Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1. II. specificity and inhibition studies of Achromobacter protease I.
The unique specificity of Achromobacter protease I for lysine residue was investigated using synthetic and natural substrates, i.e., lysine derivatives, arginine derivatives, lysine vasopressin, substance P, ACTH and insulin. The enzyme cleaved only the -Lys-X- bonds in the above substrates. The binding affinity of alkylamines as determined by Ki was much stronger than that of the corresponding alkylguanidines.
D000324:Adrenocorticotropic Hormone / Q000378:metabolism; D000596:Amino Acids; D007700:Kinetics; D008236:Lypressin / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D011480:Protease Inhibitors; D013373:Substance P / Q000378:metabolism; D013379:Substrate Specificity; D014357:Trypsin / Q000378:metabolism
D000596:Amino Acids; D011480:Protease Inhibitors; D013373:Substance P; D008236:Lypressin; D000324:Adrenocorticotropic Hormone; D010447:Peptide Hydrolases; D014357:Trypsin