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Literature summary for 2.7.7.23 extracted from
- Increasing in archaeal GlcNAc-1-P uridyltransferase activity by targeted mutagenesis while retaining its extreme thermostability (2007), J. Biochem., 141, 553-562.
Application
| Application | Comment | Organism |
|---|---|---|
| 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
| Protein Variants | Comment | Organism |
|---|---|---|
| D208A | enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions | Sulfurisphaera tokodaii |
| D208A | exhibits slightly weaker UDP-N-acetylglucosamine diphosphorylase activity than wild-type enzyme | Sulfurisphaera tokodaii |
| E146A | exhibits slightly weaker UDP-N-acetylglucosamine diphosphorylase activity than wild-type enzyme | Sulfurisphaera tokodaii |
| G9A | enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions | Sulfurisphaera tokodaii |
| K147A | enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions | Sulfurisphaera tokodaii |
| 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 |
| R13A | shows the same activity as wild-type protein | Sulfurisphaera tokodaii |
| T80A | enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions | Sulfurisphaera tokodaii |
| Y97A | enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions | Sulfurisphaera tokodaii |
| Y97F | enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions | Sulfurisphaera tokodaii |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0017 | - |
UTP | pH 7.5, 80°C | Sulfurisphaera tokodaii |  |
| 0.008 | - |
N-acetyl-alpha-D-glucosamine 1-phosphate | pH 7.5, 80°C | Sulfurisphaera tokodaii | |
| 0.016 | - |
diphosphate | pH 7.5, 80°C | Sulfurisphaera tokodaii | |
| 0.016 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.5, 80°C | Sulfurisphaera tokodaii | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| 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 | |
| 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 | |
| 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 | |
| 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 | |
| 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 | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | |
| 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 | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sulfurisphaera tokodaii | Q975F9 | - |
- |
| Sulfurisphaera tokodaii 7 | Q975F9 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | |
| 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 | |
| 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 | |
| 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 | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GlcNAc-1-P UTase | - |
Sulfurisphaera tokodaii |
| ST0452 | locus name | Sulfurisphaera tokodaii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
assay at | Sulfurisphaera tokodaii |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
half-life: 180 min | Sulfurisphaera tokodaii |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2.54 | - |
N-acetyl-alpha-D-glucosamine 1-phosphate | pH 7.5, 80°C | Sulfurisphaera tokodaii | |
| 3.53 | - |
UTP | pH 7.5, 80°C | Sulfurisphaera tokodaii | |
| 6.21 | - |
diphosphate | pH 7.5, 80°C | Sulfurisphaera tokodaii | |
| 8.4 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.5, 80°C | Sulfurisphaera tokodaii | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Sulfurisphaera tokodaii |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 320 | - |
N-acetyl-alpha-D-glucosamine 1-phosphate | pH 7.5, 80°C | Sulfurisphaera tokodaii | |
| 380 | - |
diphosphate | pH 7.5, 80°C | Sulfurisphaera tokodaii | |
| 530 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.5, 80°C | Sulfurisphaera tokodaii | |
| 2120 | - |
UTP | pH 7.5, 80°C | Sulfurisphaera tokodaii | |
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Release 2023.1 (January 2023)
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