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Literature summary extracted from

  • Peters, R.J.; Croteau, R.B.
    Abietadiene synthase catalysis: mutational analysis of a prenyl diphosphate ionization-initiated cyclization and rearrangement (2002), Proc. Natl. Acad. Sci. USA, 99, 580-584.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.5.1.12 expression in Escherichia coli Abies grandis

Protein Variants

EC Number Protein Variants Comment Organism
4.2.3.18 D621A
-
Abies grandis
4.2.3.18 D625A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
4.2.3.18 D766A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
4.2.3.18 D845A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
4.2.3.18 E589A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
4.2.3.18 E699A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
4.2.3.18 E773A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
4.2.3.18 E778A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
4.2.3.18 N765A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
4.2.3.18 R584A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
4.2.3.18 R586A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
4.2.3.18 R762A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
4.2.3.18 S721A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
4.2.3.18 T617A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
4.2.3.18 T769A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
4.2.3.18 T848A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
4.2.3.18 Y841F no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
4.2.3.132 D621A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
4.2.3.132 D625A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
4.2.3.132 D766A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
4.2.3.132 D845A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
4.2.3.132 E589A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
4.2.3.132 E699A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
4.2.3.132 E773A the mutant shows decreased Km and reduced kcat values compared to the wild type enzyme Abies grandis
4.2.3.132 E778A the mutant shows decreased Km and reduced kcat values compared to the wild type enzyme Abies grandis
4.2.3.132 N765A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
4.2.3.132 R584A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
4.2.3.132 R586A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
4.2.3.132 R762A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
4.2.3.132 S721A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
4.2.3.132 T617A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
4.2.3.132 T769A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
4.2.3.132 T848A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
4.2.3.132 Y841F the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
5.5.1.12 D621A
-
Abies grandis
5.5.1.12 D625A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
5.5.1.12 D766A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
5.5.1.12 D845A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
5.5.1.12 E589A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
5.5.1.12 E699A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
5.5.1.12 E773A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
5.5.1.12 E778A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
5.5.1.12 N765A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
5.5.1.12 R584A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
5.5.1.12 R586A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
5.5.1.12 R762A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
5.5.1.12 S721A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
5.5.1.12 T617A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
5.5.1.12 T769A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
5.5.1.12 T848A no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis
5.5.1.12 Y841F no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type Abies grandis

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.3.18 (13alpha)-N,13-dimethylpodocarp-8(14)-en-13-aminium chloride
-
Abies grandis
5.5.1.12 (13alpha)-N,13-dimethylpodocarp-8(14)-en-13-aminium chloride
-
Abies grandis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.3.18 0.0003
-
copalyl diphosphate mutants E773A, E778A Abies grandis
4.2.3.18 0.0004
-
copalyl diphosphate wild-type, mutant D766A Abies grandis
4.2.3.18 0.0005
-
copalyl diphosphate mutant N765A Abies grandis
4.2.3.18 0.0007
-
copalyl diphosphate mutants R762A, E699A, D621A Abies grandis
4.2.3.18 0.0008
-
copalyl diphosphate mutants T848A, Y841F Abies grandis
4.2.3.18 0.001
-
copalyl diphosphate mutants E589A, R584A Abies grandis
4.2.3.18 0.002
-
copalyl diphosphate mutants R586A, T769A Abies grandis
4.2.3.18 0.003
-
copalyl diphosphate mutant S721A Abies grandis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.3.132 Mg2+ required for activity Abies grandis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.3.18 (+)-copalyl-diphosphate Abies grandis
-
(-)-abietadiene + diphosphate
-
?
5.5.1.12 geranylgeranyl diphosphate Abies grandis
-
(+)-copalyl diphosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.2.3.18 Abies grandis
-
-
-
4.2.3.132 Abies grandis
-
-
-
5.5.1.12 Abies grandis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.3.18 (+)-copalyl-diphosphate
-
Abies grandis (-)-abietadiene + diphosphate
-
?
4.2.3.132 additional information abietadiene synthase catalyzes the cyclization and rearrangement of (E,E,E)-geranylgeranyl diphosphate to a mixture of abietadiene double-bond isomers. The enzyme is bifunctional: Protonation across the terminal 14-15 double bond of (E,E,E)-geranylgeranyl diphosphate followed by bicyclization and deprotonation, produces the stable intermediate (+)-copalyl diphosphate (CPP). Then the enzyme ionizes CPP to promote cyclization to the tricyclic perhydrophenanthrene backbone. However, this cyclization is further coupled to a 1,2-methyl migration, by means of intramolecular proton transfer within a pimarenyl intermediate, to generate the C13 isopropyl group characteristic of the abietane skeleton. Finally, deprotonation of the resulting abietenyl carbocation at one of three alternative positions (C7, C12, or C15) leads to the three principal olefin products abieta-7(8),13(14)-diene (abietadiene), abieta-8(14),12(13)-diene (levopimaradiene), and abieta-8(14)-13(15)-diene (neoabietadiene), respectively, as a function of pH Abies grandis ?
-
?
5.5.1.12 geranylgeranyl diphosphate
-
Abies grandis (+)-copalyl diphosphate
-
?

Synonyms

EC Number Synonyms Comment Organism
4.2.3.132 abietadiene synthase
-
Abies grandis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.3.18 0.05
-
copalyl diphosphate mutant E589A Abies grandis
4.2.3.18 0.2
-
copalyl diphosphate mutant E778A Abies grandis
4.2.3.18 0.4
-
copalyl diphosphate mutant T617A Abies grandis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.3.132 7.2
-
-
Abies grandis

General Information

EC Number General Information Comment Organism
4.2.3.132 metabolism abietadiene synthase catalyzes the committed step in resin acid biosynthesis by catalyzing the cyclization and rearrangement of (E,E,E)-geranylgeranyl diphosphate to a mixture of abietadiene double-bond isomers. The enzyme is bifunctional: Protonation across the terminal 14-15 double bond of (E,E,E)-geranylgeranyl diphosphate followed by bicyclization and deprotonation, produces the stable intermediate (+)-copalyl diphosphate (CPP). Then the enzyme ionizes the CPP to promote cyclization to the tricyclic perhydrophenanthrene backbone. However, this cyclization is further coupled to a 1,2-methyl migration, by means of intramolecular proton transfer within a pimarenyl intermediate, to generate the C13 isopropyl group characteristic of the abietane skeleton. Finally, deprotonation of the resulting abietenyl carbocation at one of three alternative positions (C7, C12, or C15) leads to the three principal olefin products abieta-7(8),13(14)-diene (abietadiene), abieta-8(14),12(13)-diene (levopimaradiene), and abieta-8(14)-13(15)-diene (neoabietadiene), respectively Abies grandis