Document Detail


The reaction of pyruvate with saccharopine dehydrogenase.
MedLine Citation:
PMID:  213275     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The preceding paper in this journal has reported that pyruvate could be substituted for 2-oxo-glutarate as a substrate of saccharopine dehydrogenase [epsilon-N-(L-glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine-forming) in the direction of reductive condensation. In the present communication, the kinetic mechanism of saccharopine dehydrogenase reaction with NADH, L-lysine and pyruvate as reactants is reported. The results of initial velocity study, inhibition studies with lysine analogs and a reaction product, NAD+, are consistent with an ordered mechanism with the coenzyme binding first and pyruvate last. The reaction mechanism is at variance with that of the normal reaction in which 2-oxoglutarate is the substrate, in that the order of addition of the amino and oxo acid substrates is reversed. This fact suggests that there exists a small degree of randomness in the binding of amino and oxo acid substrates. From a product inhibition study, NAD+ was shown to be the last reactant released. Saccharopine [epsilon-N-(L-glutaryl-2)-L-lysine] was found to act as a potent dead-end inhibitor of the condensation reactions (of lysine and 2-oxoglutarate, and of lysine and pyruvate) by forming an abortive E. NADH. saccharopine complex.
Authors:
K Sugimoto; M Fujioka
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  90     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1978 Oct 
Date Detail:
Created Date:  1979-01-15     Completed Date:  1979-01-15     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:  301-7     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Kinetics
Lysine
Mathematics
NAD
Oxidoreductases Acting on CH-NH Group Donors / metabolism*
Pyruvates*
Saccharomyces cerevisiae / enzymology
Saccharopine Dehydrogenases / metabolism*
Chemical
Reg. No./Substance:
0/Pyruvates; 53-84-9/NAD; 56-87-1/Lysine; EC 1.5.-/Oxidoreductases Acting on CH-NH Group Donors; EC 1.5.1.-/Saccharopine Dehydrogenases

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


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