Chemical nature of the inactivation of Bacillus cereus penicillinase by iodine

V. Csányi, Ilona Ferencz, I. Mile

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

The iodine inactivation reaction of Bacillus cereus 569/H penicillinase (penicillin amido-β-lactam hydrolase, EC 3.5.2.6) was studied. At pH 9 a 30-35% decrease in enzyme activity was observed. The reaction was found to be complex, its first step being a conformational change which brought the tyrosine and tryptophan side chains buried in native proteins to the surface of the molecule. This was followed by the oxidation of one tryptophan molecule and subsequent stabilization of the conformational change which occurred in the alkaline medium. Decrease of enzyme activity ensued when one molecule of tyrosine was substituted by iodine giving rise, in alkaline medium, to diiodotyrosine and, in acidic medium with the enzyme oxidized, to monoiodotyrosine.

Original languageEnglish
Pages (from-to)619-627
Number of pages9
JournalBBA - Protein Structure
Volume236
Issue number3
DOIs
Publication statusPublished - Jun 29 1971

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Bacillus cereus
Penicillinase
Iodine
Enzyme activity
Tryptophan
Molecules
Tyrosine
Enzymes
Diiodotyrosine
Monoiodotyrosine
Lactams
Hydrolases
Penicillins
Membrane Proteins
Stabilization
Oxidation
Proteins

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Chemical nature of the inactivation of Bacillus cereus penicillinase by iodine. / Csányi, V.; Ferencz, Ilona; Mile, I.

In: BBA - Protein Structure, Vol. 236, No. 3, 29.06.1971, p. 619-627.

Research output: Contribution to journalArticle

Csányi, V. ; Ferencz, Ilona ; Mile, I. / Chemical nature of the inactivation of Bacillus cereus penicillinase by iodine. In: BBA - Protein Structure. 1971 ; Vol. 236, No. 3. pp. 619-627.
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