The gene encoding alternansucrase (ASR) from Leuconostoc mesenteroides NRRL B-1355, an original sucrose glucosyltransferase (GTF) specific to alternating α-1, 3 and α-1, 6 glucosidic bond synthesis, was cloned, sequenced and expressed into Escherichia coli. Recombinant enzyme catalyzed oligoalternan synthesis from sucrose and maltose acceptor. From sequence comparison, it appears that ASR possesses the same domains as those described for GTFs specific to either contiguous α-1, 3 osidic bond or contiguous α-1, 6 osidic bond synthesis. However, the variable region and the glucan binding domain are longer than in other GTFs (by 100 and 200 amino acids respectively). The N-catalytic domain which presents 49% identity with the other GTFs from L. mesenteroides possesses the three determinants potentially involved in the glucosyl enzyme formation. © 2000 Federation of European Microbiological Societies.
Argüello-Morales, M. A., Remaud-Simeon, M., Pizzut, S., Sarçabal, P., Willemot, R. M., & Monsan, P. (2000). Sequence analysis of the gene encoding alternansucrase, a sucrose glucosyltransferase from Leuconostoc mesenteroides NRRL B-1355. FEMS Microbiology Letters, 182(1), 81–85. https://doi.org/10.1016/S0378-1097(99)00572-8