Insights into β-Ketoacyl-Chain Recognition for β-Ketoacyl-ACP Utilizing AHL Synthases

Mila Nhu Lam; Dastagiri Dudekula; Bri Durham; Noah Collingwood; Eric C. Brown; Rajesh Nagarajan

doi:10.1039/c8cc04532a

Insights into β-Ketoacyl-Chain Recognition for β-Ketoacyl-ACP Utilizing AHL Synthases

Mila Nhu Lam, Dastagiri Dudekula, Bri Durham, Noah Collingwood, Eric C. Brown, Rajesh Nagarajan

Chemistry Department

Boise State University

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

Beta-ketoacyl-ACP utilizing enzymes in fatty acid, polyketide and acyl-homoserine lactone biosynthetic pathways are important targets for developing antimicrobial, anticancer and antiparasitic compounds. Published reports on successful isolation of beta-ketoacyl-ACPs in a laboratory remain scarce to date and thus most beta-ketoacyl-ACP utilizing enzymes are routinely characterized using small molecule substrates in lieu of the bonafide 3-oxoacyl-ACPs. We report the systematic investigation into the electronic, geometric and spatial aspects of beta-ketoacyl-chain recognition to develop 3-oxoacyl-ACP substrate mimics for two beta-ketoacyl-ACP utilizing quorum signal synthases.

Original language	American English
Journal	Chemical Communications
DOIs	https://doi.org/10.1039/c8cc04532a
State	Published - 18 Aug 2018

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Chemistry

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http://dx.doi.org/10.1039/c8cc04532a

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title = "Insights into β-Ketoacyl-Chain Recognition for β-Ketoacyl-ACP Utilizing AHL Synthases",

abstract = " Beta-ketoacyl-ACP utilizing enzymes in fatty acid, polyketide and acyl-homoserine lactone biosynthetic pathways are important targets for developing antimicrobial, anticancer and antiparasitic compounds. Published reports on successful isolation of beta-ketoacyl-ACPs in a laboratory remain scarce to date and thus most beta-ketoacyl-ACP utilizing enzymes are routinely characterized using small molecule substrates in lieu of the bonafide 3-oxoacyl-ACPs. We report the systematic investigation into the electronic, geometric and spatial aspects of beta-ketoacyl-chain recognition to develop 3-oxoacyl-ACP substrate mimics for two beta-ketoacyl-ACP utilizing quorum signal synthases.",

author = "Lam, {Mila Nhu} and Dastagiri Dudekula and Bri Durham and Noah Collingwood and Brown, {Eric C.} and Rajesh Nagarajan",

year = "2018",

month = aug,

day = "18",

doi = "10.1039/c8cc04532a",

language = "American English",

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TY - JOUR

T1 - Insights into β-Ketoacyl-Chain Recognition for β-Ketoacyl-ACP Utilizing AHL Synthases

AU - Lam, Mila Nhu

AU - Dudekula, Dastagiri

AU - Durham, Bri

AU - Collingwood, Noah

AU - Brown, Eric C.

AU - Nagarajan, Rajesh

PY - 2018/8/18

Y1 - 2018/8/18

N2 - Beta-ketoacyl-ACP utilizing enzymes in fatty acid, polyketide and acyl-homoserine lactone biosynthetic pathways are important targets for developing antimicrobial, anticancer and antiparasitic compounds. Published reports on successful isolation of beta-ketoacyl-ACPs in a laboratory remain scarce to date and thus most beta-ketoacyl-ACP utilizing enzymes are routinely characterized using small molecule substrates in lieu of the bonafide 3-oxoacyl-ACPs. We report the systematic investigation into the electronic, geometric and spatial aspects of beta-ketoacyl-chain recognition to develop 3-oxoacyl-ACP substrate mimics for two beta-ketoacyl-ACP utilizing quorum signal synthases.

AB - Beta-ketoacyl-ACP utilizing enzymes in fatty acid, polyketide and acyl-homoserine lactone biosynthetic pathways are important targets for developing antimicrobial, anticancer and antiparasitic compounds. Published reports on successful isolation of beta-ketoacyl-ACPs in a laboratory remain scarce to date and thus most beta-ketoacyl-ACP utilizing enzymes are routinely characterized using small molecule substrates in lieu of the bonafide 3-oxoacyl-ACPs. We report the systematic investigation into the electronic, geometric and spatial aspects of beta-ketoacyl-chain recognition to develop 3-oxoacyl-ACP substrate mimics for two beta-ketoacyl-ACP utilizing quorum signal synthases.

UR - https://scholarworks.boisestate.edu/chem_facpubs/124

UR - http://dx.doi.org/10.1039/c8cc04532a

U2 - 10.1039/c8cc04532a

DO - 10.1039/c8cc04532a

M3 - Article

C2 - 30027952

SN - 1359-7345

JO - Chemical Communications

JF - Chemical Communications

ER -

Insights into β-Ketoacyl-Chain Recognition for β-Ketoacyl-ACP Utilizing AHL Synthases

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