Document Detail


On the domain construction of the multienzyme gramicidin S synthetase 2. Isolation of domains activating valine and leucine.
MedLine Citation:
PMID:  2190825     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The multienzyme gramicidin S synthetase 2, composed of one polypeptide chain, was treated with trypsin and chymotrypsin to give fragments retaining partial enzyme activities. Previously, a tryptic fragment of this multienzyme has been identified as a structural and functional domain. In this study two more fragments, activating Leu and Val, respectively, are shown to represent domains. Careful inspection of the data on limited proteolysis, from this study as well as from previous work, suggests that domains are not simply connected like pearls on a string, and a model for the structure of gramicidin S synthetase, with implications for other peptide synthetase multienzymes, is presented. It is suggested that gramicidin S synthetase 2 is constructed from core catalytic domains and intervening framework. Such an interpretation is in accordance with all published data on limited proteolysis of peptide synthetases, but needs an interplay with gene structural studies in order to be validated and refined.
Authors:
H J Skarpeid; T L Zimmer; H von Döhren
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  189     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1990 May 
Date Detail:
Created Date:  1990-07-13     Completed Date:  1990-07-13     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  517-22     Citation Subset:  IM    
Affiliation:
Biokjemisk Institutt, University of Oslo, Norway.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Isomerases / analysis*,  metabolism
Bacillus / enzymology
Binding Sites
Chromatography, Gel
Chromatography, Liquid / methods
Chymotrypsin
Electrophoresis, Polyacrylamide Gel
Leucine*
Multienzyme Complexes / analysis*,  metabolism
Peptide Fragments / analysis
Peptide Hydrolases
Peptide Synthases / analysis*,  metabolism
Trypsin
Valine*
Chemical
Reg. No./Substance:
0/Multienzyme Complexes; 0/Peptide Fragments; 61-90-5/Leucine; 7004-03-7/Valine; EC 3.4.-/Peptide Hydrolases; EC 3.4.21.1/Chymotrypsin; EC 3.4.21.4/Trypsin; EC 5.1.1.-/Amino Acid Isomerases; EC 6.3.2.-/Peptide Synthases; EC 6.3.2.-/gramicidin-S-synthetase 2

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


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