Document Detail


Determination of constants of substrate primary binding with baker's yeast transketolase by kinetic modelling.
MedLine Citation:
PMID:  9275280     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A kinetic model of bisubstrate reaction catalyzed by baker's yeast transketolase is proposed. The model considers individual stages of substrates reversible primary binding. The model corresponds to the observed kinetics of product accumulation within a wide range of initial substrate concentrations. Kinetic parameters for the best simulation of the experimental data are defined. The equilibrium constants of the primary binding of both the initial and produced ketose and also the initial aldose were unequivocally determined by varying the initial substrate concentrations. The dissociation constants of the primary enzyme-substrate complex for the initial ketose (xylulose 5-phosphate) and the reaction product (sedoheptulose 7-phosphate) were found to differ by more than by two orders of magnitude. The result is discussed in the context of the hypothesis of flip-flop functioning of the transketolase active sites.
Authors:
V A Selivanov; L E Meshalkina; M V Kovina; G A Kochetov
Publication Detail:
Type:  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 Apr 
Date Detail:
Created Date:  1997-09-29     Completed Date:  1997-09-29     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0376536     Medline TA:  Biochemistry (Mosc)     Country:  RUSSIA    
Other Details:
Languages:  eng     Pagination:  425-32     Citation Subset:  IM    
Affiliation:
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Russia.
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MeSH Terms
Descriptor/Qualifier:
Binding Sites
Computer Simulation
Kinetics
Models, Chemical
Pentosephosphates / metabolism
Protein Binding
Recombinant Proteins / metabolism
Saccharomyces cerevisiae / enzymology*
Sugar Phosphates / metabolism
Transketolase / chemistry,  genetics,  metabolism*
Chemical
Reg. No./Substance:
0/Pentosephosphates; 0/Recombinant Proteins; 0/Sugar Phosphates; 2646-35-7/sedoheptulose 7-phosphate; 60802-29-1/xylulose-5-phosphate; EC 2.2.1.1/Transketolase

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