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Literature summary extracted from

  • Ansbacher, T.; Freud, Y.; Major, D.
    Slow-starter enzymes role of active-site architecture in the catalytic control of the biosynthesis of taxadiene by taxadiene synthase (2018), Biochemistry, 57, 3773-3779 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
4.2.3.17 additional information a mutation Y841H, analogous to W753H mutation, can possibly lead to formation of verticillane Taxus brevifolia
4.2.3.17 W753H the mutation leads to the exclusive formation of side product cembrene A Taxus brevifolia
4.2.3.17 W753H the mutation leads to the exclusive formation of side product cembrene A. The simulations of the W753H mutant shows that, in the mutant structure, the His side chain is in the perfect position to deprotonate the cembrenyl cation en route to cembrene formation and that this abortive deprotonation is an energetically facile process Taxus brevifolia
4.2.3.150 additional information a mutation Y841H, analogous to W753H mutation, can possibly lead to formation of verticillane Taxus brevifolia
4.2.3.150 W753H the mutation leads to the exclusive formation of side product cembrene A. The simulations of the W753H mutant shows that, in the mutant structure, the His side chain is in the perfect position to deprotonate the cembrenyl cation en route to cembrene formation and that this abortive deprotonation is an energetically facile process Taxus brevifolia

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.3.17 geranylgeranyl diphosphate Taxus brevifolia
-
taxa-4,11-diene + diphosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.2.3.17 Taxus brevifolia
-
-
-
4.2.3.17 Taxus brevifolia Q41594
-
-
4.2.3.150 Taxus brevifolia
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.3.17 geranylgeranyl diphosphate
-
Taxus brevifolia taxa-4,11-diene + diphosphate
-
?
4.2.3.17 additional information the wild-type enzyme forms cembrene A as a side product, while enzyme mutant W753H produces cembrene A as main product Taxus brevifolia ?
-
?
4.2.3.150 geranylgeranyl diphosphate reaction of enzyme mutant W753H, cembrene A is only a side product for the wild-type enzyme Taxus brevifolia (R)-cembrene A + diphosphate
-
?

Synonyms

EC Number Synonyms Comment Organism
4.2.3.17 TXS
-
Taxus brevifolia

General Information

EC Number General Information Comment Organism
4.2.3.17 additional information detailed mechanistic analysis of the biosynthesis of taxadiene by enzyme TXS using a hybrid quantum mechanics-molecular mechanics potential in conjunction with free energy simulation methods, overview. Generation of a free-energy fingerprint for type I terpene synthases. The active-site Trp residue W753 is a key feature of the TXS active-site architecture and stabilizes intermediate cations via Pi-cation interactions Taxus brevifolia