4.2.3.37: epi-isozizaene synthase
This is an abbreviated version!
For detailed information about epi-isozizaene synthase, go to the full flat file.
Word Map on EC 4.2.3.37
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4.2.3.37
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cyclization
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sesquiterpene
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carbocation
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terpenoid
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coelicolor
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tricyclic
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contour
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multistep
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cyclases
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isoprenoid
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pyrophosphate
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remold
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cane
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terpene
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chemodiversity
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product-like
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bisphosphonate
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high-fidelity
- 4.2.3.37
-
cyclization
-
sesquiterpene
-
carbocation
-
terpenoid
- coelicolor
-
tricyclic
-
contour
-
multistep
-
cyclases
-
isoprenoid
- pyrophosphate
-
remold
-
cane
-
terpene
-
chemodiversity
-
product-like
- bisphosphonate
-
high-fidelity
Reaction
Synonyms
EIZS, epi-isozizaene synthase, SAV_3032, SCO5222 protein, TPS2
ECTree
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General Information
General Information on EC 4.2.3.37 - epi-isozizaene synthase
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malfunction
physiological function
substitution of hydrophobic residues with other hydrophobic residues remolds the template and expands product chemodiversity. The substitution of hydrophobic residues, specifically, Y69, F95, F96, and W203, with polar side chains also yields functional enzyme catalysts that expand product chemodiversity. The substitution of polar residues for F96 yields high-fidelity sesquisabinene synthases. Residues defining the three-dimensional contour of the hydrophobic pocket can be substituted without triggering significant structural changes elsewhere in the active site
malfunction
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substitution of hydrophobic residues with other hydrophobic residues remolds the template and expands product chemodiversity. The substitution of hydrophobic residues, specifically, Y69, F95, F96, and W203, with polar side chains also yields functional enzyme catalysts that expand product chemodiversity. The substitution of polar residues for F96 yields high-fidelity sesquisabinene synthases. Residues defining the three-dimensional contour of the hydrophobic pocket can be substituted without triggering significant structural changes elsewhere in the active site
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Streptomyces avermitilis does not produce epi-isozizaene or any of its oxidized derivatives, albaflavenols and albaflavenone, in any culture conditions examined. Recombinant SAV_3032 protein expressed in Escherichia coli catalyses the Mg2+-dependent cyclization of farnesyl diphosphate to epi-isozizaene
physiological function
the sesquiterpene cyclase epi-isozizaene synthase (EIZS) catalyzes the cyclization of farnesyl diphosphate to form the tricyclic hydrocarbon precursor of the antibiotic albaflavenone. The hydrophobic active site pocket of EIZS serves as a template as it binds and chaperones the flexible substrate and carbocation intermediates through the conformations required for a multistep reaction sequence
physiological function
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the sesquiterpene cyclase epi-isozizaene synthase (EIZS) catalyzes the cyclization of farnesyl diphosphate to form the tricyclic hydrocarbon precursor of the antibiotic albaflavenone. The hydrophobic active site pocket of EIZS serves as a template as it binds and chaperones the flexible substrate and carbocation intermediates through the conformations required for a multistep reaction sequence
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