Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Protein Variants

EC Number Protein Variants Comment Organism
4.2.3.119 Q456K site-directed mutagenesis, mutation in the alpha-domain (catalytic domain), the mutant shows increased catalytic activity compared to the wild-type Pinus taeda
4.2.3.119 Q456L site-directed mutagenesis, mutation in the alpha-domain (catalytic domain), the mutant shows increased catalytic activity compared to the wild-type Pinus taeda
4.2.3.119 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
4.2.3.119 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

EC Number Metals/Ions Comment Organism Structure
4.2.3.119 Mg2+ required, activates, kinetics of wild-type and Q457L and Q457I mutant enzymes, overview Pinus taeda
4.2.3.119 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)

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 PT1
-
 Pinus taeda

General Information

EC Number General Information Comment Organism
4.2.3.119 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
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. Residue Q457 is important for catalytic activity Pinus taeda