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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, e02291-16 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.9 expressed in Escherichia coli BL21-CodonPlus(DE3)-RIPL cells Sulfurisphaera tokodaii
2.7.7.9 expression in Escherichia coli Sulfurisphaera tokodaii
2.7.7.23 expression in Escherichia coli Escherichia coli
2.7.7.23 expression in Escherichia coli Sulfurisphaera tokodaii
2.7.7.23 gene ST0452, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL, subcloning in Escherichia coli strain JM109 Sulfurisphaera tokodaii

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.157 Y103N mutant enzyme shows increased GlcNAc-1-P UTase activity Sulfurisphaera tokodaii
2.3.1.157 Y97A mutant enzyme exhibits the highest activity of the single-mutant proteins Sulfurisphaera tokodaii
2.7.7.9 Y97A activity is 2.3fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97A the mutant shows decreased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97C activity is 1.87fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97D activity is 6.2fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97D the mutant shows decreased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97E inactive Sulfurisphaera tokodaii
2.7.7.9 Y97F activity is 1.2fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97F the mutant shows decreased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97G activity is 4.2fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97G the mutant shows decreased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97H activity is 1.6fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97H the mutant shows increased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97I inactive Sulfurisphaera tokodaii
2.7.7.9 Y97I the mutant shows decreased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97K activity is 3.7fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97K the mutant shows decreased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97L activity is 2.4fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97L the mutant shows increased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97M activity is 2.8fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97M the mutant shows increased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97N activity is 4.1fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97N the mutant shows increased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97P inactive Sulfurisphaera tokodaii
2.7.7.9 Y97Q activity is 1.04fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97Q the mutant shows increased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97R inactive Sulfurisphaera tokodaii
2.7.7.9 Y97S activity is 1.1fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97S the mutant shows increased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97T activity is 3.96fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97T the mutant shows decreased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97V activity is 3.34fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97V the mutant shows decreased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme Sulfurisphaera tokodaii
2.7.7.9 Y97W inactive Sulfurisphaera tokodaii
2.7.7.23 G9A site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type Sulfurisphaera tokodaii
2.7.7.23 G9A/K147A activity is 71.8fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 G9A/K147A site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 G9A/T80A activity is 35fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 G9A/T80A site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 G9A/Y97A inactive mutant enzyme Sulfurisphaera tokodaii
2.7.7.23 G9A/Y97A site-directed mutagenesis, inactive mutant Sulfurisphaera tokodaii
2.7.7.23 G9A/Y97F activity is 14.5fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 G9A/Y97F site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 K147A site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type Sulfurisphaera tokodaii
2.7.7.23 additional information ST0452 proteins exhibiting a further increase in activity are created using a site saturation mutagenesis strategy at the 97th position. Kinetic analyses show that the increased activities of the mutant proteins are principally due to increased apparent kcat values. Nine double-mutant ST0452 proteins are generated with the intent of obtaining enzymes exhibiting a further increase in catalysis, but all show less than 15% of the wild-type N-acetyl-D-glucosamine-1-phosphate uridyltransferase (GlcNAc-1-P UTase) activity. The Y97A mutant exhibits the highest activity of the single-mutant proteins. Analysis of mutant ST0452 proteins generated using a site saturation mutagenesis strategy at the 97th position, overview Sulfurisphaera tokodaii
2.7.7.23 T80A site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type Sulfurisphaera tokodaii
2.7.7.23 T80A/K147A activity is 11.1fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 T80A/K147A site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 T80A/Y97A activity is 31.4fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 T80A/Y97A site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 T80A/Y97F activity is 25.1fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 T80A/Y97F site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y103A activity is 25% higher than that of the wild-type enzyme Escherichia coli
2.7.7.23 Y103N activity is 30% higher than that of the wild-type enzyme Escherichia coli
2.7.7.23 Y103N activity is 30% lower than that of the wild-type enzyme Escherichia coli
2.7.7.23 Y97A activity is 1.83fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97A site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type Sulfurisphaera tokodaii
2.7.7.23 Y97A/K147A activity is 11.9fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97A/K147A site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97C activity is 1.4fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97C site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97D activity is 1.3fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97D site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type Sulfurisphaera tokodaii
2.7.7.23 Y97E activity is 2.1fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97E site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97F activity is 1.2fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97F site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type Sulfurisphaera tokodaii
2.7.7.23 Y97F/K147A activity is 5.4fold lower than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97F/K147A site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97G activity is 1.2fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97G site-directed mutagenesis, the mutant exhibits slightly increased GlcNAc-1-P UTase activity compared to wild-type Sulfurisphaera tokodaii
2.7.7.23 Y97H activity is 2.9fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97H site-directed mutagenesis, the mutant exhibits highly increased GlcNAc-1-P UTase activity compared to wild-type Sulfurisphaera tokodaii
2.7.7.23 Y97I activity is 1.2fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97I site-directed mutagenesis, the mutant exhibits slightly increased GlcNAc-1-P UTase activity compared to wild-type Sulfurisphaera tokodaii
2.7.7.23 Y97K activity is 1.35fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97K site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type Sulfurisphaera tokodaii
2.7.7.23 Y97L activity is 1.5fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97L site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type Sulfurisphaera tokodaii
2.7.7.23 Y97M activity is 1.3fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97M site-directed mutagenesis, the mutant exhibits slightly increased GlcNAc-1-P UTase activity compared to wild-type Sulfurisphaera tokodaii
2.7.7.23 Y97N activity is 4.5fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97N site-directed mutagenesis, the mutant exhibits highly increased GlcNAc-1-P UTase activity compared to wild-type Sulfurisphaera tokodaii
2.7.7.23 Y97P activity is 1.5fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97P site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97Q activity is 2.3fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97Q site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type Sulfurisphaera tokodaii
2.7.7.23 Y97R inactive mutant enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97R site-directed mutagenesis, inactive mutant Sulfurisphaera tokodaii
2.7.7.23 Y97S activity is 1.97fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97S site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type Sulfurisphaera tokodaii
2.7.7.23 Y97T activity is 2.1fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97T site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type Sulfurisphaera tokodaii
2.7.7.23 Y97V activity is 3.6fold higher than that of the wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 Y97V site-directed mutagenesis, the mutant exhibits highly increased GlcNAc-1-P UTase activity compared to wild-type Sulfurisphaera tokodaii
2.7.7.23 Y97W inactive mutant 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 1.23
-
 alpha-D-glucose 1-phosphate wild type enzyme, at pH 7.5 and 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 1.74
-
 alpha-D-glucose 1-phosphate mutant enzyme Y97M, at pH 7.5 and 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 2.5 3 alpha-D-glucose 1-phosphate mutant enzyme Y97N, at pH 7.5 and 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
2.7.7.9 3.28
-
 alpha-D-glucose 1-phosphate mutant enzyme Y97V, at pH 7.5 and 80°C Sulfurisphaera tokodaii
2.7.7.23 additional information
-
 additional information kinetics of wild-type and mutant enzymes for Glc-1-P UTase activities, overview 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 0.068
-
 N-acetyl-alpha-D-glucosamine 1-phosphate wild-type ST0452, 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 0.097
-
 N-acetyl-alpha-D-glucosamine 1-phosphate mutant 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 0.147
-
 N-acetyl-alpha-D-glucosamine 1-phosphate mutant 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
2.7.7.23 0.861
-
 N-acetyl-alpha-D-glucosamine 1-phosphate mutant Y97V, pH 7.5, 80°C Sulfurisphaera tokodaii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.23 Mg2+ required Sulfurisphaera tokodaii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.9 UDP + alpha-D-glucose 1-phosphate Sulfurisphaera tokodaii
-
 phosphate + UDP-glucose
-
 ?
2.7.7.9 UDP + alpha-D-glucose 1-phosphate Sulfurisphaera tokodaii DSM 16993
-
 phosphate + UDP-glucose
-
 ?
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
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.157 Sulfurisphaera tokodaii Q975F9
-
-
2.3.1.157 Sulfurisphaera tokodaii DSM 16993 Q975F9
-
-
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 Q975F9 multifunctional enzyme
-
2.7.7.23 Sulfurisphaera tokodaii DSM 16993 Q975F9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.9
-
 Sulfurisphaera tokodaii
2.7.7.9 His SpinTrap Talon column chromatography Sulfurisphaera tokodaii
2.7.7.23
-
 Escherichia coli
2.7.7.23
-
 Sulfurisphaera tokodaii
2.7.7.23 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography and ultrafiltration Sulfurisphaera tokodaii

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.7.9 0.66
-
 mutant enzyme Y97D, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 0.98
-
 mutant enzyme Y97G, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 1.03
-
 mutant enzyme Y97T, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 1.09
-
 mutant enzyme Y97K, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 1.22
-
 mutant enzyme Y97V, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 1.74
-
 mutant enzyme Y97A, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 2.18
-
 mutant enzyme Y97C, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 3.35
-
 mutant enzyme Y97F, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 4.08
-
 wild-type enzyme, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 4.26
-
 mutant enzyme Y97Q, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 4.51
-
 mutant enzyme Y97S, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 9.97
-
 mutant enzyme Y97L, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 10.41
-
 mutant enzyme Y97H, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 11.45
-
 mutant enzyme Y97M, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.9 16.92
-
 mutant enzyme Y97N, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 additional information
-
 wild-type and mutant enzymes' Glc-1-P UTase activities, overview Sulfurisphaera tokodaii
2.7.7.23 0.21
-
 mutant enzyme G9A/K147A, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 0.21
-
 mutant G9A/K147A, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 0.43
-
 mutant enzyme G9A/T80A, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 0.43
-
 mutant G9A/T80A, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 0.48
-
 mutant enzyme T80A/Y97A, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 0.48
-
 mutant T80A/Y97A, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 0.6
-
 mutant enzyme T80A/Y97F, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 0.6
-
 mutant T80A/Y97F, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 1.04
-
 mutant enzyme G9A/Y97F, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 1.04
-
 mutant G9A/Y97F, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 1.27
-
 mutant enzyme Y97A/K147A, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 1.27
-
 mutant Y97A/K147A, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 1.36
-
 mutant enzyme T80A/K147A, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 1.36
-
 mutant T80A/K147A, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 2.78
-
 mutant enzyme Y97F/K147A, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 2.78
-
 mutant Y97F/K147A, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 7.04
-
 mutant enzyme Y97E, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 7.04
-
 mutant Y97E, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 10.3
-
 mutant enzyme Y97C, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 10.3
-
 mutant Y97C, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 10.31
-
 mutant enzyme Y97P, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 10.31
-
 mutant Y97P, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 15.08
-
 wild-type enzyme, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 18.12
-
 mutant enzyme Y97G, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 18.12
-
 mutant Y97G, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 18.4
-
 mutant enzyme Y97F, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 18.4
-
 mutant Y97F, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 18.68
-
 mutant enzyme Y97I, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 18.68
-
 mutant Y97I, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 19.51
-
 mutant enzyme Y97M, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 19.51
-
 mutant Y97M, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 20.37
-
 mutant enzyme Y97K, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 20.37
-
 mutant Y97K, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 21.06
-
 mutant enzyme Y97D, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 21.06
-
 mutant Y97D, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 22.03
-
 mutant enzyme Y97L, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 22.03
-
 mutant Y97L, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 27.52
-
 mutant enzyme Y97A, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 27.52
-
 mutant Y97A, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 29.77
-
 mutant enzyme Y97R, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 29.77
-
 mutant Y97S, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 31.27
-
 mutant enzyme Y97S, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 31.27
-
 mutant Y97T, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 34.6
-
 mutant enzyme Y97Q, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 34.6
-
 mutant Y97Q, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 43.7
-
 mutant enzyme Y97H, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 43.7
-
 mutant Y97H, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 52.56
-
 mutant enzyme Y103V, 37°C, pH 7.5 Escherichia coli
2.7.7.23 53.79
-
 mutant enzyme Y97T, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 53.79
-
 mutant enzyme Y97V, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 53.79
-
 mutant Y97V, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 67.11
-
 mutant enzyme Y97N, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 67.11
-
 mutant Y97N, pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 75.63
-
 wild-type enzyme, 37°C, pH 7.5 Escherichia coli
2.7.7.23 93.97
-
 mutant enzyme Y103A, 37°C, pH 7.5 Escherichia coli
2.7.7.23 99.8
-
 mutant enzyme Y103N, 37°C, pH 7.5 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.9 UDP + alpha-D-glucose 1-phosphate
-
 Sulfurisphaera tokodaii phosphate + UDP-glucose
-
 ?
2.7.7.9 UDP + alpha-D-glucose 1-phosphate
-
 Sulfurisphaera tokodaii DSM 16993 phosphate + UDP-glucose
-
 ?
2.7.7.9 UTP + alpha-D-glucose 1-phosphate
-
 Sulfurisphaera tokodaii diphosphate + UDP-glucose
-
-
2.7.7.9 UTP + alpha-D-glucose 1-phosphate
-
 Sulfurisphaera tokodaii DSM 16993 diphosphate + UDP-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
2.3.1.157 ST0452 protein
-
 Sulfurisphaera tokodaii
2.7.7.9 Glc-1-P UTase
-
 Sulfurisphaera tokodaii
2.7.7.9 GlcNAc-1-P UTase
-
 Sulfurisphaera tokodaii
2.7.7.9 ST0452 bifunctional enzyme exhibiting sugar-1-phosphate nucleotidylyltransferase and amino-sugar-1-phosphate acetyltransferase activities Sulfurisphaera tokodaii
2.7.7.9 ST0452 protein
-
 Sulfurisphaera tokodaii
2.7.7.9 sugar-1-P NTase
-
 Sulfurisphaera tokodaii
2.7.7.9 sugar-1-phosphate nucleotidylyltransferase
-
 Sulfurisphaera tokodaii
2.7.7.23 amino-sugar-1-phosphate acetyltransferase
-
 Sulfurisphaera tokodaii
2.7.7.23 GlcNAc-1-P UTase
-
 Escherichia coli
2.7.7.23 GlcNAc-1-P UTase
-
 Sulfurisphaera tokodaii
2.7.7.23 GlmU
-
 Escherichia coli
2.7.7.23 ST0452
-
 Sulfurisphaera tokodaii
2.7.7.23 ST0452 protein
-
 Sulfurisphaera tokodaii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
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 2.08
-
 alpha-D-glucose 1-phosphate mutant enzyme Y97V, at pH 7.5 and 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 2.97
-
 alpha-D-glucose 1-phosphate wild type enzyme, at pH 7.5 and 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 14.97
-
 alpha-D-glucose 1-phosphate mutant enzyme Y97M, at pH 7.5 and 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
2.7.7.9 38.15
-
 alpha-D-glucose 1-phosphate mutant enzyme Y97N, at pH 7.5 and 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 9.97
-
 N-acetyl-alpha-D-glucosamine 1-phosphate wild-type ST0452, 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 10.9
-
 N-acetyl-alpha-D-glucosamine 1-phosphate mutant 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 48.95
-
 N-acetyl-alpha-D-glucosamine 1-phosphate mutant 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
2.7.7.23 49.75
-
 N-acetyl-alpha-D-glucosamine 1-phosphate mutant Y97N, pH 7.5, 80°C Sulfurisphaera tokodaii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.23 7.5
-
 assay at Sulfurisphaera tokodaii

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.7.23 UTP
-
 Sulfurisphaera tokodaii

General Information

EC Number General Information Comment Organism
2.7.7.23 evolution comparison of the activities of the ST0452 protein to those of similar enzymes from bacteria show that both the apparent Km and kcat values of the ST0452 GlcNAc-1-P UTase activity are smaller than those of Escherichia coli GlmU (EcGlmU) enzymes indicating that the archaeal ST0452 protein can accept a low concentration of substrate but that its turnover rate is lower than that of the EcGlmU enzyme Sulfurisphaera tokodaii
2.7.7.23 additional information Tyr at the 97th position of the ST0452 protein plays an important role in catalysis. Reaction scheme of the sugar-1-P UTase, overview Sulfurisphaera tokodaii
2.7.7.23 physiological function the ST0452 protein, a thermostable protein isolated from the thermophilic archaeon Sulfolobus tokodaii, is a bifunctional protein exhibiting sugar-1-phosphate nucleotidylyltransferase (sugar-1-PNTase) and amino-sugar-1-phosphate acetyltransferase activities. ST0452 protein exhibits increased activity following single amino acid substitutions of Ala Sulfurisphaera tokodaii

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 0.63
-
 alpha-D-glucose 1-phosphate mutant enzyme Y97V, at pH 7.5 and 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 2.41
-
 alpha-D-glucose 1-phosphate wild type enzyme, at pH 7.5 and 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 8.6
-
 alpha-D-glucose 1-phosphate mutant enzyme Y97M, at pH 7.5 and 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
2.7.7.9 15.08
-
 alpha-D-glucose 1-phosphate mutant enzyme Y97N, at pH 7.5 and 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 56.9
-
 N-acetyl-alpha-D-glucosamine 1-phosphate mutant 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
2.7.7.23 112.4
-
 N-acetyl-alpha-D-glucosamine 1-phosphate mutant 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
2.7.7.23 146.6
-
 N-acetyl-alpha-D-glucosamine 1-phosphate wild-type ST0452, 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
2.7.7.23 338.4
-
 N-acetyl-alpha-D-glucosamine 1-phosphate mutant Y97N, pH 7.5, 80°C Sulfurisphaera tokodaii