Open AccessThe cellular location of nitrilase and amidase enzymes of Brevibacterium R312
Author(s) -
Miller Jacqueline M.,
Knowles Christopher J.
Publication year - 1984
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1984.tb00201.x
Subject(s) - nitrilase , brevibacterium , amidase , enzyme , biochemistry , chemistry , microbiology and biotechnology , biology , bacteria , genetics , microorganism
Growth of Brevibacterium R312 on acetonitrile results in the appearance of acetate and ammonia in the medium, whereas incubation of harvested bacteria with acetonitrile results in appearance of acetamide, acetate and ammonia in the medium. Acetonitrilase and acetamidase activities were found to be located in the cytosolic fraction of the cell, suggesting that acetonitrile and acetamide readily enter and leave the bacterium. This was confirmed by the inability of these compounds to osmotically stabilise protoplasts, whereas acetate does so. The small size and neutral non‐ionic structure of acetonitrile and acetamide suggest they probably permeate by simple diffusion.