RT Journal Article SR Electronic(1) A1 Huerta-Zepeda, Alejandra A1 Durán, Socorro A1 Du Pont, Gisela A1 Calderón, JorgeYR 1996 T1 Asparagine degradation in Rhizobium etli JF Microbiology, VO 142 IS 5 SP 1071 OP 1076 DO https://doi.org/10.1099/13500872-142-5-1071 PB Microbiology Society, SN 1465-2080, AB 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. , UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/13500872-142-5-1071