ISSN:
1573-4943
Keywords:
Pantetheine hydrolase
;
active site
;
ESR spectroscopy
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1020685619173
Permalink