Chemical mechanism of malic enzyme as determined by isotope effects and alternate substrates

W. W.      Cleland

doi:10.2174/092986650705221207142855

Abstract

Isotope effect studies have shown that malic enzyme from avian liver or Ascaris suum has a stepwise mechanism with NAD(P) as substrate, but a concerted one with nucleotide substrates with higher redox potentials. It has been possible to calculate intrinsic deuterium and 13C isotope effects and commitments. The enzyme is very specific, with only erythro-fluoromalate, D- and mesotartrate and L-aspartate with an unprotonated amino group as slow alternate substrates.

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Protein & Peptide Letters

Title:Chemical mechanism of malic enzyme as determined by isotope effects and alternate substrates

Volume: 7 Issue: 5

Author(s): W. W. Cleland

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Abstract: Isotope effect studies have shown that malic enzyme from avian liver or Ascaris suum has a stepwise mechanism with NAD(P) as substrate, but a concerted one with nucleotide substrates with higher redox potentials. It has been possible to calculate intrinsic deuterium and 13C isotope effects and commitments. The enzyme is very specific, with only erythro-fluoromalate, D- and mesotartrate and L-aspartate with an unprotonated amino group as slow alternate substrates.

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Cleland W. W., Chemical mechanism of malic enzyme as determined by isotope effects and alternate substrates, Protein & Peptide Letters 2000; 7 (5) . https://dx.doi.org/10.2174/092986650705221207142855

DOI https://dx.doi.org/10.2174/092986650705221207142855	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305