1.14.14.126: beta-amyrin 28-monooxygenase
This is an abbreviated version!
For detailed information about beta-amyrin 28-monooxygenase, go to the full flat file.
Word Map on EC 1.14.14.126
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1.14.14.126
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triterpenoids
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oleanolic
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cyp716as
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2,3-oxidosqualene
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oleanane-type
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lupeol
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erythrodiol
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sapogenins
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oxidosqualene
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hederagenin
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amyrins
- 1.14.14.126
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triterpenoids
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oleanolic
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cyp716as
- 2,3-oxidosqualene
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oleanane-type
- lupeol
- erythrodiol
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sapogenins
- oxidosqualene
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hederagenin
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amyrins
Reaction
+ 3 O2 + 3 [reduced NADPH-hemoprotein reductase] = + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
Synonyms
101251676, 101252702, alpha-amyrin 28-hydroxylase, amyrin C-28 oxidase, beta-amyrin 28-hydroxylase, beta-amyrin 28-oxidase, C-28 oxidase, CYP716A12, CYP716A140v2, CYP716A141, CYP716A15, CYP716A17, CYP716A175, CYP716A179, CYP716A244, CYP716A253, CYP716A254, CYP716A44, CYP716A46, CYP716A52v2, CYP716A94, EC 1.14.13.201, lupeol 28-hydroxylase, More, multifunctional oxidase, multifunctional P450, multifunctional triterpene C-28 oxidase, triterpene C-28 oxidase, triterpene monooxygenase
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General Information
General Information on EC 1.14.14.126 - beta-amyrin 28-monooxygenase
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evolution
metabolism
physiological function
additional information
the enzyme belongs to the CYP716A subfamily of cytochrome P450 monooxygenases
evolution
EB148173
CYP716A175 is clearly grouped with the CYP716A subfamily. Expression patterns of triterpene-related genes in different apple cultivars, overview
evolution
the enzyme belongs to the CYP716C subfamily, many CYP716 family P450 enzymes are characterized as multifunctional triterpene C-28 oxidases, which oxidize alpha-amyrin and beta-amyrin to the widely distributed triterpenoids ursolic and oleanolic acids, respectively. Isolation of all six CYP716 family genes from tomato, including CYP716A46, and sequence comparisons
evolution
the enzyme belongs to the CYP716C subfamily, many CYP716 family P450 enzymes are characterized as multifunctional triterpene C-28 oxidases, which oxidize alpha-amyrin and beta-amyrin to the widely distributed triterpenoids ursolic and oleanolic acids, respectively. Isolation of all six CYP716 family genes from tomato, including gene CYP716A44, and sequence comparisons
the enzyme is involved in the biosynthesis of oleanane-type triterpenoids, such as ginsenoside Ro
metabolism
cytochrome P450 monooxygenase CYP716A254 is involved in oleanane-type triterpenoid saponins biosynthesis, i.e. the biosynthesis of oleanolic acid, which involves cyclization of 2,3-oxidosqualene to the oleanane-type triterpenoid skeleton, followed by a series of oxidation reactions catalyzed by cytochrome P450 monooxygenase (CYP450), Proposed biosynthetic pathway for oleanolic acid in Anemone flaccida, overview
metabolism
enzymes CYP716A252 and CYP716A253 catalyze sequential three-step oxidation at the C-28 position of alpha-amyrin and beta-amyrin to produce ursolic acid and oleanolic acid, respectively, essential roles for both of these CYP716As in constitutive biosynthesis of ursolic acid and oleanolic acid in sweet basil leaves, similar as well as distinct roles of CYP716A252 and CYP716A253 for the spatio-temporal biosynthesis of pentacyclic triterpenes. The cyclization of 2,3-oxidosqualene into either of two structural isomers, alpha-amyrin or beta-amyrin is the initial diversifying step for ursolic acid and oleanolic acid biosynthesis, pathway overview
metabolism
the enzyme catalyzes a step in the putative saponin biosynthetic pathway from 2,3-oxidosqualene to hederagenin saponin, overview. Two enzymes (beta-amyrin synthase and beta-amyrin 28-oxidase) are essential for oleanane-type saponin biosynthesis from 2,3-oxidosqualene
metabolism
oleanane-type triterpenes are the major saponin components in Eleutherococcus senticosus. The two enzymes, beta-amyrin synthase and beta-amyrin 28-oxidase, are essential for oleanane-type saponin biosynthesis from 2,3-oxidosqualene
metabolism
the enzyme is involved in the triterpenoid biosynthesis in tomato
F8J4R7
enzyme is responsible for an early step in the saponin biosynthetic pathway. Mutants in CYP716A12 are unable to produce hemolytic saponins and only synthetize soyasaponins. CYP716A12 catalyzes the oxidation of beta-amyrin and erythrodiol at the C-28 position, yielding oleanolic acid
physiological function
CYP716A140v2, catalyzed a three-step oxidation reaction at C-28 on beta-amyrin to produce oleanolic acid, a reaction performed by CYP716A subfamily P450s in a variety of plant species
physiological function
CYP716A244 is a beta-amyrin 28-oxidase involved in saponin biosynthesis, beta-amyrin is the oleanane-type triterpene backbone. beta-Amyrin is oxidised at the C-28 position in a sequential three-step oxidation by the single cytochrome P450 enzyme to yield oleanolic acid through erythrodiol
physiological function
CYP716A94 is a beta-amyrin 28-oxidase for the production of oleanolic acid
physiological function
cytochrome P450 monooxygenase CYP716A254 catalyzes the formation of oleanolic acid from beta-amyrin during oleanane-type triterpenoid saponins biosynthesis. Oleanolic acid is natural triterpenoid in plants with diverse biological activities
physiological function
the medicinal plant sweet basil (Ocimum basilicum) accumulates bioactive ursane- and oleanane-type pentacyclic triterpenes (PCTs), ursolic acid and oleanolic acid, respectively, in a spatio-temporal manner. Major role for CYP716A253 and a minor role for CYP716A252 in determining elicitor-induced biosynthesis of ursolic acid and oleanolic acid
enzyme CYP716A253 contains conserved amino acid motifs characteristic of bona fide CYP450s includig the highly conserved heme-binding motif FxxGxRxCxG at the C-terminal end, an EXXR.-.R motif (ERR triad) that maintains protein tertiary structure and positioning of the heme pocket, an A/GGXD/ET motif that participates in oxygen binding and activation, and a proline-rich and a hydrophobic regions at the N-terminal end
additional information
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enzyme CYP716A253 contains conserved amino acid motifs characteristic of bona fide CYP450s includig the highly conserved heme-binding motif FxxGxRxCxG at the C-terminal end, an EXXR.-.R motif (ERR triad) that maintains protein tertiary structure and positioning of the heme pocket, an A/GGXD/ET motif that participates in oxygen binding and activation, and a proline-rich and a hydrophobic regions at the N-terminal end