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