Literature DB >> 16667257

A squared michaelis-menten function of substrate concentration for plant mitochondrial respiration.

A T James1, J T Wiskich, I B Dry.   

Abstract

Dry and Wiskich ([1987] Arch Biochem Biophys 257: 92-99) have published data showing the response of plant mitochondrial respiration to increasing additions of oxaloacetate or malate when these substrates have been depleted by inhibition of succinate dehydrogenase by malonate, and coenzyme A (CoA) has been sequestered as acetyl-CoA by pyruvate dehydrogenase. In the presence of 2-oxoglutarate, it is shown that the response is given by a Michaelis-Menten curve, but in its absence, when malate has to supply substrate for dehydrogenation as well as to liberate CoA via malate dehydrogenase and citrate synthase, the response is presumably the product of two Michaelis-Menten functions, which can be approximated by the square of a single function.

Entities:  

Year:  1990        PMID: 16667257      PMCID: PMC1062280          DOI: 10.1104/pp.92.1.265

Source DB:  PubMed          Journal:  Plant Physiol        ISSN: 0032-0889            Impact factor:   8.340


  3 in total

1.  Regulation of the 2-oxoglutarate dehydrogenase lipoate succinyltransferase complex from cauliflower by nucleotide. Steady state kinetic studies.

Authors:  D W Craig; R T Wedding
Journal:  J Biol Chem       Date:  1980-06-25       Impact factor: 5.157

2.  Role of the external adenosine triphosphate/adenosine diphosphate ratio in the control of plant mitochondrial respiration.

Authors:  I B Dry; J T Wiskich
Journal:  Arch Biochem Biophys       Date:  1982-08       Impact factor: 4.013

3.  2-Oxoglutarate dehydrogenase and pyruvate dehydrogenase activities in plant mitochondria: interaction via a common coenzyme a pool.

Authors:  I B Dry; J T Wiskich
Journal:  Arch Biochem Biophys       Date:  1987-08-15       Impact factor: 4.013

  3 in total

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