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Microbiology 142 (1996), 1071-1076; DOI  10.1099/13500872-142-5-1071
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Asparagine degradation in Rhizobium etli

Alejandra Huerta-Zepeda1, Socorro Durán1, Gisela Du Pont1 and Jorge Calderón1,2

Departamento de Biotecnología, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, Mexico DF 04510

2Author for correspondence: Jorge Calderón. Tel: +52 6 22 38 80. Fax: +52 5 50 00 48.

ABSTRACT

The degradation of asparagine by Rhizobium etli involves asparaginase and aspartate ammonia-lyase (L-aspartase). The two enzymes were shown to be positively regulated by asparagine and negatively regulated by the carbon source. Asparaginase activity was not regulated by oxygen concentration or by nitrogen catabolite repression. Induction of both enzymes by asparagine enables R. etli to utilize asparagine as carbon source. Asparaginase may also be involved in maintaining the optimal balance between asparagine and aspartate. Aspartase was not involved in the utilization of aspartate or glutamate as carbon source. The presence of high levels of the two enzymes in R. etli bacteroids suggests that they may have a role in symbiosis between R. etli and Phaseolus vulgaris.

Keywords: Rhizobium etli, asparaginase, aspartase, catabolism, symbiosi




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