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Literature summary for 4.2.3.12 extracted from
- Structure of a 6-pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor (2008), Acta Crystallogr. Sect. F, 64, 875-879.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli as a His-tagged fusion protein | Streptomyces coelicolor |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| X-ray crystal structure of the PTPS homolog from Streptomyces coelicolor, SCO 6650, is solved at 1.5 A resolution. SCO 6650 forms a hexameric T-fold that closely resembles other PTPS proteins. The biological activity of SCO 6650 is unknown, but it lacks both a required active-site zinc metal ion and the essential catalytic triad and does not catalyze the PTPS reaction. SCO 6650 maintains active-site residues consistent with binding a pterin-like substrate | Streptomyces coelicolor |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces coelicolor | - |
- |
- |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
no enzymatic activity detected | Streptomyces coelicolor |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 6-pyruvoyltetrahydropterin synthase | - |
Streptomyces coelicolor |
| PTPS homologue | - |
Streptomyces coelicolor |
| SCO 6650 | - |
Streptomyces coelicolor |
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