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Results 1 - 7 of 7
EC Number
General Information
Commentary
Reference
evolution
the enzyme belongs to the sesquiterpene synthases
malfunction
identification of constitutive photomorphogenic mutants, cop2, cop3, and cop4,in which dark-grown seedlings have open and enlarged cotyledons resembling those of light-grown wild-type seedlings. Mutations in each of the three loci alleviate the normal inhibition of cell-type differentiation, cell enlargement, and lateral cell division observed in cotyledons of dark-grown wild-type seedlings, but do not affect plastid differentiation. Cop4 mutation also leads to high-leve1 dark expression of nuclear, but not plastid-encoded, light-inducible genes
metabolism
epistatic relationships of these three mutations to previously characterized phytochrome-deficient mutations suggest that COP2, COP3, and COP4 may act downstream of phytochrome in the light regulatory pathway
more
directed mutations of the H-alpha1 loop have a marked effect on the product profile Cop4, loop mutations in Cop4 also implicate specific residues responsible for the pH sensitivity of the enzyme. In vivo analysis of sesquiterpene product profiles of H-alpha1 loop mutants, overview. Mutation of K233, presumed to interact with the second Asp92 in the DDXXD motif of Cop4, does not significantly change the overall product promiscuity of Cop4, though beta-cubebene, with 27% of total sesquiterpene products, does become the major product
more
structural modeling, structure-function relationship, overview. Changing the pH of the reaction drastically alters the fidelity of Cop4 and makes it a highly selective enzyme
physiological function
the COP4 locus may be involved in both light-signaling and gravity-sensing processes. COP4 modulates cabl promoter activity through a pathway distinct from that of COPl and COP9, nuclear cabl gene encodes a chlorophyll alb binding protein of the photosynthetic light-harvesting complex. Modulation of cabl promoter activity by light and by the cop4 mutation
physiological function
the enzyme belongs to the sesquiterpene synthases that are responsible for the cyclization of farnesyl diphosphate into a myriad of structurally diverse compounds with various biological activities
Results 1 - 7 of 7