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Literature summary for 4.2.3.47 extracted from

  • Zhao, B.; Lei, L.; Vassylyev, D.G.; Lin, X.; Cane, D.E.; Kelly, S.L.; Yuan, H.; Lamb, D.C.; Waterman, M.R.
    Crystal structure of albaflavenone monooxygenase containing a moonlighting terpene synthase active site (2009), J. Biol. Chem., 284, 36711-36719.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Streptomyces coelicolor

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Streptomyces coelicolor

Inhibitors

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 [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

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

Organism UniProt Comment Textmining
Streptomyces coelicolor
-
-
-
Streptomyces coelicolor A3(2)
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Streptomyces coelicolor

Substrates and Products (Substrate)

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

Synonyms Comment Organism
farnesene synthase
-
Streptomyces coelicolor
sesquiterpene synthase
-
Streptomyces coelicolor
terpene synthase
-
Streptomyces coelicolor

Turnover Number [1/s]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
maximum between pH 5.5 and 6.5 (farnesene synthase activity) Streptomyces coelicolor

pH Range

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 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

General Information Comment Organism
metabolism bifunctional enzyme: containing albaflavenone synthase activity (CYP170A1) Streptomyces coelicolor