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[Some arylamidases from vetch seeds].
Biokhimiia (Moscow, Russia)
|May 1, 1975
Summary
Researchers purified a vetch seed enzyme, PPAase, that hydrolyzes specific amino acid amides. This arylamidase plays a role in seed biochemistry and has potential applications in peptide research.
Area of Science:
- Biochemistry
- Enzymology
Context:
- Vetch seeds contain enzymes that hydrolyze peptide bonds.
- Two distinct arylamidases were identified in resting vetch seed extracts.
Purpose:
- To isolate and characterize an arylamidase responsible for hydrolyzing L-phenylalanyl-p-nitroanilide (PPA).
- To investigate the biochemical properties and substrate specificity of the purified enzyme.
Summary:
- A specific enzyme, PPAase, was purified 2000-fold from vetch seeds using hydroxylapatite, DEAE-cellulose, and Sephadex G-100 chromatography.
- The purified PPAase exhibited a molecular weight of 66,000 Da and a K(m) of 1.64 x 10^-4 M.
- PPAase is inhibited by SH-reagents and o-oxyquinoline, with activity enhanced by low concentrations of Ca2+, Mg2+, and Mn2+.
- The enzyme preferentially hydrolyzes amino acid arylamides with hydrophobic side groups and specific dipeptides.
Impact:
- Elucidates the enzymatic machinery present in plant seeds.
- Provides insights into enzyme kinetics and substrate specificity for arylamidases.
- Characterizes a novel enzyme with potential applications in biotechnology and biochemical research.