| Literature DB >> 1271 |
C Lazdunski, J Busuttil, A Lazdunski.
Abstract
A periplasmic aminoendopeptidase from Escherichia coli has been purified to hemogeneity. It is a monomer of molecular weight 45000 and containing one -- SH group that is necessary for catalytic activity. The study of its substrate specificity indicated that the enzyme has both aminopeptidase and endopeptidase activity. The pH optimum for L-alanine p-nitroanilide hydrolysis is between 7 and 7.5 and that for 125I-labeled casein proteolysis between 7.3 and 7.6. The activation energy for the hydrolysis of L-anine p-nitroanilide was calculated to be 5.3 kcal X mol-1 (22.2 kJ X mol-1).Entities:
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Year: 1975 PMID： 1271 DOI： 10.1111/j.1432-1033.1975.tb21011.x
Source DB: PubMed Journal: Eur J Biochem ISSN： 0014-2956