Document Detail


A study of tryptophan fluorescence quenching of bifunctional alginate lyase from a marine bacterium Pseudoalteromonas sp. strain No. 272 by acrylamide.
MedLine Citation:
PMID:  14519987     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A fluorescence quenching study of a sole tryptophan residue of a bifunctional alginate lyase from Pseudoalteromonas sp. strain No. 272 was done in the presence and absence of substrates, oligomeric guluronic and its C5 isomer mannuronic acid, by a Stern-Volmer plot with a quencher, acrylamide. N-Acetyltryptophanamide and reduced and carboxymethylated alginate lyase showed large quenching constants, on the other hand, the native enzyme had small constants regardless of the presence or absence of the substrates. The result suggests that the tryptophan residue is located in a buried region of the enzyme molecule, but is barely accessible to acrylamide, and that the residue is not masked by the substrates with various degrees of polymerization.
Authors:
Yoshiko Iwamoto; Hidetoshi Hidaka; Tatsuya Oda; Tsuyoshi Muramatsu
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Bioscience, biotechnology, and biochemistry     Volume:  67     ISSN:  0916-8451     ISO Abbreviation:  Biosci. Biotechnol. Biochem.     Publication Date:  2003 Sep 
Date Detail:
Created Date:  2003-10-01     Completed Date:  2004-06-14     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9205717     Medline TA:  Biosci Biotechnol Biochem     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  1990-2     Citation Subset:  IM    
Affiliation:
Division of Biochemistry, Faculty of Fisheries, Nagasaki University, Japan.
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MeSH Terms
Descriptor/Qualifier:
Acrylamide / chemistry*
Methylation
Oligosaccharides / chemistry,  metabolism
Polysaccharide-Lyases / chemistry*,  metabolism
Pseudoalteromonas / enzymology*,  genetics
Spectrometry, Fluorescence / methods
Substrate Specificity
Tryptophan / analogs & derivatives*,  chemistry*,  metabolism
Chemical
Reg. No./Substance:
0/Oligosaccharides; 2382-79-8/N-acetyltryptophanamide; 73-22-3/Tryptophan; 79-06-1/Acrylamide; EC 4.2.2.-/Polysaccharide-Lyases; EC 4.2.2.3/poly(beta-D-mannuronate) lyase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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