Open AccessAminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A 4 hydrolase
Author(s) -
Sandrine Cadel,
Thierry Foulon,
A. Viron,
Ágnes Balogh,
Stéphanie Midol-Monnet,
Nadine Noël,
Paul A. Cohen
Publication year - 1997
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.94.7.2963
Subject(s) - biology , aminopeptidase , hydrolase , biochemistry , enzyme , peptide sequence , complementary dna , microbiology and biotechnology , phosphofructokinase 2 , amino acid , epoxide hydrolase 2 , nucleic acid sequence , leucine , gene
An aminopeptidase B (Ap-B) was previously purified to homogeneity from rat testis extracts and characterized. In the present work, by using oligonucleotides selected on the basis of partial amino acid microsequences of pure Ap-B and PCR techniques, the nucleotide sequence of a 2.2-kb cDNA was obtained. The deduced amino acid sequence corresponds to a 648-residue protein (72.3 kDa) containing the canonical “HEXXHX18 E” signature, which allowed its classification as a member of the M1 family of metallopeptidases. It exhibits 33% identity and 48% similarity with leukotriene-A4 hydrolase, a relation further supported by the capacity of Ap-B to hydrolyze leukotriene A4 . Both enzymes also were closely related to a partially sequenced protein fromDictyostelium discoideum , which might constitute the putative common ancestor of either aminopeptidase or epoxide hydrolase, or both. Ap-B and its mRNA were detected in the germ line and in the Sertoli and peritubular cells of the seminiferous tubules. Because the enzyme was found in the medium conditioned by spermatocytes and spermatids and in the acrosome during spermatozoa formation, together these observations suggested an involvement of this exometallopeptidase in the secretory pathway. It is concluded that this ubiquitous enzyme may be involved in multiple processing mechanisms.