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Literature summary 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)

EC Number Cloned (Comment) Organism
1.14.15.39
-
 Streptomyces coelicolor
4.2.3.47
-
 Streptomyces coelicolor

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.15.39
-
 Streptomyces coelicolor
4.2.3.47
-
 Streptomyces coelicolor

Protein Variants

EC Number Protein Variants Comment Organism
1.14.15.39 D253A/D254A/D257A DDXX(D/E) conserved in terpene synthases Streptomyces coelicolor
1.14.15.39 D254A/D257A DDXX(D/E) conserved in terpene synthases Streptomyces coelicolor

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.3.47 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.3.47 0.0168
-
 (2E,6E)-farnesyl diphosphate pH 5.5, in the presence of Mg2+ Streptomyces coelicolor

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.3.47 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
4.2.3.47 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
4.2.3.47 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

EC Number Organism UniProt Comment Textmining
1.14.15.39 Streptomyces coelicolor
-
-
-
1.14.15.39 Streptomyces coelicolor A3(2)
-
-
-
4.2.3.47 Streptomyces coelicolor
-
-
-
4.2.3.47 Streptomyces coelicolor A3(2)
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.15.39
-
 Streptomyces coelicolor
4.2.3.47
-
 Streptomyces coelicolor

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.3.47 (2E,6E)-farnesyl diphosphate
-
 Streptomyces coelicolor (E)-beta-farnesene + diphosphate
-
 ?
4.2.3.47 (2E,6E)-farnesyl diphosphate
-
 Streptomyces coelicolor A3(2) (E)-beta-farnesene + diphosphate
-
 ?
4.2.3.47 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%) ?
4.2.3.47 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%) ?
4.2.3.47 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 ?
-
 ?
4.2.3.47 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

EC Number Synonyms Comment Organism
1.14.15.39 albaflavenone synthase
-
 Streptomyces coelicolor
1.14.15.39 CYP170A1
-
 Streptomyces coelicolor
4.2.3.47 farnesene synthase
-
 Streptomyces coelicolor
4.2.3.47 sesquiterpene synthase
-
 Streptomyces coelicolor
4.2.3.47 terpene synthase
-
 Streptomyces coelicolor

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.3.47 0.019
-
 (2E,6E)-farnesyl diphosphate pH 5.5, in the presence of Mg2+ Streptomyces coelicolor

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.15.39 7 8.2
-
 Streptomyces coelicolor
4.2.3.47 5.5
-
 maximum between pH 5.5 and 6.5 (farnesene synthase activity) Streptomyces coelicolor

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.2.3.47 4 7 pH 4.0: about 25% of maximal activity, pH 7.0: about 40% of maximal activity Streptomyces coelicolor

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
4.2.3.47 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

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.39 cytochrome-P450
-
 Streptomyces coelicolor

General Information

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