title: Isolation of acetyl esterase mutants of Bacillus subtilis 168.
abstract: Five mutants of Bacillus subtilis 168 defective in an intracellular esterase activity were identified. By polyacrylamide gel electrophoresis, four of the mutants were shown to lack esterase B activity, and the fifth lacked esterase A activity. All of the back-crossed esterase mutants were able to sporulate at wild-type frequency and produce exoprotease(s) and antibiotic(s). No difference in motility could be attributed to the esterase mutation. PBS1 transduction analysis showed all the esterase B mutations to be linked to the hisA marker.
mesh_terms: D000115:Acetylesterase / Q000096:biosynthesis*; D000900:Anti-Bacterial Agents / Q000096:biosynthesis; D001412:Bacillus subtilis / Q000201:enzymology* / Q000254:growth & development / Q000378:metabolism; D009154:Mutation; D010447:Peptide Hydrolases / Q000096:biosynthesis; D013171:Spores, Bacterial / Q000254:growth & development
chemical_list: D000900:Anti-Bacterial Agents; D000115:Acetylesterase; D010447:Peptide Hydrolases