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Literature summary extracted from

  • Zhang, Z.; Akutsu, J.; Tsujimura, M.; Kawarabayasi, Y.
    Increasing in archaeal GlcNAc-1-P uridyltransferase activity by targeted mutagenesis while retaining its extreme thermostability (2007), J. Biochem., 141, 553-562.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.7.7.23 synthesis biosynthesis of UDP-N-acetyl-alpha-D-glucosamine. As glycosylation is the most important modification for activating peptide drugs, the activated form of N-acetyl-alpha-D-glucosamine is thought to be important for future development of effective drugs Sulfurisphaera tokodaii

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.23 D208A enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions Sulfurisphaera tokodaii
2.7.7.23 D208A exhibits slightly weaker UDP-N-acetylglucosamine diphosphorylase activity than wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 E146A exhibits slightly weaker UDP-N-acetylglucosamine diphosphorylase activity than wild-type enzyme Sulfurisphaera tokodaii
2.7.7.23 G9A enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions Sulfurisphaera tokodaii
2.7.7.23 K147A enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions Sulfurisphaera tokodaii
2.7.7.23 additional information for industrial applications, activity needs to be increased without decreasing thermostability. To enhance this activity, mutations are introduced into the amino acid residues located within the predicted reaction centre by targeted mutagenesis. All 12 mutant ST0452 proteins show no decrease in thermostability. Among them, six mutant proteins are found to have increased UDP-N-acetylglucosamine diphosphorylase activity under optimal reaction conditions with sufficient substrates or an appropriate metal ion Sulfurisphaera tokodaii
2.7.7.23 R13A shows the same activity as wild-type protein Sulfurisphaera tokodaii
2.7.7.23 T80A enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions Sulfurisphaera tokodaii
2.7.7.23 Y97A enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions Sulfurisphaera tokodaii
2.7.7.23 Y97F enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions Sulfurisphaera tokodaii
2.7.7.24 D208A UDP-N-acetylglucosamine diphosphorylase activity is very low Sulfurisphaera tokodaii
2.7.7.24 E146A UDP-N-acetylglucosamine diphosphorylase activity is very low Sulfurisphaera tokodaii
2.7.7.24 G9A UDP-N-acetylglucosamine diphosphorylase activity is very low Sulfurisphaera tokodaii
2.7.7.24 K147A UDP-N-acetylglucosamine diphosphorylase activity is very low Sulfurisphaera tokodaii
2.7.7.24 R13A UDP-N-acetylglucosamine diphosphorylase activity is very low Sulfurisphaera tokodaii
2.7.7.24 T80A enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions Sulfurisphaera tokodaii
2.7.7.24 Y97A enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions Sulfurisphaera tokodaii
2.7.7.24 Y97F UDP-N-acetylglucosamine diphosphorylase activity is very low Sulfurisphaera tokodaii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.23 0.0017
-
 UTP pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 0.008
-
 N-acetyl-alpha-D-glucosamine 1-phosphate pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 0.016
-
 diphosphate pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 0.016
-
 UDP-N-acetyl-alpha-D-glucosamine pH 7.5, 80°C Sulfurisphaera tokodaii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.23 Ca2+ 2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation Sulfurisphaera tokodaii
2.7.7.23 Co2+ 2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation Sulfurisphaera tokodaii
2.7.7.23 Mg2+ 2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation Sulfurisphaera tokodaii
2.7.7.23 Mn2+ 2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation Sulfurisphaera tokodaii
2.7.7.23 Zn2+ 2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation Sulfurisphaera tokodaii
2.7.7.24 Ca2+ 2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Co2+, Mn2+, Mg2+, Zn2+, Ca2+. No activity is detectable without a divalent cation Sulfurisphaera tokodaii
2.7.7.24 Co2+ 2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Co2+, Mn2+, Mg2+, Zn2+, Ca2+. No activity is detectable without a divalent cation Sulfurisphaera tokodaii
2.7.7.24 Mg2+ 2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Co2+, Mn2+, Mg2+, Zn2+, Ca2+. No activity is detectable without a divalent cation Sulfurisphaera tokodaii
2.7.7.24 Mn2+ 2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Co2+, Mn2+, Mg2+, Zn2+, Ca2+. No activity is detectable without a divalent cation Sulfurisphaera tokodaii
2.7.7.24 Zn2+ 2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Co2+, Mn2+, Mg2+, Zn2+, Ca2+. No activity is detectable without a divalent cation Sulfurisphaera tokodaii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.23 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate Sulfurisphaera tokodaii the enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 r
2.7.7.23 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate Sulfurisphaera tokodaii 7 the enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 r
2.7.7.24 additional information Sulfurisphaera tokodaii the multifunctional enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms ?
-
 ?
2.7.7.24 additional information Sulfurisphaera tokodaii 7 the multifunctional enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.23 Sulfurisphaera tokodaii Q975F9
-
-
2.7.7.23 Sulfurisphaera tokodaii 7 Q975F9
-
-
2.7.7.24 Sulfurisphaera tokodaii Q975F9
-
-
2.7.7.24 Sulfurisphaera tokodaii 7 Q975F9
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.23 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate the enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms Sulfurisphaera tokodaii diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 r
2.7.7.23 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate the enzyme also shows activity of EC 2.7.7.24, glucose-1-phosphate thymidylyltransferase Sulfurisphaera tokodaii diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 r
2.7.7.23 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate the enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms Sulfurisphaera tokodaii 7 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 r
2.7.7.23 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate the enzyme also shows activity of EC 2.7.7.24, glucose-1-phosphate thymidylyltransferase Sulfurisphaera tokodaii 7 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 r
2.7.7.24 dTTP + alpha-D-glucose 1-phosphate the enzyme also shows activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase Sulfurisphaera tokodaii diphosphate + dTDP-alpha-D-glucose
-
 ?
2.7.7.24 dTTP + alpha-D-glucose 1-phosphate the enzyme also shows activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase Sulfurisphaera tokodaii 7 diphosphate + dTDP-alpha-D-glucose
-
 ?
2.7.7.24 additional information the multifunctional enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms Sulfurisphaera tokodaii ?
-
 ?
2.7.7.24 additional information the multifunctional enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms Sulfurisphaera tokodaii 7 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.7.23 GlcNAc-1-P UTase
-
 Sulfurisphaera tokodaii
2.7.7.23 ST0452 locus name Sulfurisphaera tokodaii
2.7.7.24 Glc-1-P TTase
-
 Sulfurisphaera tokodaii
2.7.7.24 ST0452 locus name 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
2.7.7.24 80
-
 assay at Sulfurisphaera tokodaii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.7.23 80
-
 half-life: 180 min Sulfurisphaera tokodaii
2.7.7.24 80
-
 half-life: 180 min Sulfurisphaera tokodaii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.7.23 2.54
-
 N-acetyl-alpha-D-glucosamine 1-phosphate pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 3.53
-
 UTP pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 6.21
-
 diphosphate pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 8.4
-
 UDP-N-acetyl-alpha-D-glucosamine 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
2.7.7.24 7.5
-
 assay at Sulfurisphaera tokodaii

General Information

EC Number General Information Comment Organism
2.7.7.23 physiological function the enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms Sulfurisphaera tokodaii
2.7.7.24 physiological function the multifunctional enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms 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
2.7.7.23 320
-
 N-acetyl-alpha-D-glucosamine 1-phosphate pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 380
-
 diphosphate pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 530
-
 UDP-N-acetyl-alpha-D-glucosamine pH 7.5, 80°C Sulfurisphaera tokodaii
2.7.7.23 2120
-
 UTP pH 7.5, 80°C Sulfurisphaera tokodaii