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Studies on the Aminotransferases Participating in the Glycolate Metabolism of the Alga Mougeotia
Author(s) -
U. Winkler,
W. Säftel,
H. Stabenau
Publication year - 1982
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.70.2.340
Subject(s) - glyoxylate cycle , serine , glycine , glycine cleavage system , biochemistry , alanine , transferase , biology , chemistry , enzyme , amino acid
Microbodies from Mougeotia spec., Strain 168.80 contain aminotransferases for conversion of glyoxylate to glycine and serine to hydroxypyruvate. Formation of glycine is possible at highest rates with alanine and glutamate as amino donors, whereas for deamination of serine, pyruvate and glyoxylate are the most convenient substrates. A serine hydroxymethyl-transferase was found exclusively in the mitochondrial fraction. There are indications that this enzyme is bound to the mitochondrial membranes. The activities of all transferases are increased under culture conditions stimulating the synthesis of glycolate.

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