Literature DB >> 3569523

The kinetic effects of in vitro phosphorylation of rabbit muscle enolase by protein kinase C. A possible new kind of enzyme regulation.

F A Nettelblad, L Engström.   

Abstract

Rabbit muscle enolase was found to be phosphorylated in vitro by calcium-activated phospholipid-dependent protein kinase. The extent of incorporation (about 0.6 mol/mol subunit) and the apparent Km for the reaction (3.0 microM subunit) were determined. Kinetic studies on the unphosphorylated and phosphorylated enzymes displayed an unexpected effect of phosphorylation resulting in activation of the forward reaction and inhibition of the backward one.

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Year:  1987        PMID: 3569523     DOI: 10.1016/0014-5793(87)80064-9

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


  4 in total

1.  Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins.

Authors:  T Merkulova; M Lucas; C Jabet; N Lamandé; J D Rouzeau; F Gros; M Lazar; A Keller
Journal:  Biochem J       Date:  1997-05-01       Impact factor: 3.857

2.  Mutation of conserved active-site threonine residues in creatine kinase affects autophosphorylation and enzyme kinetics.

Authors:  Martin Stolz; Thorsten Hornemann; Uwe Schlattner; Theo Wallimann
Journal:  Biochem J       Date:  2002-05-01       Impact factor: 3.857

3.  Human TNF-α induces differential protein phosphorylation in Schistosoma mansoni adult male worms.

Authors:  Katia C Oliveira; Mariana L P Carvalho; José Matheus C Bonatto; Debora Schechtman; Sergio Verjovski-Almeida
Journal:  Parasitol Res       Date:  2015-11-07       Impact factor: 2.289

4.  Posttranscriptional and posttranslational control of enolase expression in the facultative Crassulacean acid metabolism plant Mesembryanthemum Crystallinum L.

Authors:  N R Forsthoefel; M A Cushman; J C Cushman
Journal:  Plant Physiol       Date:  1995-07       Impact factor: 8.340

  4 in total

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