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. 1983 Apr;71(4):874–878. doi: 10.1104/pp.71.4.874

Evidence for the Presence in Tobacco Leaves of Multiple Enzymes for the Oxidation of Glycolate and Glyoxylate

Evelyn A Havir 1
PMCID: PMC1066137  PMID: 16662922

Abstract

The enzymic oxidation of glycolate to glyoxylate and glyoxylate to oxalate by preparations purified from tobacco (Nicotiana tabacum var Havana Seed) leaves was studied. The Km values for glycolate and glyoxylate were 0.26 and 1.0 millimolar, respectively. The ratio of glycolate to glyoxylate oxidation was 3 to 4 in crude extracts but decreased to 1.2 to 1.5 on purification by (NH4)2SO4 fractionation and chromatography on agarose A-15 and hydroxylapatite. This level of glyoxylate oxidation activity was higher than that previously found for glycolate oxidase (EC 1.1.3.1). The ratio of the two activities was changed by reaction with the substrate analog 2-hydroxy-3-butynoate (HBA) which at all concentrations inhibited glyoxylate oxidation to a greater extent than glycolate oxidation. The ratio of the two activities could also be altered by changing the O2 concentration. Glycolate oxidation increased 3.6-fold when the O2 atmosphere was increased from 21 to 100%, whereas glyoxylate oxidation increased only 1.6-fold under the same conditions. These changes in ratio during purification, on inhibition by HBA, and under varying O2 concentrations imply that tobacco leaves contain at least two enzymes capable of oxidizing glycolate and glyoxylate.

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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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