5.4.99.39: beta-amyrin synthase
This is an abbreviated version!
For detailed information about beta-amyrin synthase, go to the full flat file.
Word Map on EC 5.4.99.39
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5.4.99.39
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triterpene
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oxidosqualene
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saponin
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triterpenoids
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lupeol
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cyclases
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glycyrrhiza
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cycloartenol
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oleanolic
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lanosterol
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uralensis
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oleanane-type
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2,3-oxidosqualene
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oleanane
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dammarenediol
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soyasapogenol
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synthesis
- 5.4.99.39
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triterpene
- oxidosqualene
- saponin
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triterpenoids
- lupeol
- cyclases
- glycyrrhiza
- cycloartenol
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oleanolic
- lanosterol
- uralensis
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oleanane-type
- 2,3-oxidosqualene
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oleanane
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dammarenediol
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soyasapogenol
- synthesis
Reaction
Synonyms
AMS1, amyrin synthase, B-AS, bAS, BAS-like 2, BAS1, BAS2, beta-amyrin cyclase, beta-amyrin synthase, beta-AS, betaAS, BPY, CbbAS, CrAS, EsBAS, EtAS, GmAMS1, GsAS1, GsAS2, MdOSC1, MtAMY1, multifunctional OSC, ObAS1, OPSC 1, OSC, OSC1, OSC2, OXA1, Oxidosqualene cyclase, PBA, PlgOSC1, PNY, PSY, PtBS, SITTS1, SlTTS1, SvBS
ECTree
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General Information
General Information on EC 5.4.99.39 - beta-amyrin synthase
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evolution
malfunction
metabolism
physiological function
additional information
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analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
evolution
H9NAL5
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
evolution
PlgOSC1 not only contains a DCTAE motif that is implicated in substrate binding, but also has four repeats of the QXXXGXW motif, which is a typical feature of the triterpene synthase superfamily. PlgOSC1 has a Try residue in the MWCYCR motif that plays a role in the formation of beta-amyrin
evolution
residue F474 of Euphorbia tirucalli beta-amyrin cyclase is highly conserved in the superfamily of oxidosqualene cyclases
evolution
the enzyme is a member of the oxidosqualene cyclase (OSC) family
evolution
the sequence of the mature protein contains the highly conserved motifs (QXXXGXW/DCTAE) of OSCs and (MWCYCR) of beta-amyrin synthases
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saponin biosynthesis in soybean seeds is suppressed through RNA interference-mediated beta-amyrin synthase gene silencing
malfunction
enzyme mutant F474A and F474G produces significantly larger amounts of the bicyclic products and a decreased amount of beta-amyrin compared to wild-type. The mutant variant F474A produces (9betaH)-polypoda-7,13,17,21-tetraen-3beta-ol and (9betaH)-polypoda-8(26),13,17,21-tetraen-3beta-ol, which are generated from a chair-boat folding conformation. Substitutions with aliphatic amino acids lacking Pi-electrons such as Val, Leu, and Met lead to a significantly decreased production of bicyclic compounds, and in turn exhibit a higher production of beta-amyrin
malfunction
RNAi-directed suppression of GsAS1 in Gentiana straminea decreases oleonolic acid levels by 65.9%
malfunction
RNAi-directed suppression of GsAS2 in Gentiana straminea decreasing oleonolic acid levels by 21.0%
malfunction
the Gly and Ala variants with a smaller bulk size at position 483, compared to wild-type Val483, predominantly afford monocyclic camelliol C, which suggests that the orientation of the (3S)-2,3-oxidosqualene substrate is not appropriately arranged in the reaction cavity as a result of the decreased bulk size, leading to failure of its normal folding into the chair-chair-chair-boat-boat conformation. The Ile variant, with a somewhat larger bulk, affords beta-amyrin as the dominant product. Various point mutants of Trp534 exhibit significantly decreased enzymatic activities and provide no aberrantly cyclized products, although the aromatic Phe and Tyr residues are incorporated and the steric sizes of the aliphatic residues are altered. Therefore, the Trp534 residue does not stabilize the transient cation through a cation-Pi interaction. Altering the steric bulk at the Met729 position afforded the pentacyclic skeletons
malfunction
the Y259F variant shows nearly equivalent activity to that of the wild type, but aliphatic mutants such as the Ala, Val, and Leu variants show significantly decreased activity and yield the tetracyclic dammarane scaffold. The aliphatic variants of Trp257 exhibit remarkably decreased enzymatic activity, and lupeol is produced in a high production ratio. The aromatic Phe and Tyr mutants exhibit high activities owing to their more increased Pi-electron density relative to that of the aliphatic mutants, but lupeol is produced in a significantly high yield besides beta-amyrin. The Trp residue is likely to be responsible for the robust binding of Me-30 through CH-Pi interaction. The decreased Pi-electron density of the Phe and Tyr mutants compared to that of Trp results in the high production of lupeol
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expression of PtBS in the triterpenoid synthase-deficient yeast mutant GIL77 leads to the production of beta-amyrin as sole product
metabolism
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functional expression of ObAS1 in Saccharomyces cerevisiae leads to the production of beta-amyrin
metabolism
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beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
metabolism
H9NAL5
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
metabolism
MdOSC1 and MdOSC5 are key genes in apple fruit triterpene biosynthesis, analysis of biosynthetic pathway of triterpenic acids in apple, overview. The gene expression of MdOSC1 is linked to the concentrations of ursolic and oleanolic acid
metabolism
the enzyme is involved in the putative saponin biosynthetic pathway from 2,3-oxidosqualene in Eleutherococcus senticosus, overview
metabolism
the enzyme plays a key role in the biosynthesis of triterpenoid saponins
metabolism
the enzyme synthesizes beta-amyrin, a central precursor in the platycoside biosynthesis pathway, overview. 69 platycosides are identified from Platycodon grandiflorum
beta-amyrin in Eleutherococcus senticosus may play a key role in saponin biosynthesis
physiological function
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beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
H9NAL5
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
Conyza blinii is a widely used medicinal herb in southwestern China. The main pharmacological components of Conyza blinii are a class of oleanane-type pentacyclic triterpene glycosides, known as conyzasaponins, which are thought to be synthesized from beta-amyrin. The beta-amyrin synthase mediates cyclization of 2,3-oxidosqualene to yield beta-amyrin. The enzyme is an oxidosqualene cyclase (OSC) involved in conyzasaponin biosynthesis
physiological function
GsAS2 plays a more important role than GsAS1 in oleanolic acid biosynthesis in Gentiana straminea. Wild-type GsAS1 and mutant GsAS1 H560Y show 7-11% of wild-type GSAS2 activity
physiological function
the enzyme is involved in the biosynthesis of pentacyclic triterpenes, which, in apple, account for 32-70% of the epicuticular waxes, depending on the cultivar
physiological function
the enzyme plays a key role in the biosynthesis of triterpenoid saponins
analysis of triterpenes from apple fruits in a collection of 20 contrasting apple cultivars, expression patterns of triterpene-related genes in different apple cultivars, overview
additional information
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analysis of triterpenes from apple fruits in a collection of 20 contrasting apple cultivars, expression patterns of triterpene-related genes in different apple cultivars, overview
additional information
beta-AS of Panax japonicus does not cross the membrane, three-dimensional enzyme structure modeling
additional information
beta-AS of Panax quinquefolius does not cross the membrane, three-dimensional enzyme structure modeling
additional information
catalytically important residue F474 residue is located near the B-ring formation site. The major role of Phe474 is not to stabilize the transient cation via cation-Pi interaction, but is to confer the appropriate steric bulk near the B-ring formation site, leading to the completion of the normal polycyclization pathway without accumulation of abortive cyclization products
additional information
the highly conserved aromatic residues Phe413, Tyr259 and Trp257 disclose the importance of the appropriate steric bulk, and cation-Pi and CH-Pi interactions for the efficient catalytic action of the polyolefin cyclization cascade, functional analysis, overview. Homology modeling of beta-amyrin synthase using the X-ray crystal structure of human lanosterol cyclase, PDB ID 1w6k, as template. Structure comparisons. The Tyr259 residue stabilizes the baccharenyl secondary cation via cation-Pi interaction, residue Trp257 stabilizes the oleanyl cation via cation-Pi interaction
additional information
the intronless beta-amyrin synthase gene GSAS2 is more efficient in oleanolic acid accumulation than its paralogue GsAS1 in Gentiana straminea. Both enzymes harbor two (alpha/alpha) barrel domains connected by loops, as well as three smaller beta structures
additional information
the intronless beta-amyrin synthase gene GSAS2 is more efficient in oleanolic acid accumulation than its paralogue GsAS1 in Gentiana straminea. Both enzymes harbor two (alpha/alpha) barrel domains connected by loops, as well as three smaller beta structures
additional information
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the intronless beta-amyrin synthase gene GSAS2 is more efficient in oleanolic acid accumulation than its paralogue GsAS1 in Gentiana straminea. Both enzymes harbor two (alpha/alpha) barrel domains connected by loops, as well as three smaller beta structures
additional information
the Trp534 residue does not stabilize the transient cation through a cation-Pi interaction. the Trp residue, with the largest steric bulk among all natural amino acids, is essential for high enzymatic activity. Robust CH-Pi complexation between the Val483 and Trp534 residues is proposed. Met729 is positioned at the E-ring formation site. Homology modeling and structure-function analysis, overview