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Literature summary for 2.4.2.8 extracted from
- Functional roles for amino acids in active site loop II of a hypoxanthine phosphoribosyltransferase (2003), Biochim. Biophys. Acta, 1650, 105-116.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of active wild-type and of mutant enzymes in Escherichia coli strain DH5alpha | Trypanosoma cruzi |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | saturation mutagenesis for randomly exchange of amino acids of the active site loop II, construction of diverse mutants of the residues S102 to Q112, kinetic analysis and determination of catalytic efficiencies in the forward and reverse reaction, overview | Trypanosoma cruzi |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic analysis in the forward and reverse reaction of the wild-type enzyme and diverse mutant enzymes, overview | Trypanosoma cruzi |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Trypanosoma cruzi |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| IMP + diphosphate | Trypanosoma cruzi | - |
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Trypanosoma cruzi | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type and mutant enzymes from Escherichia coli strain DH5alpha by GMP affinity chromatography | Trypanosoma cruzi |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | reaction mechanism, the flexible loop II, comprising 12 amino acid residues, closes over the active site of the enzyme as it approaches the transition state, the loop is required for full activity, structure-function relationship for the conserved residues | Trypanosoma cruzi |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
kinetic analysis and determination of catalytic efficiencies in the forward and reverse reaction for the wild-type and diverse mutant enzymes, overview | Trypanosoma cruzi |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| IMP + diphosphate | - |
Trypanosoma cruzi | hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| HPRT | - |
Trypanosoma cruzi |
| inosine monophosphate:pyrophosphate phosphoribosyltransferase | - |
Trypanosoma cruzi |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at, forward and reverse reaction | Trypanosoma cruzi |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | wild-type and diverse mutant enzymes, overview | Trypanosoma cruzi |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at, forward and reverse reaction | Trypanosoma cruzi |
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Release 2023.1 (January 2023)
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