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Literature summary for 3.5.4.16 extracted from
- Biosynthesis of pteridines. Stopped-flow kinetic analysis of GTP cyclohydrolase I (2001), Biochemistry, 40, 7896-7902.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| tetrahydrobiopterin | feedback inhibition | Escherichia coli |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | stopped-flow kinetic analysis of the reaction, single turnover experiments, the rate-limiting step occurs rather late in the reaction sequence | Escherichia coli |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | catalytically essential ion, complexed to 2 cysteine and 1 histidine residue | Escherichia coli | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate | reaction mechanism, six consecutive unimolecular reaction steps, the first of which being reversible | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GTP + H2O | - |
Escherichia coli | formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
assay at | Escherichia coli |
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Release 2023.1 (January 2023)
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