CLONING AND EXPRESSION IN ESCHERICHIA-COLI OF THE GENE ENCODING A NOVEL L-2,4-DIAMINOBUTYRATE DECARBOXYLASE OF ACINETOBACTER-BAUMANNII

The gene encoding L-2,4-diaminobutyrate decarboxylase (DABA DC) was cl oned from Acinetobacter baumannii ATCC 19606. The gene was evidently u nder the control of its own promoter. Interestingly, the host carrying this clone also produced an appreciable amount of 1,3-diaminopropane. Restriction mapping and subsequent subcloning of the cloned insert lo calized the DABA DC gene within a 2.45-kb SphI/EcoRI fragment. For end ogenous production of DAP, a 1.75-kb EcoRI/PstI region downstream from the DABA DC gene was further required. Southern blot hybridization re vealed some heterogeneity in the DABA DC genes among other Acinetobact er species.