3.4.11.9: Xaa-Pro aminopeptidase
This is an abbreviated version!
For detailed information about Xaa-Pro aminopeptidase, go to the full flat file.
Reaction
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
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Synonyms
aminoacylproline aminopeptidase, aminopeptidase P, aminopeptidase P-like enzyme, aminopeptidase P1, aminopeptidase, aminoacylproline, AMPP, AP-P, APaseP, APP, APP1, APPro, DAP-P, dapUm, Dr-smAPP, Ec-smAPP, ecAPP, hAPP1, hcAMPP, Icp55, LeAPP1, LeAPP2, M24B peptidase, mAmP, Membrane-bound AmP, Membrane-bound APP, membrane-bound proline-specific APaseP, More, Mt-smAPP, Pa-PepP, PEPP, PepQ, peptidase PepQ, PepX aminopeptidase, PfAPP, proline aminopeptidase, sll0136, small aminopeptidase-P, TgAPP, TvMP50, X-Pro aminopeptidase, X-prolyl aminopeptidase, X-prolyl aminopeptidase 2, X-prolyl aminopeptidase 3, X-prolyl peptidase, X-prolyl-dipeptidyl aminopeptidase, Xaa-Pro aminopeptidase, Xaa-Pro aminopeptidase-1, Xaa-Pro aminopeptidase-2, Xaa-Pro dipeptidase, XPD, XpmA, XPNEP2, XPNPEP-1, XPNPEP-2, XPNPEP1, XPNPEP2, XPNPEP3, YpdF
ECTree
Reaction
Reaction on EC 3.4.11.9 - Xaa-Pro aminopeptidase
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release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
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release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
mechanism, cis-trans specificity
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release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
acive site configuration, modeling, Asp449, Asp460, His523, Glu554, and Glu568 are in volved in metal binding in the active site, His429 and His523 are involved in shuttling protons during catalysis
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release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
isozyme APP-2 shows a preference for Arg-Pro-Pro-, Arg-Pro-Lys-, Pro-Pro-Gly-, -Phe-Gly- in descending order
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
H243 stabilizes substrate binding, H361 stabilizes substrate binding and the gem-diol catalytic intermediate. H350 forms part of a hydrophobic binding pocket that gives the enzyme its proline specificity
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
R404 participates in proton relay and in the hydrogen bond network
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release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
mechanism, cis-trans specificity
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