Substrate specificity of human pancreatic elastase 2
作者： Eric G. Del Mar , Corey Largman , James W. Brodrick , Maria Fassett , Michael C. Geokas
DOI: 10.1021/BI00544A011
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摘要: The substrate specificity of human pancreatic elastase 2 was investigated by using a series peptide p-nitroanilides. kinetic constants, kcat and Km, for the hydrolysis these peptides revealed that this serine protease preferentially hydrolyzes containing P1 amino acids which have medium to large hydrophobic side chains, except those are disubstituted on first carbon chain. Thus, appears be similar in bond recently described porcine [Gertler, A., Weiss, Y., & Burstein, Y. (1977) Biochemistry 16, 2709] but differs significantly from 1. best substrates were glutaryl-Ala-Ala-Pro-Leu-p nitroanilide succinyl-Ala-Ala-Pro-Met-p-nitroanilide. However, there little difference among with leucine, methionine, phenylalanine, tyrosine, norvaline, or norleucine position. Changes rate differing P5 residues indicate enzyme has an extended binding site interacts at least five substrates. overall catalytic efficiency is lower than 1 bovine chymotrypsin compounds studied.
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