"Protease I" of Escherichia coli functions as a thioesterase in vivo.
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.
Cho
H
H
Department of Microbiology, University of Illinois at Urbana-Champaign 61801.
Cronan
J E
JE
D010450:Endopeptidases / Q000235:genetics* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005798:Genes, Bacterial / Q000502:physiology*; D013869:Thiolester Hydrolases / Q000235:genetics* / Q000378:metabolism
D013869:Thiolester Hydrolases; D010450:Endopeptidases