Cloned (Comment) | Organism |
---|---|
- |
Streptomyces coelicolor |
Crystallization (Comment) | Organism |
---|---|
- |
Streptomyces coelicolor |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
epi-isozizaene | about 3-fold decreases in kcat for both farnesene synthase activity and P450 monooxygenase activity when the two substrates are present at the same time | Streptomyces coelicolor |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0168 | - |
(2E,6E)-farnesyl diphosphate | pH 5.5, in the presence of Mg2+ | Streptomyces coelicolor |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | strict requirement for a divalent cation cofactor, highest activity being observed in the presence of Mg2+ or Ca2+. Mn2+ shows relatively high activity at lower concentration, reaching 50% of the maximum synthase activity observed with Mg2+ as cofactor | Streptomyces coelicolor | |
Mg2+ | strict requirement for a divalent cation cofactor, highest activity being observed in the presence of Mg2+ or Ca2+. Mn2+ shows relatively high activity at lower concentration, reaching 50% of the maximum synthase activity observed with Mg2+ as cofactor | Streptomyces coelicolor | |
Mn2+ | strict requirement for a divalent cation cofactor, highest activity being observed in the presence of Mg2+ or Ca2+. Mn2+ shows relatively high activity at lower concentration, reaching 50% of the maximum synthase activity observed with Mg2+ as cofactor | Streptomyces coelicolor |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces coelicolor | - |
- |
- |
Streptomyces coelicolor A3(2) | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Streptomyces coelicolor |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2E,6E)-farnesyl diphosphate | - |
Streptomyces coelicolor | (E)-beta-farnesene + diphosphate | - |
? | |
(2E,6E)-farnesyl diphosphate | - |
Streptomyces coelicolor A3(2) | (E)-beta-farnesene + diphosphate | - |
? | |
farnesyl diphosphate | - |
Streptomyces coelicolor | (E)-beta-farnesene + diphosphate | 61% (E)-beta-farnesene, by-products: (3E,6E)-alpha-farnesene (26%), (3Z,6E)-alpha-farnesene (6.8%), neroliol (4.9%), and farnesol (1.8%) | ? | |
farnesyl diphosphate | - |
Streptomyces coelicolor A3(2) | (E)-beta-farnesene + diphosphate | 61% (E)-beta-farnesene, by-products: (3E,6E)-alpha-farnesene (26%), (3Z,6E)-alpha-farnesene (6.8%), neroliol (4.9%), and farnesol (1.8%) | ? | |
additional information | CYP170A1 posseses two distinct active sites that catalyze two very different and probably unrelated biochemical activities: beta-farnesene synthase and albaflavenone synthase (monooxygenase activity) | Streptomyces coelicolor | ? | - |
? | |
additional information | CYP170A1 posseses two distinct active sites that catalyze two very different and probably unrelated biochemical activities: beta-farnesene synthase and albaflavenone synthase (monooxygenase activity) | Streptomyces coelicolor A3(2) | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
farnesene synthase | - |
Streptomyces coelicolor |
sesquiterpene synthase | - |
Streptomyces coelicolor |
terpene synthase | - |
Streptomyces coelicolor |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.019 | - |
(2E,6E)-farnesyl diphosphate | pH 5.5, in the presence of Mg2+ | Streptomyces coelicolor |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | - |
maximum between pH 5.5 and 6.5 (farnesene synthase activity) | Streptomyces coelicolor |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4 | 7 | pH 4.0: about 25% of maximal activity, pH 7.0: about 40% of maximal activity | Streptomyces coelicolor |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
6.5 | 9 | partially denatured below pH 6.5 and above pH 9.0. At pH 5.5, all of the P450 form of CYP170A1 is converted to the P420 form, which is consistent with the absence of residual monooxygenase activity at this pH. Monooxygenase activity declines at the lower pH, which favors sesquiterpene synthase activity | Streptomyces coelicolor |
General Information | Comment | Organism |
---|---|---|
metabolism | bifunctional enzyme: containing albaflavenone synthase activity (CYP170A1) | Streptomyces coelicolor |