Conformational Changes at the Active Site of Pantetheine Hydrolase During Denaturation by Guanidine Hydrochloride

被引：0
|
作者：
Giuseppina Pitari
Angelo A. D'Archivio
Luana Di Leandro
Giovanni Antonini
Alberto Panatta
Enzo Tettamanti
Silvestro Duprè
Francesco Malatesta
机构：
[1] University of L'Aquila,Dipartimento di Biologia di Base e Applicata
[2] University of L'Aquila,Dipartimento di Chimica Ingegneria Chimica e Materiali
[3] University of L'Aquila,Istituto Nazionale di Fisica della Materia (INFM), Dipartimento di Fisica
[4] University “La Sapienza” and Centro di Biologia Molecolare,Dipartimento di Scienze Biochimiche
[5] C.N.R.,undefined
来源：
Journal of Protein Chemistry | 1999年 / 18卷
关键词：
Pantetheine hydrolase; active site; ESR spectroscopy;
D O I：
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中图分类号：
学科分类号：
摘要：
Conformational changes at the active site of pantetheine hydrolase (EC3.5.1.-) during guanidine hydrochloride (GndHCl) denaturation were investigated by UV and circular dichroism spectroscopy and by electron spin resonance spectroscopy, following the spectral behaviour of the nitroxide radicals (N- (1- oxyl - 2,2,5,5, -tetramethyl-3-pyrrolidinyl) iodacetamide) covalently linked to the two active site cysteine residues. At low denaturant concentrations (0.2 M) no conformational changes may be observed, whereas the catalytic activity, is strongly affected. The results indicate that the active site of pantetheine hydrolase is labile and unfolds under conditions in which no global tertiary struscture modifications can be observed.
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页码：785 / 789
页数：4
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