Altered Enolase in Aged Turbatrix aceti Results from Conformational Changes in the Enzyme

Young- and old-type enolases (2-phospho-D-glycerate hydrolyase, EC 4.2.1.11) from the free-living nematode Turbatrix aceti can be unfolded in 1.25 M guanidine hydrochloride and subsequently refolded with essentially a quantitative recovery. After refolding, both enolases form an identical or near-id...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1980-10, Vol.77 (10), p.5865-5868
Main Authors: Sharma, H. K., Rothstein, Morton
Format: Article
Language:English
Subjects:
Aging
Antiserum
Biochemistry
Circular Dichroism
Dichroism
Enzymes
Epitopes
Heat inactivation
Hydrochlorides
Liver
Molecules
Nematoda - enzymology
Phosphopyruvate Hydratase - immunology
Phosphopyruvate Hydratase - metabolism
Protein Conformation
Protein refolding
Room temperature
Spectrum Analysis
Structure-Activity Relationship
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Summary:Young- and old-type enolases (2-phospho-D-glycerate hydrolyase, EC 4.2.1.11) from the free-living nematode Turbatrix aceti can be unfolded in 1.25 M guanidine hydrochloride and subsequently refolded with essentially a quantitative recovery. After refolding, both enolases form an identical or near-identical third type of the enzyme as determined by spectral criteria, sensitivity to heat, immunotitration, and rate of inactivation by bacterial protease. By the same criteria, the refolded enolase is closer in conformation to the native old from of the enzyme than to the young form. The results prove that young and old enolases are conformational isomers and that an in vivo transformation from young to old enzyme takes place by conformational changes without covalent modification. The process may be related to the previously demonstrated slowing of enolase turnover in T. aceti. Errors in sequence cannot be involved in the age-related alteration of the enzyme.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.77.10.5865