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. 1981 Jan;145(1):452–458. doi: 10.1128/jb.145.1.452-458.1981

Glyoxylate bypass enzymes in Yersinia species and multiple forms of isocitrate lyase in Yersinia pestis.

S Hillier, W T Charnetzky
PMCID: PMC217293  PMID: 7462147

Abstract

Isocitrate lyase and malate synthase, the two unique enzymes of the glyoxylate cycle, were detected in crude extracts of Yersinia pestis, Y. pseudotuberculosis, and Y. enterocolitica. Y. pestis, unlike Escherichia coli and the other yersiniae tested, yielded two forms of isocitrate lyase during growth on acetate. These forms differed in electrophoretic mobility and temperature optima. One form (A) was present during growth on acetate, but was absent during growth on alternate carbon sources such as glucose. The second form (B) was not constitutive, but was found during growth on acetate, glucose, xylose, or other complex carbon sources. Itaconate, a succinate analog which inhibited both forms of isocitrate lyase in crude extracts, did not affect the growth of Y. pestis under conditions where little isocitrate lyase activity was detected. This inhibitor, however, retarded the growth of Y. pestis under conditions where acetate was provided as the primary carbon and energy source as well as under all conditions in which either form of isocitrate lyase was evident. This suggests that the B form may play an important role in the growth of this bacterium under conditions where a requirement for the classical anaplerotic sequence involving this enzyme is not apparent.

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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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