The specificity of glycine-N-acylase and acylglycine excretion in the organicacidaemias

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Abstract

The specificity of the enzyme glycine-N-acylase prepared from ox liver mitochondria for the coenzyme A derivatives of several organic acids has been investigated. The kinetic constants of this enzyme for the coenzyme A derivatives of these organic acids closely parallel the degree of glycine conjugation found in patients with the organicacidaemias.

References (21)

  • K. Tanaka et al.

    J. Biol. Chem.

    (1967)
  • D. Schachter et al.

    J. Biol. Chem.

    (1953)
  • S.L. Tishler et al.

    Biochem. Pharmacol.

    (1970)
  • D. Schachter et al.

    J. Biol. Chem.

    (1954)
  • F. Lipmann et al.

    J. Biol. Chem.

    (1945)
  • G.L. Ellman

    Arch. Biochem. Biophys.

    (1959)
  • E.R. Stadtman
  • D. Schachter et al.

    J. Biol. Chem.

    (1954)
  • G. Urata et al.

    J. Biol. Chem.

    (1963)
  • L. Eldjarn et al.

    Lancet

    (1970)
There are more references available in the full text version of this article.

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