This paper reports the complete amino acid sequence of a novel subtilisin: alkaline mesentericopeptidase. The protein contains 275 amino acid residues in a single polypeptide chain. The sequence data presented allow the linear arrangement of the whole molecule. Comparison with the subtilisins amylosacchariticus, novo, carlsberg, DY, and a subtilisin isolated from B. subtilis strain I 168, respectively classifies the enzyme as a serine protease of the subtilisin novo type closely related to subtilisin amylosacchariticus. Special features of mensentericopeptidase with respect to enzymatic and physico-chemical properties are discussed.
