Literature DB >> 7785086

Some evidence in favour of the partnership between rabbit muscle aldolase and glyceraldehyde 3-phosphate dehydrogenase in the consecutive reactions.

Y V Chumachenko1.   

Abstract

An additional indication in favour of interaction between sequential glycolytic enzymes is provided by the mutual enhancement of aldolase and glyceraldehyde 3-phosphate dehydrogenase activities. The efficiency of aldolase as the activator is progressively affected by the presence of its substrate, fructose-1,6-diphosphate, and its structural analogue, hexitol-1,6-diphosphate. Such interrelation of two sequential glycolytic enzymes can originate from their conformational interadjustment for the subsequent metabolic channeling between them.

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Year:  1994        PMID: 7785086

Source DB:  PubMed          Journal:  Ukr Biokhim Zh (1978)        ISSN: 0201-8470


  2 in total

Review 1.  Functional aspects of the X-ray structure of mitochondrial creatine kinase: a molecular physiology approach.

Authors:  U Schlattner; M Forstner; M Eder; O Stachowiak; K Fritz-Wolf; T Wallimann
Journal:  Mol Cell Biochem       Date:  1998-07       Impact factor: 3.396

2.  Substitutions at a rheostat position in human aldolase A cause a shift in the conformational population.

Authors:  Kathryn D Fenton; Kathleen M Meneely; Tiffany Wu; Tyler A Martin; Liskin Swint-Kruse; Aron W Fenton; Audrey L Lamb
Journal:  Protein Sci       Date:  2021-11-12       Impact factor: 6.725

  2 in total

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