Document Detail

Complexes of muscle aldolase in equilibrium with fructose 1,6-bisphosphate.
MedLine Citation:
PMID:  4052378     Owner:  NLM     Status:  MEDLINE    
Minimum values for the content of covalent intermediates in the equilibria of muscle aldolase with its cleavable substrates have been determined by acid denaturation/precipitation. Ribulose 1,5-bisphosphate, a nonsubstrate that binds well to aldolase in the native state, does not form a covalent complex that is acid precipitable. The insoluble protein complexes with substrates fructose 1,6-bisphosphate and sedoheptulose 1,7-bisphosphate, representing approximately 50% and approximately 60% of total bound substrate, are much more stable in acid and alkali than that with substrate 5-deoxyfructose 1,6-bisphosphate, suggesting that they have the form of protein-bound N-glycosides. Whether such complexes exist on the enzyme in the native state in addition to being formed subsequent to denaturation is unresolved. Both the acid-precipitable and nonprecipitable forms of fructose 1,6-bisphosphate are converted to triose phosphate products at the same rate, providing no kinetic evidence for a pool that is not on the main reaction path. Total fructose 1,6-bisphosphate liganded to enzyme returns to the free solution about 9 times for each net cleavage reaction. It is still not clear whether this is limited by the cleavage step or by release of glyceraldehyde phosphate.
I A Rose; J V Warms
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  24     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1985 Jul 
Date Detail:
Created Date:  1985-12-05     Completed Date:  1985-12-05     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  3952-7     Citation Subset:  IM    
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MeSH Terms
Drug Stability
Fructose-Bisphosphate Aldolase / metabolism*
Fructosediphosphates / metabolism*
Glyceraldehyde 3-Phosphate / metabolism
Glycosides / analysis
Hexosediphosphates / metabolism*
Hydrogen-Ion Concentration
Muscles / enzymology*
Phosphorus Radioisotopes
Protein Binding
Protein Denaturation
Substrate Specificity
Grant Support
Reg. No./Substance:
0/Fructosediphosphates; 0/Glycosides; 0/Hexosediphosphates; 0/Phosphorus Radioisotopes; 142-10-9/Glyceraldehyde 3-Phosphate; 488-69-7/fructose-1,6-diphosphate; EC Aldolase

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

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