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J Bacteriol. 1994 March; 176(6): 1793-1795

research-article

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

H Cho and J E Cronan Jr

Department of Microbiology, University of Illinois at Urbana-Champaign 61801.

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.

J Bacteriol. 1994 March; 176(6): 1793-1795




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