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Literature summary for 4.2.3.132 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
Search for more literature for 4.2.3.132

Protein Variants

Protein Variants Comment Organism
D621A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
D625A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
D766A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
D845A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
E589A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
E699A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
E773A the mutant shows decreased Km and reduced kcat values compared to the wild type enzyme Abies grandis
E778A the mutant shows decreased Km and reduced kcat values compared to the wild type enzyme Abies grandis
N765A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
R584A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
R586A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
R762A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
S721A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
T617A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
T769A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
T848A the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis
Y841F the mutant shows increased Km and reduced kcat values compared to the wild type enzyme Abies grandis

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Abies grandis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?

Synonyms

Synonyms Comment Organism
abietadiene synthase
-
 Abies grandis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
-
 Abies grandis

General Information

General Information Comment Organism
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