4.2.3.120: (-)-beta-pinene synthase
This is an abbreviated version!
For detailed information about (-)-beta-pinene synthase, go to the full flat file.
Reaction
Synonyms
(-)-(1S,5S)-pinene synthase, (-)-pinene synthase, ag9, AvPS, AvTPS1, beta-geraniolene synthase, cyclase II, EC 4.1.99.8, EC 4.2.3.14, mono-tps, More, pinene synthase, QH6, TPS-(-)apin1, TPS-(-)bpin1, TPS-(-)bpin2, TPS1, TPS2, TPS3
ECTree
4.2.3.120 (-)-beta-pinene synthaseAdvanced search results
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results (Engineering
Engineering on EC 4.2.3.120 - (-)-beta-pinene synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
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
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
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
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
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
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
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
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
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
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
L423A/S454A
-
site-directed mutagenesis, mutation M2, the mutant shows altered substrate specificity and product profile compared to the wild-type enzyme
N345A
N345A/L423A/S454A
-
site-directed mutagenesis, mutation M3 enlarges the active site, the mutant shows altered substrate specificity and product profile compared to the wild-type enzyme, the mutant acts as a pinene synthase and produces about 70% pinenes and has about 2fold increase in the yield of overall terpene products
N345A/L423A/S454G
-
site-directed mutagenesis, mutation M5, the mutant shows altered substrate specificity and product profile compared to the wild-type enzyme, products of M5 are composed of 9.8% alpha-pinene, 52.7% beta-pinene and 13.4% limonene, it has about 2fold increase in the yield of overall terpene products
N345G/L423A/S454A
-
site-directed mutagenesis, mutation M4, the mutant shows altered substrate specificity and product profile compared to the wild-type enzyme, products of M4 are composed of 18.81% alpha-pinene, 44.00% beta-pinene, and 16.2% limonene
S454A
S454G
-
site-directed mutagenesis, the mutation enlarges the active site, the mutant shows altered substrate specificity and product profile compared to the wild-type enzyme, the mutant enzyme produces about 46% alpha- and beta-pinenes and only about 52% limonene
additional information
N345A
-
site-directed mutagenesis, the mutation enlarges the active site, the mutant shows altered substrate specificity and product profilecompared to the wild-type enzyme
S454A
-
site-directed mutagenesis, the mutation enlarges the active site, the mutant shows altered substrate specificity and product profile compared to the wild-type enzyme
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
additional information
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S-limonene synthase is converted to pinene or phellandrene synthases by site-directed mutagenesis, product profiles of mutant enzymes, overview
