EC Number | Cloned (Comment) | Organism |
---|---|---|
5.5.1.12 | expression in Escherichia coli | Abies grandis |
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 |
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 |
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 |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
4.2.3.132 | Mg2+ | required for activity | Abies grandis |
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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.3.18 | Abies grandis | - |
- |
- |
4.2.3.132 | Abies grandis | - |
- |
- |
5.5.1.12 | Abies grandis | - |
- |
- |
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 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.2.3.132 | abietadiene synthase | - |
Abies grandis |
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 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.2.3.132 | 7.2 | - |
- |
Abies grandis |
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 |