Proofreading of noncognate Acyl adenylates by an acyl-coenzyme a ligase

Miglena Manandhar; John E. Cronan

doi:10.1016/j.chembiol.2013.10.010

Proofreading of noncognate Acyl adenylates by an acyl-coenzyme a ligase

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Abstract

Summary Aminoacyl-tRNA synthetases remove (proofread) incorrect substrates and thereby prevent errors in protein synthesis. We report enzyme-catalyzed pretransfer editing by pimeloyl-coenzyme A (CoA) ligase (BioW), a biotin synthetic enzyme that converts pimelate, a seven-carbon dicarboxylic acid, to its CoA ester. The noncognate BioW substrate glutaric acid results in hydrolysis of ATP to AMP with formation of only trace amounts of glutaryl-CoA, thereby mimicking pretransfer editing of incorrect aminoacyl-adenylates by aminoacyl-tRNA synthetases.

Original language	English (US)
Pages (from-to)	1441-1446
Number of pages	6
Journal	Chemistry and Biology
Volume	20
Issue number	12
DOIs	https://doi.org/10.1016/j.chembiol.2013.10.010
State	Published - Dec 19 2013

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Pharmacology
Drug Discovery
Clinical Biochemistry

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10.1016/j.chembiol.2013.10.010

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title = "Proofreading of noncognate Acyl adenylates by an acyl-coenzyme a ligase",

abstract = "Summary Aminoacyl-tRNA synthetases remove (proofread) incorrect substrates and thereby prevent errors in protein synthesis. We report enzyme-catalyzed pretransfer editing by pimeloyl-coenzyme A (CoA) ligase (BioW), a biotin synthetic enzyme that converts pimelate, a seven-carbon dicarboxylic acid, to its CoA ester. The noncognate BioW substrate glutaric acid results in hydrolysis of ATP to AMP with formation of only trace amounts of glutaryl-CoA, thereby mimicking pretransfer editing of incorrect aminoacyl-adenylates by aminoacyl-tRNA synthetases.",

author = "Miglena Manandhar and Cronan, \{John E.\}",

note = "This work was supported by National Institutes of Health grant AI15650 from the National Institute of Allergy and Infectious Diseases. We thank Dr. Steven Lin and Vandana Chakravartty for advice and support.",

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AU - Manandhar, Miglena

AU - Cronan, John E.

N1 - This work was supported by National Institutes of Health grant AI15650 from the National Institute of Allergy and Infectious Diseases. We thank Dr. Steven Lin and Vandana Chakravartty for advice and support.

PY - 2013/12/19

Y1 - 2013/12/19

N2 - Summary Aminoacyl-tRNA synthetases remove (proofread) incorrect substrates and thereby prevent errors in protein synthesis. We report enzyme-catalyzed pretransfer editing by pimeloyl-coenzyme A (CoA) ligase (BioW), a biotin synthetic enzyme that converts pimelate, a seven-carbon dicarboxylic acid, to its CoA ester. The noncognate BioW substrate glutaric acid results in hydrolysis of ATP to AMP with formation of only trace amounts of glutaryl-CoA, thereby mimicking pretransfer editing of incorrect aminoacyl-adenylates by aminoacyl-tRNA synthetases.

AB - Summary Aminoacyl-tRNA synthetases remove (proofread) incorrect substrates and thereby prevent errors in protein synthesis. We report enzyme-catalyzed pretransfer editing by pimeloyl-coenzyme A (CoA) ligase (BioW), a biotin synthetic enzyme that converts pimelate, a seven-carbon dicarboxylic acid, to its CoA ester. The noncognate BioW substrate glutaric acid results in hydrolysis of ATP to AMP with formation of only trace amounts of glutaryl-CoA, thereby mimicking pretransfer editing of incorrect aminoacyl-adenylates by aminoacyl-tRNA synthetases.

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Proofreading of noncognate Acyl adenylates by an acyl-coenzyme a ligase

Abstract

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