Document Detail

Chemical modification of lysine and arginine residues of bovine heart 2-oxoglutarate dehydrogenase: effect on the enzyme activity and regulation.
MedLine Citation:
PMID:  10397349     Owner:  NLM     Status:  MEDLINE    
Chemical modification of arginine and lysine residues of bovine heart 2-oxoglutarate dehydrogenase with phenylglyoxal and pyridoxal 5'-phosphate inactivated the enzyme, indicating the importance of these residues for the catalysis. Inactivation caused by pyridoxal 5'-phosphate was prevented in the presence of thiamine pyrophosphate and Mg2+ allowing the assumption that lysine residues participate in binding of the cofactor.
S A Ostrovtsova
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Acta biochimica Polonica     Volume:  45     ISSN:  0001-527X     ISO Abbreviation:  Acta Biochim. Pol.     Publication Date:  1998  
Date Detail:
Created Date:  1999-09-30     Completed Date:  1999-09-30     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  14520300R     Medline TA:  Acta Biochim Pol     Country:  POLAND    
Other Details:
Languages:  eng     Pagination:  1031-6     Citation Subset:  IM    
Institute of Biochemistry, National Academy of Sciences of Belarus, Grodno.
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MeSH Terms
Adenosine Diphosphate / pharmacology
Arginine / chemistry*,  physiology
Dose-Response Relationship, Drug
Enzyme Inhibitors / pharmacology
Ketoglutarate Dehydrogenase Complex / metabolism*,  physiology
Lysine / chemistry*,  physiology
Myocardium / enzymology*
Phenylglyoxal / pharmacology
Pyridoxal Phosphate / pharmacology
Thiamine Pyrophosphate / metabolism
Time Factors
Reg. No./Substance:
0/Enzyme Inhibitors; 1074-12-0/Phenylglyoxal; 154-87-0/Thiamine Pyrophosphate; 54-47-7/Pyridoxal Phosphate; 56-87-1/Lysine; 58-64-0/Adenosine Diphosphate; 74-79-3/Arginine; EC Dehydrogenase Complex

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

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