Comparative Studies on Extracellular Penicillinases of the Same Structural Gene, penP, Expressed in Bacillus licheniformis and Bacillus subtilis

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Abstract
Extracellular penicillinases produced by B. licheniformis ATCC 9945A and B. subtilis from the same structural gene, penP, were compared. The 2 strains secreted the same large exopenicillinase (MW, 30,500; isoelectric point, pI = 5.00-5.04; NH2-terminal amino acid, Ser). The small exoenzyme from B. subtilis (MW, 29,500; pI = 5.00-5.04; NH2-terminal amino acid, Glu or Asn) was slightly different from that of B. licheniformis (MW, 29,500; pI = 5.13; NH2-terminal amino acid, Lys). The difference in the NH2-terminal residue is most probably due to differences in degradation by host-specific proteolytic enzymes.