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Divergent evolution of the thiolase superfamily and chalcone synthase family

Molecular Phylogenetics and Evolution, 2008
Enzymes of the thiolase superfamily catalyze the formation of carbon-carbon bond via the Claisen condensation reaction. Thiolases catalyze the reversible non-decarboxylative condensation of acetoacetyl-CoA from two molecules of acetyl-CoA, and possess a conserved Cys-His catalytic diad.
Sun Young Kim   +2 more
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Evidence for Catalytic Cysteine–Histidine Dyad in Chalcone Synthase

Biochemical and Biophysical Research Communications, 2000
Chalcone and stilbene synthases (CHS and STS) catalyze condensation reactions of p-coumaroyl-CoA and three C(2)-units from malonyl-CoA, but catalyze different cyclization reactions to produce naringenin chalcone and resveratrol, respectively. Condensing activities of wild-type CHS and STS as well as STS-C60S mutant were inhibited by iodoacetamide (Idm)
Ushio Sankawa   +3 more
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Engineered Biosynthesis of Plant Polyketides:  Manipulation of Chalcone Synthase

Organic Letters, 2006
[reaction: see text]. Chalcone synthase (CHS) is a plant-specific type III polyketide synthase catalyzing condensation of 4-coumaroyl-CoA with three molecules of malonyl-CoA. Surprisingly, it was demonstrated that S338V mutant of Scutellaria baicalensis CHS produced octaketides SEK4/SEK4b from eight molecules of malonyl-CoA.
Tatsuya Watanabe   +4 more
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Organization of the genes encoding chalcone synthase in Pisum sativum

Plant Molecular Biology, 1993
To analyze the regulation of defense-related genes by signal molecules produced by phytopathogens, we isolated genes that encode chalcone synthase (CHS) in Pisum sativum. We have obtained seven independent genomic clones that contain at least seven classes of CHS genes, identified by the hybridization analysis to CHS cDNA and by the restriction mapping
Yoshikazu Tanaka   +5 more
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In Trifolium subterraneum, chalcone synthase is encoded by a ultigene family

Gene, 1994
Chalcone synthase (CHS) catalyzes the first and key regulatory step in flavonoid biosynthesis. We report the existence and characterization of a CHS multigene family present in Trifolium subterraneum L. cultivar Karridale. The CHS family consists of at least four members, which are tightly clustered in a 15-kb region.
Tony Arioli   +3 more
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Enzymatic Formation of Unnatural Aromatic Polyketides by Chalcone Synthase

Biochemical and Biophysical Research Communications, 2000
Substrate specificity of recombinant chalcone synthase (CHS) from Scutellaria baicalensis (Labiatae) was investigated using chemically synthesized aromatic and aliphatic CoA esters. It was demonstrated for the first time that CHS converted benzoyl-CoA to phlorobenzophenone (2,4,6-trihydroxybenzophenone) along with pyrone by-products. On the other hand,
Hiroyuki Morita   +3 more
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Characterization and expression analysis of chalcone synthase and chalcone isomerase genes in Phyllanthus emblica (L.)

Journal of Plant Biochemistry and Biotechnology, 2018
The two decisive enzymes in flavonoid biosynthetic pathway are chalcone synthase (CHS) and chalcone isomerase (CHI), wherein the former carries the first committed step of the pathway and later is involved in isomerization of chalcone. In the present study, full-length cDNA sequence of both the genes (PeCHS and PeCHI) from Phyllanthus emblica (L.) were
Kashmir Singh   +4 more
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Transcriptional Control of Chalcone Synthase by Environmental Stimuli

Journal of Plant Research, 2000
UV protectants and antimicrobial compounds phytoalexins. Chalcone synthase (CHS), the key enzyme of flavonoid biosynthesis, is induced by environmental stresses such as UV, mechanical wounding and pathogen attack. Characterization of the cis elements and trans factors involved in CHS expression has enabled delineation of the terminal stage of the ...
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Regulation of Chalcone Synthase with Regard to Anthocyanin Biosynthesis

1989
Cell cultures of an Afghan cultivar of Daucus carota L. (”black carrot”) propagated under dark conditions accumulate large amounts of cyanidin 3-(sinapoyl-xylosylglucosylgalactoside) as the major anthocyanin (Harborne et al. 1983 ; Hopp and Scitz 1987).
H. U. Seitz, J. Gleitz
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