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Literature summary for 6.3.4.18 extracted from
- Structural and functional modularity of proteins in the de novo purine biosynthetic pathway (2009), Protein Sci., 18, 881-892.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | generation of six recombinant hybrid proteins combining functional domains of PurK and PurT, glycinamide ribonucleotide formyltransferase, on the basis of structural and sequence alignments, overview. The mutant chimeras are functional and show activity with different substrates, overview | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics of recombinant mutant proteins, overview | Escherichia coli | |
| 0.0068 | - |
ATP | pH 8.0, 25°C, chimeric mutant with PurK activity | Escherichia coli |  |
| 0.0103 | - |
5-amino-1(5-phospho-D-ribosyl)imidazole | pH 8.0, 25°C, chimeric mutant with PurK activity | Escherichia coli | |
| 0.048 | - |
ATP | pH 8.0, 25°C, wild-type PurK | Escherichia coli | |
| 0.066 | - |
5-amino-1(5-phospho-D-ribosyl)imidazole | pH 8.0, 25°C, wild-type PurK | Escherichia coli | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + 5-amino-1(5-phospho-D-ribosyl)imidazole + HCO3- | Escherichia coli | - |
ADP + phosphate + 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
strains, DH-5alpha and BL21(DE3), and purK- strain K-12 MG1655, gene purK | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.23 | - |
wild-type PurK, ADP formation | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + 5-amino-1(5-phospho-D-ribosyl)imidazole + HCO3- | - |
Escherichia coli | ADP + phosphate + 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole | - |
? | |
| ATP + 5-amino-1(5-phospho-D-ribosyl)imidazole + HCO3- | catalytic steps are the formation of an acyl phosphate intermediate upon ATP cleavage, followed by the nucleophilic attack on the carboxyl carbon of the intermediates by the amino nitrogen of the mononucleotides, formation of acyl phosphate intermediates | Escherichia coli | ADP + phosphate + 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole | - |
? | |
| additional information | comparison of active site organization and reaction mechanism to purT-encoded glycinamide ribonucleotide formyltransferase, overview | Escherichia coli | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | comparison of tertiary structure and active site organization to purT-encoded glycinamide ribonucleotide formyltransferase, PurK shows a three domain structure | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| More | PurK is a member of the ATP-grasp protein superfamily | Escherichia coli |
| N5-carboxylaminoimidazole ribonucleotide synthetase | - |
Escherichia coli |
| PurK | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.87 | - |
ATP | pH 8.0, 25°C, chimeric mutant with PurK activity | Escherichia coli | |
| 5.9 | - |
ATP | pH 8.0, 25°C, wild-type PurK | Escherichia coli | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Escherichia coli | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the enzyme is involved in the de novo purine biosynthetic pathway | Escherichia coli |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 84 | - |
ATP | pH 8.0, 25°C, chimeric mutant with PurK activity | Escherichia coli | |
| 89 | - |
ATP | pH 8.0, 25°C, wild-type PurK | Escherichia coli | |
| 120 | - |
5-amino-1(5-phospho-D-ribosyl)imidazole | pH 8.0, 25°C, wild-type PurK | Escherichia coli | |
| 130 | - |
5-amino-1(5-phospho-D-ribosyl)imidazole | pH 8.0, 25°C, chimeric mutant with PurK activity | Escherichia coli | |
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