4.2.3.89: (+)-beta-caryophyllene synthase
This is an abbreviated version!
For detailed information about (+)-beta-caryophyllene synthase, go to the full flat file.
Reaction
Synonyms
(E)-beta-caryophyllene synthase, BCS, beta-caryophyllene synthase, CsSesquiTPS6a, CsSesquiTPS6b, CsSesquiTPS6c, DcTPS1, E-(beta)-caryophyllene synthase, GcoA, More, OkBCS, PlCAHS, PnCPS, PnTPS1, RtTPS1, RtTPS3, SQS6a, SQS6b, SQS7, TPS1, tps23, TPS3, VvGwECar2, WtDcTPS
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General Information
General Information on EC 4.2.3.89 - (+)-beta-caryophyllene synthase
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evolution
metabolism
physiological function
additional information
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gene WtDcTPS1 exhibits highly conserved sequences of plant TPSs including the asparate-rich motif DDxxD and the RxR motif, both of which are involved in catalysis
evolution
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in grapevine five genes are known to code for beta-caryophyllene synthases, but only one of them, VvGwECar2, is actually expressed in all plant tissues and therefore accounts for most of the volatile production in vegetative parts and berries, although in flowers two other genes, VvGwECar1 and VvPNECar2, seem to play a big role
evolution
isozyme RtTPS1 contains all the conserved domains of the TPS family, including the RR(P)X8W, RXR, and DDXXD (X is any amino acid) motifs, and absolutely conserved arginine, cysteine and histidine residues in active-site
evolution
isozyme RtTPS3 contains all the conserved domains of the TPS family, including the RR(P)X8W, RXR, and DDXXD (X is any amino acid) motifs, and absolutely conserved arginine, cysteine and histidine residues in active-site
evolution
the cyclization process catalyzed by PnTPSs follows a 1,10-closure mechanism assuming that the present PnTPSs have evolved from a common ancestor
evolution
the enzyme belongs to the terpene synthase (TPS) family
evolution
the enzyme belongs to the terpene synthase family, TPS-a subfamily
evolution
the enzyme belongs to typical class of sesquiterpene synthases from angiosperms, clade TPS-a. Across five Ocimum species, OkBCS shows the highest expression in Ocimum kilimandscharicum followed by Ocimum americanum, Ocimum tenuiflorum, and Ocimum gratissimum while Ocimum basilicum hadve trace levels
beta-caryophyllene is produced via the mevalonate (MVA)-mediated pathway, overview
metabolism
GC/MS profiling of terpenes from immature black pepper fruit, accumulation of beta-caryophyllene, the major sesquiterpene in peppercorn, changes from 46% to 70% as fruits ripen
metabolism
putative alpha-pinene and beta-caryophyllene biosynthesis pathway
(E)-beta-caryophyllene synthase is a possible key enzyme of plant defence
physiological function
agro-infiltration based transient expression manipulation with OkBCS overexpression and silencing confirms its role in beta-caryophyllene biosynthesis
physiological function
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the TPS enzyme (VvGwECar2) is responsible for most of the production of E-(beta)-caryophyllene in grapevine (VvGwECar2). It might play a key role in the plant regulation machinery
isozymes RtTPS1-4 mainly produce (+)-alpha-pinene and (+)-beta-pinene, as well as small amounts of (-)-alpha-pinene and (-)-beta-pinene with geranyl diphosphate, while RtTPS1 and RtTPS3 are also active with farnesyl diphosphate, producing beta-caryophyllene (65.71% for RtTPS1 and 93.05% for RtTPS3), along with a smaller amount of alpha-humulene (4.29% for RtTPS1 and 6.95% for RtTPS3). alpha/beta-Pinene, beta-caryophyllene, and alpha-humulene constitute the major active components in Rhodomyrtus tomentosa. Among them, (+)-alpha-pinene and beta-caryophyllene are most abundant in the leaves
additional information
isozymes RtTPS1-4 mainly produce (+)-alpha-pinene and (+)-beta-pinene, as well as small amounts of (-)-alpha-pinene and (-)-beta-pinene with geranyl diphosphate, while RtTPS1 and RtTPS3 are also active with farnesyl diphosphate, producing beta-caryophyllene (65.71% for RtTPS1 and 93.05% for RtTPS3), along with a smaller amount of alpha-humulene (4.29% for RtTPS1 and 6.95% for RtTPS3). alpha/beta-Pinene, beta-caryophyllene, and alpha-humulene constitute the major active components in Rhodomyrtus tomentosa. Among them, (+)-alpha-pinene and beta-caryophyllene are most abundant in the leaves
additional information
isozymes RtTPS1-4 mainly produce (+)-alpha-pinene and (+)-beta-pinene, as well as small amounts of (-)-alpha-pinene and (-)-beta-pinene with GPP, while RtTPS1 and RtTPS3 are also active with FPP, producing beta-caryophyllene (65.71% for RtTPS1 and 93.05% for RtTPS3), along with a smaller amount of alpha-humulene (4.29% for RtTPS1 and 6.95% for RtTPS3). alpha/beta-Pinene, beta-caryophyllene, and alpha-humulene constitute the major active components in Rhodomyrtus tomentosa. Among them, (+)-alpha-pinene and beta-caryophyllene are most abundant in the leaves
additional information
isozymes RtTPS1-4 mainly produce (+)-alpha-pinene and (+)-beta-pinene, as well as small amounts of (-)-alpha-pinene and (-)-beta-pinene with GPP, while RtTPS1 and RtTPS3 are also active with FPP, producing beta-caryophyllene (65.71% for RtTPS1 and 93.05% for RtTPS3), along with a smaller amount of alpha-humulene (4.29% for RtTPS1 and 6.95% for RtTPS3). alpha/beta-Pinene, beta-caryophyllene, and alpha-humulene constitute the major active components in Rhodomyrtus tomentosa. Among them, (+)-alpha-pinene and beta-caryophyllene are most abundant in the leaves
additional information
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monoterpene contents comparisons of different wild accessions of carrot. In cell-free extracts from carrot fruit pericarp of wild accession 23727, the monoterpenes contained are geraniol, sabinene, limonene, alpha-pinene, beta-pinene, beta-myrcene, and alpha-phellandrene and the sesquiterpenes are E-beta-caryophellene, E-beta-farnesene, and alpha-humelene
additional information
three-dimensional structure homology modelling using the crystal structure of the delta-cadinene synthase from Gossypium. The functional C-terminal domain consists of 14 alpha-helices forming a central cavity and the amino terminal domain formed by two 10 antiparallel alpha-helices. The aspartate-rich motifs DDXXD (located on helix-alpha-13) and NSE/DTE motif (located helix alpha-20) are both involved in binding a trio of divalent magnesium ions, co-orientated to the catalytic pocket
additional information
three-dimensional structure homology modelling using the crystal structure of the delta-cadinene synthase from Gossypium. The functional C-terminal domain consists of 14 alpha-helices forming a central cavity and the amino terminal domain formed by two 10 antiparallel alpha-helices. The aspartate-rich motifs DDXXD (located on helix-alpha-13) and NSE/DTE motif (located helix alpha-20) are both involved in binding a trio of divalent magnesium ions, co-orientated to the catalytic pocket
additional information
three-dimensional structure homology modelling using the crystal structure of the delta-cadinene synthase from Gossypium. The functional C-terminal domain consists of 14 alpha-helices forming a central cavity and the amino terminal domain formed by two 10 antiparallel alpha-helices. The aspartate-rich motifs DDXXD (located on helix-alpha-13) and NSE/DTE motif (located helix alpha-20) are both involved in binding a trio of divalent magnesium ions, co-orientated to the catalytic pocket
additional information
three-dmensional structure homology modelling using the crystal structure of the delta-cadinene synthase from Gossypium. The functional C-terminal domain consists of 14 alpha-helices forming a central cavity and the amino terminal domain formed by two 10 antiparallel alpha-helices. The aspartate-rich motifs DDXXD (located on helix-alpha-13) and NSE/DTE motif (located helix alpha-20) are both involved in binding a trio of divalent magnesium ions, co-orientated to the catalytic pocket
additional information
three-dmensional structure homology modelling using the crystal structure of the delta-cadinene synthase from Gossypium. The functional C-terminal domain consists of 14 alpha-helices forming a central cavity and the amino terminal domain formed by two 10 antiparallel alpha-helices. The aspartate-rich motifs DDXXD (located on helix-alpha-13) and NSE/DTE motif (located helix alpha-20) are both involved in binding a trio of divalent magnesium ions, co-orientated to the catalytic pocket
additional information
three-dmensional structure homology modelling using the crystal structure of the delta-cadinene synthase from Gossypium. The functional C-terminal domain consists of 14 alpha-helices forming a central cavity and the amino terminal domain formed by two 10 antiparallel alpha-helices. The aspartate-rich motifs DDXXD (located on helix-alpha-13) and NSE/DTE motif (located helix alpha-20) are both involved in binding a trio of divalent magnesium ions, co-orientated to the catalytic pocket