PMID: 1271Dec 15, 1975

Purification and properties of a periplasmic aminoendopeptidase from Escherichia coli

European Journal of Biochemistry
C LazdunskiA 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).

References

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Citations

Jan 1, 1982·Molecular & General Genetics : MGG·C G MillerR Schultz
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Aug 1, 2020·International Journal of Molecular Sciences·Patrick SchallBernhard Grimm

Related Concepts

Aminopeptidase
Calorimetry
Enzyme Activation
Alkalescens-Dispar Group
Hydrogen-Ion Concentration
Plasma Protein Binding Capacity
Protein Conformation
Structure-Activity Relationship
Sulfhydryl Compounds
Thermodynamics

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