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Literature summary extracted from

  • Hyat, D.C.; Croteau, R.
    Mutational analysis of a monoterpene synthase reaction: altered catalysis through directed mutagenesis of (-)-pinene synthase from Abies grandis (2005), Arch. Biochem. Biophys., 439, 222-233.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.3.119 expression in Escherichia coli Abies grandis
4.2.3.120 expression in Escherichia coli Abies grandis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.3.117 modeling of amino acid sequence onto the crystal structures of tobacco 5-epi-aristolochene synthase and bornyl diphosphate synthase and comparison with (-)-pinene synthase Abies grandis
4.2.3.119 modeling of amino acid sequence onto the crystal structures of tobacco 5-epi-aristolochene synthase and bornyl diphosphate synthase and comparison with (-)-camphene synthase Abies grandis
4.2.3.120 modeling of amino acid sequence onto the crystal structures of tobacco 5-epi-aristolochene synthase and bornyl diphosphate synthase and comparison with (-)-camphene synthase Abies grandis

Protein Variants

EC Number Protein Variants Comment Organism
4.2.3.117 additional information replacement of selected amino acid residues in (-)-pinene synthase with the corresponding residues from (-)-camphene synthase in an effort to identify the amino acids responsible for the catalytic differences. The approach produces an enzyme in which more than half of the product is channeled through an alternative pathway. Several (-)-pinene synthase to (-)-camphene synthase amino acid substitutions are necessary before catalysis is significantly altered Abies grandis
4.2.3.119 C372S replacement with corresponding residue of (-)-camphene synthase, 97% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant Abies grandis
4.2.3.119 C372S/C480S replacement with corresponding residue of (-)-camphene synthase, 72% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene Abies grandis
4.2.3.119 C372S/F597W replacement with corresponding residue of (-)-camphene synthase, 100% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene Abies grandis
4.2.3.119 C372S/F597W/S485C/F597W replacement with corresponding residue of (-)-camphene synthase, 99% of wild-type activity. Mutant produces about 80%(-)-alpha-pinene and 10% (-)-beta-pinene Abies grandis
4.2.3.119 C372S/S485C replacement with corresponding residue of (-)-camphene synthase, 92% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene Abies grandis
4.2.3.119 C480S replacement with corresponding residue of (-)-camphene synthase, 97% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant Abies grandis
4.2.3.119 C480S/F597W replacement with corresponding residue of (-)-camphene synthase, 7% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene Abies grandis
4.2.3.119 C480S/S485C replacement with corresponding residue of (-)-camphene synthase, 70% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene Abies grandis
4.2.3.119 F597W replacement with corresponding residue of (-)-camphene synthase, 73% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant Abies grandis
4.2.3.119 additional information replacement of selected amino acid residues in (-)-pinene synthase with the corresponding residues from (-)-camphene synthase in an effort to identify the amino acids responsible for the catalytic diVerences. The approach produces an enzyme in which more than half of the product is channeled through an alternative pathway. Several (-)-pinene synthase to (-)-camphene synthase amino acid substitutions are necessary before catalysis is significantly altered Abies grandis
4.2.3.119 S485C replacement with corresponding residue of (-)-camphene synthase, 100% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant Abies grandis
4.2.3.119 S485C/F597W replacement with corresponding residue of (-)-camphene synthase, 68% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene Abies grandis
4.2.3.120 C372S replacement with corresponding residue of (-)-camphene synthase, 97% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant Abies grandis
4.2.3.120 C372S/C480S replacement with corresponding residue of (-)-camphene synthase, 72% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene Abies grandis
4.2.3.120 C372S/F597W replacement with corresponding residue of (-)-camphene synthase, 100% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene Abies grandis
4.2.3.120 C372S/F597W/S485C/F597W replacement with corresponding residue of (-)-camphene synthase, 99% of wild-type activity. Mutant produces about 80%(-)-alpha-pinene and 10% (-)-beta-pinene Abies grandis
4.2.3.120 C372S/S485C replacement with corresponding residue of (-)-camphene synthase, 92% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene Abies grandis
4.2.3.120 C480S replacement with corresponding residue of (-)-camphene synthase, 97% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant Abies grandis
4.2.3.120 C480S/F597W replacement with corresponding residue of (-)-camphene synthase, 7% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene Abies grandis
4.2.3.120 C480S/S485C replacement with corresponding residue of (-)-camphene synthase, 70% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene Abies grandis
4.2.3.120 F597W replacement with corresponding residue of (-)-camphene synthase, 73% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant Abies grandis
4.2.3.120 additional information replacement of selected amino acid residues in (-)-pinene synthase with the corresponding residues from (-)-camphene synthase in an effort to identify the amino acids responsible for the catalytic diVerences. The approach produces an enzyme in which more than half of the product is channeled through an alternative pathway. Several (-)-pinene synthase to (-)-camphene synthase amino acid substitutions are necessary before catalysis is significantly altered Abies grandis
4.2.3.120 S485C replacement with corresponding residue of (-)-camphene synthase, 100% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant Abies grandis
4.2.3.120 S485C/F597W replacement with corresponding residue of (-)-camphene synthase, 68% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene Abies grandis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.2.3.119 chloroplast
-
 Abies grandis 9507
-
4.2.3.120 chloroplast
-
 Abies grandis 9507
-

Organism

EC Number Organism UniProt Comment Textmining
4.2.3.117 Abies grandis Q948Z0
-
-
4.2.3.119 Abies grandis O24475
-
-
4.2.3.120 Abies grandis O24475
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.3.119 geranyl diphosphate
-
 Abies grandis (-)-alpha-pinene + diphosphate products are 29% (-)-alpha-pinene, 63% (-)-beta-pinene, 1.8% myrcene, 3.6% limonene ?
4.2.3.120 geranyl diphosphate
-
 Abies grandis (-)-beta-pinene + diphosphate products are 29% (-)-alpha-pinene, 63% (-)-beta-pinene, 1.8% myrcene, 3.6% limonene ?

Synonyms

EC Number Synonyms Comment Organism
4.2.3.117 (-)-pinene synthase
-
 Abies grandis
4.2.3.119 (-)-pinene synthase
-
 Abies grandis
4.2.3.120 (-)-pinene synthase
-
 Abies grandis