Document Detail


Formation of a beta-aspartyl phosphate intermediate by the vanadate-sensitive ATPase of Streptococcus faecalis.
MedLine Citation:
PMID:  3155519     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The vanadate-sensitive membrane ATPase of Streptococcus faecalis forms, as part of the reaction cycle, an acylphosphate intermediate. The phosphorylated amino acid residue was identified by reducing the purified reconstituted phosphoenzyme with [3H]borohydride, followed by acid hydrolysis of the protein and quantitative amino acid analysis. Tritiated homoserine was found to be the resulting reaction product, generated through the reduction of a beta-aspartyl phosphate residue. The S. faecalis ATPase thus forms the same phosphorylated intermediate as a number of eukaryotic transport ATPases and appears to be related to these enzymes.
Authors:
P Fürst; M Solioz
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  260     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1985 Jan 
Date Detail:
Created Date:  1985-02-15     Completed Date:  1985-02-15     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  50-2     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / metabolism*
Amino Acids / analysis
Aspartic Acid / analogs & derivatives*,  analysis
Enterococcus faecalis / enzymology*
Phosphorylation
Vanadates
Vanadium / pharmacology*
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Vanadates; 22138-53-0/beta-aspartyl phosphate; 56-84-8/Aspartic Acid; 7440-62-2/Vanadium; EC 3.6.1.-/Adenosine Triphosphatases

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


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