Document Detail

Oxidation of a methionine residue in subtilisin-type proteinases by the hydrogen peroxide/borate system--an active site-directed reaction.
MedLine Citation:
PMID:  3275467     Owner:  NLM     Status:  MEDLINE    
Subtilisin-type proteinases (thermitase, subtilisin Carlsberg, alkaline proteinase ZIMET 10911, proteinase K) are partially inactivated by hydrogen peroxide in the alkaline pH range only in the presence of boric acid or phenylboronic acid. A model is presented to describe the inactivation mechanism. Both boric acid and perboric acid existing in equilibrium in the presence of hydrogen peroxide bind competitively at the active site of the enzyme. The inactivation, which is known to be caused by sulfoxide formation from the methionine residue in the active site (Stauffer, C.E. and Etson, D. (1969) J. Biol. Chem. 244, 5333-5338), is due to the enzyme-bound perboric acid species. The dissociation constants for the boric acid-thermitase and perboric acid-thermitase complexes are 36 +/- 7 and 4 +/- 1 mM, respectively. The first-order rate constant of inactivation is k = 0.63 +/- 0.14 min-1. The same mechanism of inactivation holds true for phenylboronic acid in alkaline hydrogen peroxide solutions.
G Hausdorf; K Krüger; G Küttner; H G Holzhütter; C Frömmel; W E Höhne
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  952     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1988 Jan 
Date Detail:
Created Date:  1988-02-16     Completed Date:  1988-02-16     Revised Date:  2004-11-17    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  20-6     Citation Subset:  IM    
Institute of Biochemistry, Humboldt University of Berlin, G.D.R.
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MeSH Terms
Bacillus / enzymology
Binding Sites
Hydrogen Peroxide
Peptide Hydrolases / metabolism*
Subtilisins / metabolism*
Thermus / enzymology
Reg. No./Substance:
0/Borates; 63-68-3/Methionine; 7722-84-1/Hydrogen Peroxide; EC 3.4.-/Peptide Hydrolases; EC 3.4.21.-/Subtilisins

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