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. 1982 Aug;70(2):340–343. doi: 10.1104/pp.70.2.340

Studies on the Aminotransferases Participating in the Glycolate Metabolism of the Alga Mougeotia1

U Winkler 1, W Säftel 1, H Stabenau 1
PMCID: PMC1067145  PMID: 16662491

Abstract

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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