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PMID: 7029535 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Chemical synthesis of acyl thioesters of acyl carrier protein with native structure.

Cronan JE, Klages AL

Abstract

The acyl carrier protein (ACP) of Escherichia coli was converted to acyl-ACP by imidazole-catalyzed S-acylation with N-acylimidazole. The acylation was specific to the sulfhydryl group; no acylation of tyrosine or amino groups of the protein occurred. The acyl-ACP substrates synthesized had a native structure as determined by gel electrophoresis, hydrophobic chromatography, and enzymatic activity. N-Acylimidazoles are readily synthesized and permit preparation of those acyl-ACP substrates that cannot be produced enzymatically.

MeSH Terms
Acyl Carrier Protein/metabolism Escherichia coli/enzymology Esters/chemical synthesis Kinetics Structure-Activity Relationship Substrate Specificity Sulfhydryl Compounds
Chemicals
Acyl Carrier Protein Esters Sulfhydryl Compounds
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Cronan J E
Klages A L
References (22)
22 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1981-09-00
Pages
5440-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC348761
Subset
IM
Grants
NIAID NIH HHS · AI 15650 · United States
NIGMS NIH HHS · GM 25616 · United States
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