Studies on the aminotransferases participating in the glycolate metabolism of the alga mougeotia.
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.
Winkler
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Universität Oldenburg, Fachbereich Biologie, Postfach 2503, D-2900 Oldenburg, West Germany.
Säftel
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Stabenau
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