p<i>‐Coumaroyltriacetic acid synthase, a new homologue of chalcone synthase, from </i>Hydrangea macrophylla<i> var. </i>thunbergii

Akiyama, Takumi; Shibuya, Masabumi; Liu, Hong‐Min; Ebizuka, Yutaka

doi:10.1046/j.1432-1327.1999.00562.x

Cited by 87 publications

(114 citation statements)

References 19 publications

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“…This suggests potentially different strategies for the engineered biosynthesis of novel pharmaceutically relevant polyketides. [41]. A comparison between the amino acid sequences of H. macrophylla CHS and CTAS showed 76% identity and only 12 amino acid residues which were significantly different in charge and size.…”

Section: Truncation Products and Chain Length Specificitymentioning

confidence: 94%

“…3,5-Dihydroxyphenylacetic acid synthase from Amycolatopsis mediterranei (DpgA) catalyzes the decarboxylative condensation of four units of malonyl-CoA, followed by a likely C8 to C3 aldol condensation to yield 3,5-dihydroxyphenylacetic acid (41,Scheme 14). The compound is a precursor of (S)-3,5-dihydroxyphenylglycine, an amino acid utilized in the biosynthesis of balhimycin, a vancomycin derivative [18].…”

Section: -Dihydroxyphenylacetic Acid Synthasementioning

confidence: 99%

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Exploiting the Biosynthetic Potential of Type III Polyketide Synthases

Lim

Yew

2016

Molecules

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Abstract:Polyketides are structurally and functionally diverse secondary metabolites that are biosynthesized by polyketide synthases (PKSs) using acyl-CoA precursors. Recent studies in the engineering and structural characterization of PKSs have facilitated the use of target enzymes as biocatalysts to produce novel functionally optimized polyketides. These compounds may serve as potential drug leads. This review summarizes the insights gained from research on type III PKSs, from the discovery of chalcone synthase in plants to novel PKSs in bacteria and fungi. To date, at least 15 families of type III PKSs have been characterized, highlighting the utility of PKSs in the development of natural product libraries for therapeutic development.

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Section: Truncation Products and Chain Length Specificitymentioning

confidence: 94%

Section: -Dihydroxyphenylacetic Acid Synthasementioning

confidence: 99%

Exploiting the Biosynthetic Potential of Type III Polyketide Synthases

Lim

Yew

2016

Molecules

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“…STS catalyzes a similar reaction to CHS to form a tetraketide chain, which is subsequently subjected to a C2/C7 cyclization instead of C1/C6 cyclization, leading to the formation of resveratrol after a step of decarboxylation (11). CTAS synthesizes the same polyketide chain, while giving rise to 4-coumaroyl triacetic acid lactone through a C1/C5 cyclization (12).…”

Section: Plant Type III Pkssmentioning

confidence: 99%

Type III polyketide synthases in natural product biosynthesis

et al. 2012

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SummaryPolyketides represent an important class of biologically active and structurally diverse compounds in nature. They are synthesized from acyl-coenzyme A substrates by polyketide synthases (PKSs). PKSs are classified into three groups: types I, II, and III. This article introduces recent studies on type III PKSs identified from plants, bacteria, and fungi, and describes the catalytic functions of these enzymes in detail. Plant type III PKSs have been widely studied, as exemplified by chalcone synthase, which plays an important role in the synthesis of plant metabolites. Bacterial type III PKSs fall into five groups, many of which were identified from Streptomyces, a genus that has been well known for its production of bioactive molecules and genetic alterability. Although it was believed that type III PKSs exist exclusively in plants and bacteria, recent fungal genome sequencing projects and biochemical studies revealed the presence of type III PKSs in filamentous fungi, which provides a new chance to study fungal secondary metabolism and synthesize ''unnatural'' natural products. Type III PKSs have been used for the biosynthesis of novel molecules through precursordirected and structure-based mutagenesis approaches.2012 IUBMB IUBMB Life, 64(4): [285][286][287][288][289][290][291][292][293][294][295] 2012

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“…Benzalacetone synthase (BAS) (EC 2.3.1.-) catalyzes a one-step decarboxylative condensation of 4-coumaroyl-CoA (1) with malonylCoA (2) to produce a diketide benzalacetone (4) (Fig. 1), whereas CHS (EC 2.3.1.74) performs sequential condensations of 4-coumaroyl-CoA with three acetate units from malonyl-CoA followed by a Claisen-type cyclization reaction, leading to formation of a tetraketide naringenin chalcone (6).…”

mentioning

confidence: 99%

“…1), whereas CHS (EC 2.3.1.74) performs sequential condensations of 4-coumaroyl-CoA with three acetate units from malonyl-CoA followed by a Claisen-type cyclization reaction, leading to formation of a tetraketide naringenin chalcone (6). Further, in the CHS enzyme reaction in vitro, a triketide and a tetraketide pyrone, bisnoryangonin (BNY) (3, 4) and 4-coumaroyltriacetic acid lactone (CTAL) (4,5) are also obtained as early released derailment by-products when the reaction mixtures are acidified before extraction (Fig. 1).…”

mentioning

confidence: 99%

Site-directed Mutagenesis of Benzalacetone Synthase

Abe

Sano

Takahashi

et al. 2003

Journal of Biological Chemistry

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Benzalacetone synthase (BAS) and chalcone synthase (CHS) are plant-specific type III polyketide synthases (PKSs) that share ϳ70% amino acid sequence identity. BAS catalyzes a one-step decarboxylative condensation of 4-coumaroyl-CoA with malonyl-CoA to produce a diketide benzalacetone, whereas CHS performs sequential condensations with three malonyl-CoA to generate a tetraketide chalcone. A homology model suggested that BAS has the same overall fold as CHS with cavity volume almost as large as that of CHS. One of the most characteristic features is that Rheum palmatum BAS lacks active site Phe-215; the residues 214 LF conserved in type III PKSs are uniquely replaced by IL. Our observation that the BAS I214L/L215F mutant exhibited chalcone-forming activity in a pH-dependent manner supported a hypothesis that the absence of Phe-215 in BAS accounts for the interruption of the polyketide chain elongation at the diketide stage. On the other hand, Phe-215 mutants of Scutellaria baicalensis CHS (L214I/ F215L, F215W, F215Y, F215S, F215A, F215H, and F215C) afforded increased levels of truncated products; however, none of them generated benzalacetone. These results confirmed the critical role of Phe-215 in the polyketide formation reactions and provided structural basis for understanding the structure-function relationship of the plant type III PKSs.

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p‐Coumaroyltriacetic acid synthase, a new homologue of chalcone synthase, from Hydrangea macrophylla var. thunbergii

Cited by 87 publications

References 19 publications

Exploiting the Biosynthetic Potential of Type III Polyketide Synthases

Exploiting the Biosynthetic Potential of Type III Polyketide Synthases

Type III polyketide synthases in natural product biosynthesis

Site-directed Mutagenesis of Benzalacetone Synthase

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