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Literature summary for 4.2.3.119 extracted from

  • Tashiro, M.; Ono, K.; Kimura, Y.; Kawai-Noma, S.; Saito, K.; Umeno, D.
    Tweezing the cofactor preference of gymnosperm pinene synthase (2018), Biosci. Biotechnol. Biochem., 82, 1058-1061 .
    View publication on PubMed
Search for more literature for 4.2.3.119

Protein Variants

Protein Variants Comment Organism
Q456K site-directed mutagenesis, mutation in the alpha-domain (catalytic domain), the mutant shows increased catalytic activity compared to the wild-type Pinus taeda
Q456L site-directed mutagenesis, mutation in the alpha-domain (catalytic domain), the mutant shows increased catalytic activity compared to the wild-type Pinus taeda
Q456P site-directed mutagenesis, mutation in the alpha-domain (catalytic domain), the mutant shows 50% reduced catalytic activity compared to the wild-type Pinus taeda
Q456V site-directed mutagenesis, mutation in the alpha-domain (catalytic domain), the mutant shows increased catalytic activity compared to the wild-type Pinus taeda

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, activates, kinetics of wild-type and Q457L and Q457I mutant enzymes, overview Pinus taeda
additional information no manganese dependency, activity of wild-type and Q457L and Q457I mutant enzymes in the absence or presence of 0.01 mM manganese is similar Pinus taeda

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Pinus taeda Q84KL6
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
PT1
-
 Pinus taeda

General Information

General Information Comment Organism
malfunction replacement of residue Q457 with three other amino acids I, K, and V, elevates the activity of the enzyme, while Q457P shows reduced activity Pinus taeda
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. Residue Q457 is important for catalytic activity Pinus taeda