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Literature summary extracted from

  • Tashiro, M.; Kiyota, H.; Kawai-Noma, S.; Saito, K.; Ikeuchi, M.; Iijima, Y.; Umeno, D.
    Bacterial production of pinene by a laboratory-evolved pinene-synthase (2016), ACS Synth. Biol., 5, 1011-1020 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.3.119 gene PT1, recombinant expression of His-tagged enzyme from codon-optimized gene in Escherichia coli cytosol, coexpression of prenyltransferases GPP synthase and FPP synthase Pinus taeda

Protein Variants

EC Number Protein Variants Comment Organism
4.2.3.119 H346Y site-directed mutagenesis, mutation in the alpha-domain (catalytic domain), no phenotype, similar to wild-type Pinus taeda
4.2.3.119 additional information estalishment of a pinene production system in recombinant Escherichia coli by coexpression of (-)-alpha-pinene synthase from Pinus paeda and Abies grandis GPPS, as well as farnesyl diphosphate synthase mutant IspA(S80F) from Escherichia coli. The isolated alpha-pinene synthase variant PSmut outperforms the wild-type (parent) enzyme in multiple contexts in Escherichia coli and cyanobacteria. The purified variant exhibits drastically altered metal dependency, enabling to keep the activity in the cytosol that is manganese-deficient. Coexpression of this variant with mevalonate pathway enzymes, isopentenyl diphosphate isomerase, and GPP synthase yield 140 mg/l pinene in a flask culture. Screening for PS mutants with higher cellular activity and production method optimization, overview Pinus taeda
4.2.3.119 Q456L site-directed mutagenesis, mutation in the alpha-domain (catalytic domain), the mutant shows a reduction in pigmentation (PSmut) but shows improved catalytic activity Pinus taeda

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.3.119 0.0014
-
 geranyl diphosphate pH and temperature not specified in the publication Pinus taeda

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.3.119 Mg2+ required Pinus taeda

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.3.119 geranyl diphosphate Pinus taeda
-
 (-)-alpha-pinene + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.3.119 Pinus taeda Q84KL6
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.3.119 geranyl diphosphate
-
 Pinus taeda (-)-alpha-pinene + diphosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.3.119 pinene-synthase
-
 Pinus taeda
4.2.3.119 PT1
-
 Pinus taeda

General Information

EC Number General Information Comment Organism
4.2.3.119 malfunction mutation Q456L in the alpha-domain (catalytic domain) causes a reduction in pigmentation (PSmut) Pinus taeda
4.2.3.119 additional information Q457 is located on helix F, which supports a part of the catalytic core and is proximate to the highly conserved residues Y455 and E458 Pinus taeda