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The proteolytic specificity of the neutral zinc proteinase from Bacillus mesentericus strain 76 (MCP 76)/Bacillus subtilis was determined by using the alpha-chain of walrus hemoglobin as substrate. The resulting peptides were fractionated by gel filtration and than isolated by reversed-phase HPLC. The peptides were identified on the basis of their amino-acid compositions and aligned with the known sequence of the walrus alpha-chain. The proteolytic specificity of MCP 76, deduced from the experimental cleavage pattern is compared to that of thermolysin. The amino-acid residues in positions P1 and P'1 on both sides of the scissible bond are considered as most important for the cleavage. MCP 76 prefers leucine, valine, phenylalanine and threonine in position P'1 as well as lysine, threonine, leucine and alanine in position P1 and thus differs from thermolysin which shows no preference for threonine in P'1 and accepts numerous amino-acid residues of different type in P1.
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Stoeva et al. (1989) studied this question.
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