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.
Word Map on EC 3.4.11.9
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3.4.11.9
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aminopeptidases
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apstatin
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xpnpep2
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lactococci
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medicine
- 3.4.11.9
- aminopeptidases
- apstatin
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xpnpep2
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lactococci
- medicine
Reaction
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide =
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
3.4.11.9 Xaa-Pro aminopeptidaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.4.11.9 - Xaa-Pro aminopeptidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D53A
site-directed mutagenesis, mutant D53A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
H193A
site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type
H281A
site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding
R55A
site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
Y56A
site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
H193A
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site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type
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H281A
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site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding
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R55A
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site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
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Y56A
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site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
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H193A
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site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type
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H281A
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site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding
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R55A
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site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
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Y56A
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site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
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H193A
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site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type
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H281A
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site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding
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R55A
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site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
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Y56A
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site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
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H193A
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site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type
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H281A
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site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding
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R55A
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site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
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Y56A
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site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
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H193A
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site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type
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H281A
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site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding
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R55A
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site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
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Y56A
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site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
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H193A
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site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type
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H281A
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site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding
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R55A
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site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
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Y56A
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site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
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H193A
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site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type
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H281A
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site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding
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R55A
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site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
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Y56A
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site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
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H193A
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site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type
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H281A
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site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding
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R55A
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site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
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Y56A
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site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
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D260A
D271A
E383A
H243A
H350A
H354A
H361A
E41A
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the mutant maintains 91% of the wild type activity and demonstrates that the acidic residue, which is considered as a stabilizing factor in the protonation of catalytic residue His498, plays only a marginal role in catalysis
R535A
site-directed mutagenesis, the mutant enzyme shows reduced kcat and Km compared to the wild-type enzyme. The respective levels of activity restoration are determined to be 86%, 31%, 16%, and 10% for guanidine hydrochloride, methylguanidine, aminoguanidine and N-ethyl-guanidine
W477E
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the mutant, designed to block dimer formation, shows only 6% of the wild type activity
Y527F
site-directed mutagenesis, the mutant enzyme shows reduced kcat and Km compared to the wild-type enzyme
E568Q
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site-directed mutagenesis, low expression level in COS-1 cells, inactive mutant
E588A
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site-directed mutagenesis, 66% remaining activity compared to the wild-type enzyme with substrate bradykinin
E588Q
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site-directed mutagenesis, 83% remaining activity compared to the wild-type enzyme with substrate bradykinin
H519K
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site-directed mutagenesis, 2.3% remaining activity compared to the wild-type enzyme with substrate bradykinin, increased Km, reduced kcat
H519L
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site-directed mutagenesis, 73.8% remaining activity compared to the wild-type enzyme with substrate bradykinin, increased Km
H532L
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site-directed mutagenesis, very low expression level in COS-1 cells, protein degradation, inactive mutant
additional information
D260A
MnA is bound at the active site, but the MnB site is empty. Loss of catalytic activity
D271A
no atoms of Mn(II) are bound at the active site. Loss of catalytic activity
E383A
both Mn-(II) atoms are present in the active site, but the bridging solvent molecule is located significantly farther from the metals than in wild-type. Loss of catalytic activity
E383A
crystallization data. One of the two metal sites is only partially occupied
H243A
crystallization data. Mutant is capable of binding the substrate L-Val-L-Pro-L-Leu
H350A
loss of catalytic activity. H350 forms part of a hydrophobic binding pocket that gives the enzym its proline specificity
H354A
MnB is present at the active site at less than full occupancy, and a water molecule occupies the MnA site. Loss of catalytic activity
additional information
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partial or complete deletion of N-terminal domain, complete loss of enzymic activity
additional information
design of an aminopeptidase P (APaseP) targeting tissue-specific construct conjugated to a homing peptide for selective binding to human breast-derived cancer cells. Homing peptides are short amino acid sequences derived from phage display libraries that have the unique property of localizing to specific organs. The molecular construct allows for tissue-specific drug delivery, by binding to APaseP in the vascular endothelium. The breast homing peptide is a cyclic nine-amino-acid peptide with the sequence CPGPEGAGC, referred to as PEGA. The PEGA peptide and similar peptide conjugates distribute to human breast tissue xenograft specifically and evaluate the interaction with the membrane-bound proline-specific APaseP by binding studies. In vivo localization of the breast tissue specific conjugate in a breast cancer xenograft mouse model, established by implanting enzyme-expressing human breast adenocarcinoma cell line MCF-7 in nude mice with estrogen supplementation
additional information
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design of an aminopeptidase P (APaseP) targeting tissue-specific construct conjugated to a homing peptide for selective binding to human breast-derived cancer cells. Homing peptides are short amino acid sequences derived from phage display libraries that have the unique property of localizing to specific organs. The molecular construct allows for tissue-specific drug delivery, by binding to APaseP in the vascular endothelium. The breast homing peptide is a cyclic nine-amino-acid peptide with the sequence CPGPEGAGC, referred to as PEGA. The PEGA peptide and similar peptide conjugates distribute to human breast tissue xenograft specifically and evaluate the interaction with the membrane-bound proline-specific APaseP by binding studies. In vivo localization of the breast tissue specific conjugate in a breast cancer xenograft mouse model, established by implanting enzyme-expressing human breast adenocarcinoma cell line MCF-7 in nude mice with estrogen supplementation
additional information
downregulation of XPNPEP1 in 786-O cells by stable transduction with small-hairpin (sh)RNAs
additional information
downregulation of XPNPEP1 in 786-O cells by stable transduction with small-hairpin (sh)RNAs
additional information
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downregulation of XPNPEP1 in 786-O cells by stable transduction with small-hairpin (sh)RNAs
additional information
kinetic analysis of MnCl2 activation of wild-type, Y527F and R535A hcAMPPs
additional information
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kinetic analysis of MnCl2 activation of wild-type, Y527F and R535A hcAMPPs
additional information
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construction of chimeric enzymes th-sl cAPP, in which half of the N-terminal domain is derived from Streptomyces costaricanus and the rest is Streptomyces lividans isoform II and sl-th cAPP, in which half of the N-terminal domain is Streptomyces lividans isoform II and the rest is Streptomyces costaricanus. Both chimera are activated by Zn2+. Th-sl cAPP and sl-th cAPP, respectively, form a tetramer and a dimer. The pH dependence and pKa values of th-sl cAPP were almost identical to those of Streptomyces costaricanus. In contrast, sl-th cAPP showed curves and pKa values that resembled those of Streptomyces lividans isoform II
additional information
construction of chimeric enzymes th-sl cAPP, in which half of the N-terminal domain is derived from Streptomyces costaricanus and the rest is Streptomyces lividans isoform II and sl-th cAPP, in which half of the N-terminal domain is Streptomyces lividans isoform II and the rest is Streptomyces costaricanus. Both chimera are activated by Zn2+. Th-sl cAPP and slth cAPP, respectively, form a tetramer and a dimer. The pH dependence and pKa values of th-sl cAPP are almost identical to those of Streptomyces costaricanus. In contrast, sl-th cAPP shows curves and pKa values that resemble those of Streptomyces lividans isoform II
additional information
Streptomyces murinus TH-4
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construction of chimeric enzymes th-sl cAPP, in which half of the N-terminal domain is derived from Streptomyces costaricanus and the rest is Streptomyces lividans isoform II and sl-th cAPP, in which half of the N-terminal domain is Streptomyces lividans isoform II and the rest is Streptomyces costaricanus. Both chimera are activated by Zn2+. Th-sl cAPP and slth cAPP, respectively, form a tetramer and a dimer. The pH dependence and pKa values of th-sl cAPP are almost identical to those of Streptomyces costaricanus. In contrast, sl-th cAPP shows curves and pKa values that resemble those of Streptomyces lividans isoform II
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additional information
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deletion of TgAPP gene in the parasite through a CRISPR/Cas9 system
additional information
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deletion of TgAPP gene in the parasite through a CRISPR/Cas9 system
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