Aminopeptidase B from the Rat Testis is a Bifunctional Enzyme Structurally Related to leukotriene-A4Hydrolase

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 obtain...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 94; no. 7; pp. 2963 - 2968
Main Authors Cadel, Sandrine, Foulon, Thierry, Viron, Annie, Balogh, Agnes, Midol-Monnet, Stephanie, Noel, Nadine, Cohen, Paul
Format Journal Article
LanguageEnglish
Published National Academy of Sciences of the United States of America 01.04.1997
Subjects
Amino acids
Biochemistry
Complementary DNA
Enzymes
Messenger RNA
Sertoli cells
Somatic cells
Spermatids
Spermatocytes
Testes
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Summary: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 ``HEXXHX18E'' signature, which allowed its classification as a member of the M1 family of metallopeptidases. It exhibits 33% identity and 48% similarity with leukotriene-A4hydrolase, 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 from Dictyostelium 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.
ISSN:0027-8424
1091-6490