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PMID: 8132479 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

"Protease I" of Escherichia coli functions as a thioesterase in vivo.

Journal of bacteriology ·Vol. 176 ·No. 6 ·1994-03-00 ·Pages 1793-5

Cho H, Cronan JE

Abstract

Escherichia coli protease I is assayed as an esterase active with certain synthetic model chymotrypsin substrates. However, the gene encoding protease I has the same DNA sequence and genomic location as tesA, a gene that encodes E. coli thioesterase I. We report that both hydrolase activities utilize the same active site and demonstrate that the protein functions as a thioesterase in vivo.

Related Genes
MeSH Terms
Endopeptidases/genetics,metabolism Escherichia coli/enzymology,genetics Genes, Bacterial/physiology Thiolester Hydrolases/genetics,metabolism
Chemicals
Thiolester Hydrolases Endopeptidases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Cho H
Department of Microbiology, University of Illinois at Urbana-Champaign 61801.
Cronan J E
References (15)
15 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1994-03-00
Pages
1793-5
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC205273
Subset
IM
Grants
NIAID NIH HHS · AI15650 · United States
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