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Toward the smallest active subdomain of a TIM-barrel fold: Insights from a truncated α-amylase.
MedLine Citation:
PMID:  21741359     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
AmyTM is a truncated mutant of the α-amylase of Bacillus stearothermophilus US100. It has been derived from the wild type amylase gene via a reading frame shift, following a tandem duplication of the mutant primer, associated to an Adenine base deletion. AmyTM was composed of 720 nucleotides encoding 240 amino acid residues out of 549 of the wild type. The AmyTM protein was devoided of the three catalytic residues but still retains catalytic activity. It is Ca-independent maltotetraose producing amylase, optimally active at pH 6 and 60°C, under monomeric or multimeric forms. AmyTM is the smallest functional truncated TIM barrel. It contains the βαβα unit as the minimal subdomain associated to an enzymatic function. The enzymatic activity can, until now, be attributed to the presence of the whole domain B, in the structure of AmyTM. This mutant revealed, for the first time, the regeneration of a catalytic site after its abolition. This fact may be considered as the restoration of a primitive active site, which was lost in the course of evolution toward more stable domains.
Authors:
Mamdouh Ben Ali; Mehdi Ghram; Houda Hmani; Bassem Khemakhem; Richard Haser; Samir Bejar
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-6-29
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  -     ISSN:  1090-2104     ISO Abbreviation:  -     Publication Date:  2011 Jun 
Date Detail:
Created Date:  2011-7-11     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2011 Elsevier Inc. All rights reserved.
Affiliation:
Laboratoire de Métabolites et de Biomolécules, Centre de Biotechnologie de Sfax, Université de Sfax, B.P. 1177, 3018 Sfax, Tunisia.
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