23 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
2.7.7.23 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
2.7.7.23 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
2.7.7.23 Y103A mutant protein shows a 24% increase in activity compared to that of the wild-type enzyme Escherichia coli
2.7.7.23 Y103N mutant protein shows a 32% increase in activity compared to that of the wild-type enzyme Escherichia coli
2.7.7.23 Y103V mutant protein shows a 30% decrease in activity compared to that of the wild-type enzyme Escherichia coli
2.7.7.23 Y97A 1.82fold increase in GlcNAc-1-P UTase activity compared to that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 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
2.7.7.23 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
2.7.7.23 Y97N 4.45fold increase in GlcNAc-1-P UTase activity compared to that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97V 3.56fold increase in GlcNAc-1-P UTase activity compared to that of the wild-type enzyme Sulfurisphaera tokodaii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.9 1.23
-
alpha-D-glucose 1-phosphate wild-type enzyme, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 1.74
-
alpha-D-glucose 1-phosphate mutant enzyme Y97M, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 2.5 3 alpha-D-glucose 1-phosphate mutant enzyme Y97N, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 3.28
-
alpha-D-glucose 1-phosphate mutant enzyme Y97V, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 0.068
-
N-acetyl-alpha-D-glucosamine 1-phosphate wild-type enzyme, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 0.097
-
N-acetyl-alpha-D-glucosamine 1-phosphate mutant enzyme Y97M, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 0.147
-
N-acetyl-alpha-D-glucosamine 1-phosphate mutant enzyme Y97N, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 0.861
-
N-acetyl-alpha-D-glucosamine 1-phosphate mutant enzyme Y97V, pH 7.5, 80°C Sulfurisphaera tokodaii

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.9 Sulfurisphaera tokodaii Q975F9
-
-
2.7.7.9 Sulfurisphaera tokodaii DSM 16993 Q975F9
-
-
2.7.7.23 Escherichia coli P0ACC7
-
-
2.7.7.23 Escherichia coli K12 P0ACC7
-
-
2.7.7.23 Sulfurisphaera tokodaii Q975F9
-
-
2.7.7.23 Sulfurisphaera tokodaii DSM 16993 Q975F9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.9
-
Sulfurisphaera tokodaii
2.7.7.23
-
Escherichia coli
2.7.7.23
-
Sulfurisphaera tokodaii

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
2.7.7.9 Glc-1-P UTase
-
Sulfurisphaera tokodaii
2.7.7.9 ST0452
-
Sulfurisphaera tokodaii
2.7.7.23 EcGlmU
-
Escherichia coli
2.7.7.23 GlcNAc-1-P UTase
-
Sulfurisphaera tokodaii
2.7.7.23 ST0452
-
Sulfurisphaera tokodaii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.9 80
-
assay at Sulfurisphaera tokodaii
2.7.7.23 37
-
assay at Escherichia coli
2.7.7.23 80
-
assay at Sulfurisphaera tokodaii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.7.9 2.08
-
alpha-D-glucose 1-phosphate mutant enzyme Y97V, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 2.97
-
alpha-D-glucose 1-phosphate wild-type enzyme, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 14.97
-
alpha-D-glucose 1-phosphate mutant enzyme Y97M, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 38.15
-
alpha-D-glucose 1-phosphate mutant enzyme Y97N, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 9.97
-
N-acetyl-alpha-D-glucosamine 1-phosphate wild-type enzyme, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 10.9
-
N-acetyl-alpha-D-glucosamine 1-phosphate mutant enzyme Y97M, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 48.95
-
N-acetyl-alpha-D-glucosamine 1-phosphate mutant enzyme Y97V, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 49.75
-
N-acetyl-alpha-D-glucosamine 1-phosphate mutant enzyme Y97N, pH 7.5, 80°C Sulfurisphaera tokodaii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.9 7.5
-
assay atz Sulfurisphaera tokodaii
2.7.7.23 7.5
-
assay at Sulfurisphaera tokodaii
2.7.7.23 7.5
-
assay Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.7.9 0.63
-
alpha-D-glucose 1-phosphate mutant enzyme Y97V, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 2.41
-
alpha-D-glucose 1-phosphate wild-type enzyme, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 8.6
-
alpha-D-glucose 1-phosphate mutant enzyme Y97M, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 15.08
-
alpha-D-glucose 1-phosphate mutant enzyme Y97N, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 56.9
-
N-acetyl-alpha-D-glucosamine 1-phosphate mutant enzyme Y97V, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 112.4
-
N-acetyl-alpha-D-glucosamine 1-phosphate mutant enzyme Y97M, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 146.6
-
N-acetyl-alpha-D-glucosamine 1-phosphate wild-type enzyme, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 338.4
-
N-acetyl-alpha-D-glucosamine 1-phosphate mutant enzyme Y97N, pH 7.5, 80°C Sulfurisphaera tokodaii