Alternative titles; symbols
HGNC Approved Gene Symbol: RNPEP
Cytogenetic location: 1q32.1 Genomic coordinates (GRCh38) : 1:201,982,648-202,006,143 (from NCBI)
Aminopeptidase B (EC 3.4.11.6) was originally defined as an exopeptidase capable of trimming basic amino acid residues from the NH2 terminus of peptide substrates (Hopsu et al., 1964). Cadel et al. (1995) demonstrated that it is a Zn(2+)-dependent exopeptidase that selectively removes arginine and/or lysine residues from the N terminus of several peptide substrates. Structurally it is related to leukotriene A4 hydrolase (151570), an important enzyme of the arachidonic acid pathway. The structural relationship has its functional counterpart in the capacity of aminopeptidase B to hydrolyze leukotriene A4 (Cadel et al., 1997). Antibodies raised against the isolated peptidase show that it is widely distributed in a number of tissues, including endocrine and nonendocrine cell types. It is secreted by rat PC12 pheochromocytoma cells and associated with the external face of their plasma membrane. Together these data strongly argue in favor of participation of this ubiquitous and in vitro bifunctional enzyme in the final stages of precursor processing mechanisms occurring either during the intracellular transport along the secretory pathway or at the plasma membrane level, or both (Aurich-Costa et al., 1997).
By fluorescence in situ hybridization, Aurich-Costa et al. (1997) mapped the RNPEP gene to chromosome 1q32.1-q32.2.
Aurich-Costa, J., Cadel, S., Gouzy, C., Foulon, T., Cherif, D., Cohen, P. Assignment of the aminopeptidase B gene (RNPEP) to human chromosome 1 band q32 by in situ hybridization. Cytogenet. Cell Genet. 79: 143-144, 1997. [PubMed: 9533033] [Full Text: https://doi.org/10.1159/000134703]
Cadel, S., Foulon, T., Viron, A., Balogh, A., Midol-Monnet, S., Noel, N., Cohen, P. Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A4 hydrolase. Proc. Nat. Acad. Sci. 94: 2963-2968, 1997. [PubMed: 9096329] [Full Text: https://doi.org/10.1073/pnas.94.7.2963]
Cadel, S., Pierotti, A. R., Foulton, T., Creminon, C., Barre, N., Segretain, D., Cohen, P. Aminopeptidase-B in the rat testes: isolation, functional properties and cellular localization in the seminiferous tubules. Molec. Cell. Endocr. 110: 149-160, 1995. [PubMed: 7672445] [Full Text: https://doi.org/10.1016/0303-7207(95)03529-g]
Hopsu, V. K., Kantonen, U. M., Glenner, G. G. A peptidase from rat tissues selectively hydrolyzing N-terminal arginine and lysine residues. Life Sci. 3: 1449-1453, 1964.