Characterization of aminopeptidase B: Substrate specificity and affector studies

Hopsu, V. K.; Mäkinen, Kauko K.; Glenner, George G.

doi:10.1016/0003-9861(66)90381-x

Cited by 78 publications

(13 citation statements)

References 9 publications

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“…In contrast to Cp-E (6, 7), Ap-B is relatively poorly understood. The present and previous reports (13,18,19) unequivocally demonstrate the existence in several tissues of an Ap-B with a strict selectivity for the removal of Arg and͞or Lys residues at the N terminus of peptides. Ap-B can be considered, on the basis of the presence of the HEXXHX 18 E zinc binding motif in its amino acid sequence, as a metalloexoprotease of the M1 family (20).…”

Section: Discussionsupporting

confidence: 80%

“…However, complete removal of the basic residues of a doublet in a precursor can, in principle, proceed alternatively by three different pathways, of which two may involve an aminopeptidase-B (Ap-B) (1). Several reports showed the existence of endoproteases with a cleavage specificity for the N terminus of basic residues present in the doublet (8)(9)(10)(11)(12) and of poorly characterized Ap-B-like activities (9,(13)(14)(15)). An Ap-B (EC 3.4.11.6) activity initially was identified in several rat tissues (13) and was defined as an exopeptidase able to remove basic residues from the N terminus of L-amino acid-␤-naphthylamide, dipeptides, and kallidin 10 (13,14).…”

mentioning

confidence: 99%

“…Several reports showed the existence of endoproteases with a cleavage specificity for the N terminus of basic residues present in the doublet (8)(9)(10)(11)(12) and of poorly characterized Ap-B-like activities (9,(13)(14)(15)). An Ap-B (EC 3.4.11.6) activity initially was identified in several rat tissues (13) and was defined as an exopeptidase able to remove basic residues from the N terminus of L-amino acid-␤-naphthylamide, dipeptides, and kallidin 10 (13,14). More recent work has provided information about the biochemical and structural properties of the enzyme (16,17).…”

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confidence: 99%

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Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A₄hydrolase

Cadel

Foulon

Viron

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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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 ''HEXXHX 18 E'' signature, which allowed its classification as a member of the M1 family of metallopeptidases. It exhibits 33% identity and 48% similarity with leukotriene-A 4 hydrolase, a relation further supported by the capacity of Ap-B to hydrolyze leukotriene A 4 . 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.

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Section: Discussionsupporting

confidence: 80%

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confidence: 99%

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confidence: 99%

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Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A₄hydrolase

Cadel

Foulon

Viron

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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“…The selectivity of RAP for arginine distinguishes it from eukaryotic aminopeptidase B, which cleaves arginine and lysine from the N terminus equally well (23). Proteolysis with proline in the second position is generally reserved solely for members of the aminopeptidase P family (4).…”

Section: Discussionmentioning

confidence: 99%

Extracellular Arginine Aminopeptidase from Streptococcus gordonii FSS2

et al. 2002

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Streptococcus gordonii is a primary etiological agent in the development of subacute bacterial endocarditis (SBE), producing thrombus formation and tissue damage on the surfaces of heart valves. This is ironic, considering its normal role as a benign inhabitant of the oral microflora. However, strain FSS2 of S. gordonii has been found to produce several extracellular aminopeptidase-and fibrinogen-degrading activities during growth in a pH-controlled batch culture. In this report, we describe the purification, characterization, and partial cloning of a predicted serine class arginine aminopeptidase (RAP) with some cysteine class characteristics. Isolation of this enzyme by anion-exchange, gel filtration, and isoelectric focusing chromatography yielded a protein monomer of approximately 70 kDa, as shown by matrix-assisted laser desorption ionization, gel filtration, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis under denaturing conditions. Nested-PCR cloning enabled the isolation of a 324-bp-long DNA fragment encoding the 108-amino-acid N terminus of RAP. Culture activity profiles and N-terminal sequence analysis indicated the export of this protein from the cell surface. Homology was found with a putative dipeptidase from Streptococcus pyogenes and nonspecific dipeptidases from Lactobacillus helveticus and Lactococcus lactis. We believe that RAP may serve as a critical factor for arginine acquisition during nutrient stress in vivo and also in the proteolysis of host proteins and peptides during SBE pathology.

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“…Although APase B was first purified from rat liver in 1966 [5], the physiological functions of this enzyme have yet to be elucidated. In our laboratory, the presence of a ubenimex-sensitive APase B-like enzyme was indicated by the fact that ubenimex inhibited proliferation of K562 human chronic myeloid leukemia cells.…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of a ubenimex (Bestatin)‐sensitive aminopeptidase B‐like enzyme from K562 human chronic myeloid leukemia cells

et al. 1994

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A ubenimex-sensitive aminopeptidase B-like enzyme was purified from the non-membrane-bound fraction of K562 cells by a series of chromatographic procedures and slab-gel electrophoresis. The apparent molecular mass of the enzyme was estimated to be 73 kDa by SDS-PAGE. The aminopeptidase activity was activated by chloride ions and inhibited by Zn*+, Cu*+, Cd*', and p-chloromercuribenzoic acid. Ubenimex was a potent inhibitor of this aminopeptidase in the nanomolar range. The sequence of the N-terminus of the protein was not determined. Partial amino acid sequencing revealed that the N-terminus of this aminopeptidase B-like enzyme was blocked by acylation. The partial sequences of the two fragments produced by CNBr cleavage and an acylamino acid-releasing reaction showed this enzyme to be a new aminopeptidase.

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Characterization of aminopeptidase B: Substrate specificity and affector studies

Cited by 78 publications

References 9 publications

Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A₄hydrolase

Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A₄hydrolase

Extracellular Arginine Aminopeptidase from Streptococcus gordonii FSS2

Purification and characterization of a ubenimex (Bestatin)‐sensitive aminopeptidase B‐like enzyme from K562 human chronic myeloid leukemia cells

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Characterization of aminopeptidase B: Substrate specificity and affector studies

Cited by 78 publications

References 9 publications

Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A4 hydrolase

Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A4 hydrolase

Extracellular Arginine Aminopeptidase from Streptococcus gordonii FSS2

Purification and characterization of a ubenimex (Bestatin)‐sensitive aminopeptidase B‐like enzyme from K562 human chronic myeloid leukemia cells

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Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A₄hydrolase

Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A₄hydrolase