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PMID: 6343835 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

Kinetics of subtilisin and thiolsubtilisin.

Molecular and cellular biochemistry ·Vol. 51 ·No. 1 ·1983-00-00 ·Pages 5-32

Philipp M, Bender ML

Abstract

Subtilisin is a bacterial serine protease with a broad specificity in the S1 subsite. It has been very extensively studied using a variety of kinetic and physical techniques. A chemical derivative, thiolsubtilisin, has been subjected to similar studies in order to analyze the effects of the OH to SH conversion on enzyme activity. The native structure of thiolsubtilisin is indicated by a variety of physical techniques. Oligopeptides bind nearly equally well to both enzymes, and a peptide chloromethylketone is much more reactive to thiolsubtilisin than to subtilisin. Both enzymes have a similar level of activity towards activated nonspecific amides and esters. However, thiolsubtilisin is inactive towards highly specific peptide amides and esters. Thiolsubtilisin also does not show good binding to boronic and arsonic acids. The observation that these transition state analog inhibitors bind poorly to thiolsubtilisin while other compounds bind nearly equally well to both enzymes suggests that thiolsubtilisin may not be able to stabilize the transition state during acylation by specific substrates.

MeSH Terms
Acylation Amides/metabolism Animals Imidazoles/metabolism Kinetics Substrate Specificity Subtilisins/antagonists & inhibitors,isolation & purification,metabolism
Chemicals
Amides Imidazoles Subtilisins thiolsubtilisins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Philipp M
Bender M L
References (131)
131 references, click to expand
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Article Info
Journal
Molecular and cellular biochemistry
Abbr.
Mol Cell Biochem
ISSN
0300-8177
DOI
10.1007/BF00215583
Published
1983-00-00
Pages
5-32
Language
English
Region
Netherlands
NLM ID
0364456
Subset
IM
Grants
NIGMS NIH HHS · GM 20853 · United States
External Links
PubMed source DOI: 10.1007/BF00215583 View journal details
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