Literature DB >> 2666165

Remarks on the supramolecular organization of the glycolytic system in vivo.

J Batke1.   

Abstract

The great latent catalytic capacity, manifested at the extremely high intracellular concentrations and in large apparent kcat/Km values, of the glycolytic enzymes on the one hand and their tendency in experiments in vitro to form functionally-specific flux-enhancing (channeling) complexes on the other, is considered and discussed as an apparent discrepancy. A random association of glycolytic enzymes in vivo is probable.

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Year:  1989        PMID: 2666165     DOI: 10.1016/0014-5793(89)81419-x

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Metabolite channeling versus free diffusion: reinterpretation of aldolase-catalysed inactivation of glyceraldehyde-3-phosphate dehydrogenase.

Authors:  B G Vértessy; M Vas
Journal:  Biochem J       Date:  1992-09-15       Impact factor: 3.857

2.  Flight muscle function in Drosophila requires colocalization of glycolytic enzymes.

Authors:  K Wojtas; N Slepecky; L von Kalm; D Sullivan
Journal:  Mol Biol Cell       Date:  1997-09       Impact factor: 4.138

3.  19F NMR measurements of the rotational mobility of proteins in vivo.

Authors:  S P Williams; P M Haggie; K M Brindle
Journal:  Biophys J       Date:  1997-01       Impact factor: 4.033

  3 in total

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