Xaa-Pro aminopeptidase 2 is an
enzyme that in humans is encoded by the XPNPEP2gene.[5][6][7]
Aminopeptidase P is a
hydrolase specific for N-terminal imido bonds, which are common to several collagen degradation products, neuropeptides, vasoactive peptides, and cytokines. Structurally, the enzyme is a member of the 'pita bread fold' family and occurs in mammalian tissues in both soluble and
GPI-anchored membrane-bound forms. A membrane-bound and soluble form of this enzyme have been identified as products of two separate genes.[7]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Venema RC, Ju H, Zou R, Venema VJ, Ryan JW (Dec 1997). "Cloning and tissue distribution of human membrane-bound aminopeptidase P". Biochim Biophys Acta. 1354 (1): 45–8.
doi:
10.1016/s0167-4781(97)00126-7.
PMID9375790.
^Sprinkle TJ, Stone AA, Venema RC, Denslow ND, Caldwell C, Ryan JW (Apr 1999). "Assignment of the membrane-bound human aminopeptidase P gene (XPNPEP2) to chromosome Xq25". Genomics. 50 (1): 114–6.
doi:
10.1006/geno.1998.5302.
PMID9628831.
Vanhoof G, De Meester I, Goossens F, et al. (1992). "Kininase activity in human platelets: cleavage of the Arg1-Pro2 bond of bradykinin by aminopeptidase P". Biochem. Pharmacol. 44 (3): 479–87.
doi:
10.1016/0006-2952(92)90439-P.
PMID1510698.
Cottrell GS, Hyde RJ, Hooper NM, Turner AJ (1998). "The cloning and functional expression of human pancreatic aminopeptidase P". Biochem. Soc. Trans. 26 (3): S248.
doi:
10.1042/bst026s248.
PMID9765967.
Prueitt RL, Ross JL, Zinn AR (2000). "Physical mapping of nine Xq translocation breakpoints and identification of XPNPEP2 as a premature ovarian failure candidate gene". Cytogenet. Cell Genet. 89 (1–2): 44–50.
doi:
10.1159/000015560.
PMID10894934.
S2CID46232057.
Fu GK, Wang JT, Yang J, et al. (2005). "Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes". Genomics. 84 (1): 205–10.
doi:
10.1016/j.ygeno.2004.01.011.
PMID15203218.
Xaa-Pro aminopeptidase 2 is an
enzyme that in humans is encoded by the XPNPEP2gene.[5][6][7]
Aminopeptidase P is a
hydrolase specific for N-terminal imido bonds, which are common to several collagen degradation products, neuropeptides, vasoactive peptides, and cytokines. Structurally, the enzyme is a member of the 'pita bread fold' family and occurs in mammalian tissues in both soluble and
GPI-anchored membrane-bound forms. A membrane-bound and soluble form of this enzyme have been identified as products of two separate genes.[7]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Venema RC, Ju H, Zou R, Venema VJ, Ryan JW (Dec 1997). "Cloning and tissue distribution of human membrane-bound aminopeptidase P". Biochim Biophys Acta. 1354 (1): 45–8.
doi:
10.1016/s0167-4781(97)00126-7.
PMID9375790.
^Sprinkle TJ, Stone AA, Venema RC, Denslow ND, Caldwell C, Ryan JW (Apr 1999). "Assignment of the membrane-bound human aminopeptidase P gene (XPNPEP2) to chromosome Xq25". Genomics. 50 (1): 114–6.
doi:
10.1006/geno.1998.5302.
PMID9628831.
Vanhoof G, De Meester I, Goossens F, et al. (1992). "Kininase activity in human platelets: cleavage of the Arg1-Pro2 bond of bradykinin by aminopeptidase P". Biochem. Pharmacol. 44 (3): 479–87.
doi:
10.1016/0006-2952(92)90439-P.
PMID1510698.
Cottrell GS, Hyde RJ, Hooper NM, Turner AJ (1998). "The cloning and functional expression of human pancreatic aminopeptidase P". Biochem. Soc. Trans. 26 (3): S248.
doi:
10.1042/bst026s248.
PMID9765967.
Prueitt RL, Ross JL, Zinn AR (2000). "Physical mapping of nine Xq translocation breakpoints and identification of XPNPEP2 as a premature ovarian failure candidate gene". Cytogenet. Cell Genet. 89 (1–2): 44–50.
doi:
10.1159/000015560.
PMID10894934.
S2CID46232057.
Fu GK, Wang JT, Yang J, et al. (2005). "Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes". Genomics. 84 (1): 205–10.
doi:
10.1016/j.ygeno.2004.01.011.
PMID15203218.