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. 1974 Jul;141(1):113–118. doi: 10.1042/bj1410113

Aminopeptidases of pea

T C Elleman 1
PMCID: PMC1168055  PMID: 4455194

Abstract

Studies of crude extracts of pea seeds (Pisum sativum, var. Green feast) revealed the presence of three enzymes that hydrolyse the amide bond of aminoacyl β-naphthylamides. They differ in their specificity towards the aminoacyl moiety; one is proline-specific, whereas the other two hydrolyse the β-naphthylamides of primary amino acids. Of the latter, one is highly specific for hydrophobic aminoacyl residues whereas the other has a broader, somewhat complementary specificity, showing preferential hydrolysis of non-hydrophobic aminoacyl residues. These latter two aminoacyl-β-naphthylamidases have been separated and partly characterized with regard to substrate specificity and antagonism by inhibitors. Both are true aminopeptidases, requiring the presence of a free amino group and hydrolysing the amide bonds of amino acid amides, dipeptides and oligopeptides consecutively from the N-terminal end.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. AMBLER R. P. THE AMINO ACID SEQUENCE OF PSEUDOMONAS CYTOCHROME C-551. Biochem J. 1963 Nov;89:349–378. doi: 10.1042/bj0890349. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Barrett A. J. A new assay for cathepsin B1 and other thiol proteinases. Anal Biochem. 1972 May;47(1):280–293. doi: 10.1016/0003-2697(72)90302-8. [DOI] [PubMed] [Google Scholar]
  3. Cameron E. C., Mazelis M. A Nonproteolytic "Trypsin-like" Enzyme: Purification and Properties of Arachain. Plant Physiol. 1971 Sep;48(3):278–281. doi: 10.1104/pp.48.3.278. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  5. Ihle J. N., Dure L. S., 3rd The developmental biochemistry of cottonseed embryogenesis and germination. II. Catalytic properties of the cotton carboxypeptidase. J Biol Chem. 1972 Aug 25;247(16):5041–5047. [PubMed] [Google Scholar]
  6. Kolehmainen L., Mikola J. Partial purification and enzymatic properties of an aminopeptidase from barley. Arch Biochem Biophys. 1971 Aug;145(2):633–642. doi: 10.1016/s0003-9861(71)80023-1. [DOI] [PubMed] [Google Scholar]
  7. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  8. Lee H. J., Wilson I. B. Enzymic parameters: measurement of V and Km. Biochim Biophys Acta. 1971 Sep 22;242(3):519–522. doi: 10.1016/0005-2744(71)90144-6. [DOI] [PubMed] [Google Scholar]
  9. Marks N., Datta R. K., Lajtha A. Partial resolution of brain arylamidases and aminopeptidases. J Biol Chem. 1968 Jun 10;243(11):2882–2889. [PubMed] [Google Scholar]
  10. ORNSTEIN L. DISC ELECTROPHORESIS. I. BACKGROUND AND THEORY. Ann N Y Acad Sci. 1964 Dec 28;121:321–349. doi: 10.1111/j.1749-6632.1964.tb14207.x. [DOI] [PubMed] [Google Scholar]
  11. Shaw D. C., Wells J. R. Radiochemical determination of a unique sequence around the reactive serine residue of a di-isopropyl phosphorofluoridate-sensitive plant carboxypeptidase and a yeast peptidase. Biochem J. 1972 Jun;128(2):229–235. doi: 10.1042/bj1280229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Visuri K., Mikola J., Enari T. M. Isolation and partial characterization of a carboxypeptidase from barley. Eur J Biochem. 1969 Jan;7(2):193–199. doi: 10.1111/j.1432-1033.1969.tb19591.x. [DOI] [PubMed] [Google Scholar]
  13. Zuber H. Reinigung und Eigenschaften der Carboxypeptidase aus Citrusfrüchten. Hoppe Seylers Z Physiol Chem. 1968 Oct;349(10):1337–1352. [PubMed] [Google Scholar]

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