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Literature summary extracted from
- Expression and purification of imidazole glycerol phosphate synthase from Saccharomyces cerevisiae (2000), Protein Expr. Purif., 18, 366-377.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.3.1.B2 | expressed in a bacterial system under the control of T7 polymerase promoter | Saccharomyces cerevisiae |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.3.1.B2 | 0.004 | - |
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate | pH 7.0, 30°C | Saccharomyces cerevisiae |  |
| 4.3.1.B2 | 1.7 | - |
L-glutamine | pH 7.0, 30°C | Saccharomyces cerevisiae | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.B2 | 55000 | - |
gel filtration | Saccharomyces cerevisiae |
| 4.3.1.B2 | 61000 | - |
1 * 61000, SDS-PAGE, the protein is bifunctional, representing a fusion between the N-terminal HisH domain and a C-terminal HisF domain | Saccharomyces cerevisiae |
| 4.3.1.B2 | 61082 | - |
1 * 61082, calculated from sequence, the protein is bifunctional, representing a fusion between the N-terminal HisH domain and a C-terminal HisF domain | Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.3.1.B2 | L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate | Saccharomyces cerevisiae | - |
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.3.1.B2 | Saccharomyces cerevisiae | P33734 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.3.1.B2 | - |
Saccharomyces cerevisiae |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 4.3.1.B2 | culture condition | the production of the soluble HIS7 is highest at 25°C with 1 mM isopropyl beta-D-thiogalactopyranoside and this condition is used for the large-scale protein preparations | Saccharomyces cerevisiae | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.3.1.B2 | L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate | - |
Saccharomyces cerevisiae | L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | - |
? | |
| 4.3.1.B2 | L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate | - |
Saccharomyces cerevisiae | L-glutamate + D-erythro-imidazole-glycerol-phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | - |
? | |
| 4.3.1.B2 | additional information | the enzyme shows a low basal level glutaminase activity that can be enhanced 1000fold in the presence of a nucleotide substrate or analog | Saccharomyces cerevisiae | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.3.1.B2 | monomer | 1 * 61000, SDS-PAGE, the protein is bifunctional, representing a fusion between the N-terminal HisH domain and a C-terminal HisF domain | Saccharomyces cerevisiae |
| 4.3.1.B2 | monomer | 1 * 61082, calculated from sequence, the protein is bifunctional, representing a fusion between the N-terminal HisH domain and a C-terminal HisF domain | Saccharomyces cerevisiae |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.3.1.B2 | IGP synthase | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.B2 | 30 | - |
assay at | Saccharomyces cerevisiae |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.3.1.B2 | 3.9 | - |
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate | pH 7.0, 30°C | Saccharomyces cerevisiae | |
| 4.3.1.B2 | 5.2 | - |
L-glutamine | pH 7.0, 30°C | Saccharomyces cerevisiae | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.B2 | 7 | - |
assay at | Saccharomyces cerevisiae |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.3.1.B2 | physiological function | the enzyme represents a junction between histidine biosynthesis and de novo purine biosynthesis | Saccharomyces cerevisiae |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.3.1.B2 | 3.1 | - |
L-glutamine | pH 7.0, 30°C | Saccharomyces cerevisiae | |
| 4.3.1.B2 | 950 | - |
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate | pH 7.0, 30°C | Saccharomyces cerevisiae | |
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