Requirement of Catalytic-Triad and Related Amino Acids for the Acyltransferase Activity of<i>Tanacetum cinerariifolium</i>GDSL Lipase/Esterase TcGLIP for Ester-Bond Formation in Pyrethrin Biosynthesis

Kikuta, Yukio; Yamada, Gen; Mitsumori, Tomonori; Takeuchi, Takayuki; Nakayama, Koji; Katsuda, Yoshio; Hatanaka, Akikazu; Matsuda, Kazuhiko

doi:10.1271/bbb.130143

Cited by 11 publications

(16 citation statements)

References 10 publications

(16 reference statements)

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“…In these models of the tomato cutin synthase, i.e., CUS1, it is interesting to note that the conserved Asp and His residues located in Blocks V are closed to the Ser residue located in Block I ( Figure 3 D,E). This means that the catalytic triad could comprise Ser of Block I, and Asp and His residues of Block V, and not Asp from Block III, in agreement with another GDSL lipase with both hydrolase and acyl transferase activities [ 63 ]. Asp of the Block III could be in a calcium binding site by analogy with other lipases, where this site maintains a lid in the open state to allow the entrance of lipids in the catalytic site [ 64 ].…”

Section: Cutin Synthase and The Polymorphism Of The Gdsl-lipase Sumentioning

confidence: 63%

Assembly of the Cutin Polyester: From Cells to Extracellular Cell Walls

Bakan

Marion

2017

Plants

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Cuticular matrices covering aerial plant organs or delimiting compartments in these organs are composed of an insoluble hydrophobic polymer of high molecular mass, i.e., cutin, that encompass some cell wall polysaccharides and is filled by waxes. Cutin is a polyester of hydroxy and-or epoxy fatty acids including a low amount of glycerol. Screening of Arabidopsis and more recently of tomato (Solanum lycopersicum) mutants allowed the delineation of the metabolic pathway involved in the formation of cutin monomers, as well as their translocation in the apoplast. Furthermore, these studies identified an extracellular enzyme involved in the polymerization of these monomers, i.e., cutin synthase 1 (CUS1), an acyl transferase of the GDSL lipase protein family. By comparing the structure of tomato fruit cutins from wild type and down-regulated CUS1 mutants, as well as with the CUS1-catalyzed formation of oligomers in vitro, hypothetical models can be elaborated on the polymerization of cutins. The polymorphism of the GDSL-lipase family raises a number of questions concerning the function of the different isoforms in relation with the formation of a composite material, the cuticle, containing entangled hydrophilic and hydrophobic polymers, i.e., polysaccharides and cutin, and plasticizers, i.e., waxes.

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Section: Cutin Synthase and The Polymorphism Of The Gdsl-lipase Sumentioning

confidence: 63%

Assembly of the Cutin Polyester: From Cells to Extracellular Cell Walls

Bakan

Marion

2017

Plants

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“…The last step in the pyrethrin biosynthetic pathway in T. cinerariifolium , condensation of chrysanthemoyl CoA and pyrethrolone, is reported to be catalyzed by a GDSL esterase/lipase, termed TcGLIP. 6,13 Transcript PK07938.2 for GDSL lipase was fragmentary, so an alternative transcript from the Finola assembly was selected (FN10819.1). An alignment of the putative Cannabis GDSL lipase with the T. cinerariifolium GDSL lipase is shown in figure 5.…”

Section: Resultsmentioning

confidence: 99%

“…5 TcGLIP is generally expressed in the pericarp of seeds rather than trichomes, but its expression in trichomes can be induced. 4,6 Relative expression of these genes depends on the plant stressors present, as pyrethrin production is a defense mechanism. The genetics of many of the enzymes involved in producing pyrethrins, including CDS and TcGLIP have been described previously.…”

Section: Introductionmentioning

confidence: 99%

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Endogenous synthesis of pyrethrins by cannabis

Devitt-Lee

Chen³

et al. 2017

Preprint

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Pyrethrins are a class of natural terpenoid pesticides produced by Tanacetum cinerariifolium, commonly known as chrysanthemum. Here we present evidence that cannabis may be able to produce pyrethrins endogenously. Flower from a cannabis plant grown in a closed hydroponic environment contained 2.48 parts per million pyrethrin I by weight. A comparison of the genetics of T. cinerariifolium and Cannabis demonstrates Cannabis homologues of the genes that contribute to pyrethrins production in T. cinerariifolium. This provides a plausible pathway for the biosynthesis of pyrethrins in cannabis. Although preliminary, these data indicate a potentially significant confounding variable in both cannabis research and regulations on allowable pyrethrins residues in cannabis products.

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“…The SGNH superfamily hydrolases are widespread in eukaryotic and prokaryotic organisms, display broad substrate specificities, and have a diverse range of hydrolytic functions such as thioesterase, protease, lysophospholipase [17], lipase [4], arylesterase [12], carbohydrate esterase [8,18,23], and acyltransferase [14] activities. An assumption is that the broad substrate specificities are because of the flexibility of the active site of the enzymes, according to the experimental data of protease I/thioesterase I/ lysophospholipase L1 from Escherichia coli (TAP) [17], but there are no information about the substrate specificities of other SGNH hydrolases [1].…”

Section: Introductionmentioning

confidence: 99%

Identification and Characterization of a New Alkaline SGNH Hydrolase from a Thermophilic Bacterium Bacillus sp. K91

Ding

Qingxia

et al. 2016

Journal of Microbiology and Biotechnology

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est19 is a gene from Bacillus sp. K91 that encodes a new esterase. A comparison of the amino acid sequence showed that Est19 has typical Ser-Gly-Asn-His (SGNH) family motifs and could be grouped into the SGNH hydrolase family. The Est19 protein was functionally cloned, and expressed and purified from Escherichia coli BL21(DE3). The enzyme activity was optimal at 60°C and pH 9.0, and displayed esterase activity towards esters with short-chain acyl esters (C₂-C₆). A structural model of Est19 was constructed using phospholipase A1 from Streptomyces albidoflavus NA297 as a template. The structure showed an α/β-hydrolase fold and indicated the presence of the typical catalytic triad Ser49-Asp227-His230, which were further investigated by site-directed mutagenesis. To the best of our knowledge, Est19 is a new member of the SGNH hydrolase family identified from thermophiles, which may be applicable in the industrial production of semisynthetic β-lactam antibiotics after modification.

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Requirement of Catalytic-Triad and Related Amino Acids for the Acyltransferase Activity ofTanacetum cinerariifoliumGDSL Lipase/Esterase TcGLIP for Ester-Bond Formation in Pyrethrin Biosynthesis

Cited by 11 publications

References 10 publications

Assembly of the Cutin Polyester: From Cells to Extracellular Cell Walls

Assembly of the Cutin Polyester: From Cells to Extracellular Cell Walls

Endogenous synthesis of pyrethrins by cannabis

Identification and Characterization of a New Alkaline SGNH Hydrolase from a Thermophilic Bacterium Bacillus sp. K91

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