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PMID: 6214787 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Protease La from Escherichia coli hydrolyzes ATP and proteins in a linked fashion.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 79 ·No. 16 ·1982-08-00 ·Pages 4883-7

Waxman L, Goldberg AL

Abstract

The energy requirement for protein breakdown in Escherichia coli results from an ATP requirement for the function of protease La, the product of the lon gene. This novel serine protease contains an ATPase activity that is essential for proteolysis. ATP and protein hydrolysis show the same Km for ATP (30-40 muM) and are affected similarly by various inhibitors, activators, and ATP analogs. Vanadate inhibited ATP cleavage and caused a proportionate reduction in casein hydrolysis, and inhibitors of serine proteases reduced ATP cleavage. Thus, ATP and protein hydrolysis appear to be linked stoichiometrically. Furthermore, ATP hydrolysis is stimulated two- to threefold by polypeptides that are substrates for the protease (casein, glucagon) but not by nonhydrolyzed polypeptides (insulin, RNase). Unlike hemoglobin or native albumin, globin and denatured albumin stimulated ATP hydrolysis and were substrates for proteolysis. It is suggested that the stimulation of ATP hydrolysis by potential substrates triggers activation of the proteolytic function.

MeSH Terms
ATP-Dependent Proteases Adenosine Triphosphatases/antagonists & inhibitors,metabolism Adenosine Triphosphate/metabolism Endopeptidases/metabolism Escherichia coli/enzymology Escherichia coli Proteins Heat-Shock Proteins Protease Inhibitors Protease La Serine Endopeptidases Substrate Specificity
Chemicals
Escherichia coli Proteins Heat-Shock Proteins Protease Inhibitors Adenosine Triphosphate Endopeptidases ATP-Dependent Proteases Serine Endopeptidases Lon protein, E coli Protease La Adenosine Triphosphatases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Waxman L
Goldberg A L
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37 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
DOI
10.1073/pnas.79.16.4883
Published
1982-08-00
Pages
4883-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC346789
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.79.16.4883 PMC Full Text View journal details
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