Document Detail


Adenosine-5'-tetraphosphate and guanosine-5'-tetraphosphate: new substrates of the cytosolic exopolyphosphatase of the yeast Saccharomyces cerevisiae.
MedLine Citation:
PMID:  9457767     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A cytosolic preparation of Saccharomyces cerevisiae is capable of hydrolyzing adenosine-5'-tetraphosphate and guanosine-5'-tetraphosphate with activities which are 1.5-2 times greater than that with polyP15. The apparent K(m) values for hydrolysis of adenosine-5'-tetraphosphate and guanosine-5'-tetraphosphate are 100 and 80 microM, respectively. A comparative study of inhibitors shows that these activities are inherent characteristics of these exopolyphosphatases.
Authors:
T V Kulakovskaya; N A Andreeva; I S Kulaev
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemistry. Biokhimii͡a     Volume:  62     ISSN:  0006-2979     ISO Abbreviation:  Biochemistry Mosc.     Publication Date:  1997 Sep 
Date Detail:
Created Date:  1998-04-01     Completed Date:  1998-04-01     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0376536     Medline TA:  Biochemistry (Mosc)     Country:  RUSSIA    
Other Details:
Languages:  eng     Pagination:  1051-2     Citation Subset:  IM    
Affiliation:
Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.
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MeSH Terms
Descriptor/Qualifier:
Acid Anhydride Hydrolases / metabolism*
Adenine Nucleotides / metabolism*
Cytosol / enzymology
Enzyme Inhibitors / metabolism
Guanosine Tetraphosphate / metabolism*
Heparin / metabolism
Hydrolysis
Kinetics
Saccharomyces cerevisiae / enzymology*
Sodium Fluoride / metabolism
Chemical
Reg. No./Substance:
0/Adenine Nucleotides; 0/Enzyme Inhibitors; 1062-98-2/adenosine 5'-tetraphosphate; 33503-72-9/Guanosine Tetraphosphate; 7681-49-4/Sodium Fluoride; 9005-49-6/Heparin; EC 3.6.-/Acid Anhydride Hydrolases; EC 3.6.1.11/exopolyphosphatase

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