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 (Crystallization
Crystallization on EC 3.4.11.9 - Xaa-Pro aminopeptidase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme by sitting drop vapour diffusion method, crystallization buffer containing 17.5% PEG 3350, 0.1 M bis-tris propane, pH 8.5, and 0.2 M sodium malonate is mixed with an equal volume of 3 mg/ml protein in 10 mM Tris/HCl, pH 8.0, and 150 mM NaCl,16°C, X-ray diffraction structure determination and analysis at 1.93 A resolution
purified recombinant enzyme, mixing of 0.002 ml of about 15 mg/ml protein in 20 mM Tris-HCl pH 8.0, 200 mM NaCl, with 0.002 ml crystallization solution containing 0.1 M phospho-citrate, pH 4.6, 0.2 M NaCl, and 22% PEG 8000, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement using the putative prolidase from Telmatobius sibiricus (PDB ID: 4FKC) as template
8 mg/ml purified recombinant enzyme in Tris, pH 8.5, hanging drop vapour diffusion method, 0.003 ml mixed with 0.002 ml reservoir solution containing 25% PEG 4000, 0.1 M Tris-HCl, pH 8.0, 0.2 M sodium acetate, and 1 mM MnCl2, 1 month at 4°C, cryoprotectant is 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 2.4 A resolution, modeling
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Mn(II)-form of enzyme and substituted with Mg2+, Zn2+, Ca2+, Na+ and apo-enzyme in complex with L-Val-L-Pro-L-Leu
mutants E383A, H361A and H243A in complex with substrate L-Val-L-Pro-L-Leu. Substrate interacts with one of the active site metal ions via its terminal amino group
purified recombinant enzyme, mixing of 0.002 ml of about 15 mg/ml protein in 20 mM Tris-HCl pH 8.0, 200 mM NaCl, with 0.002 ml of crystallization solution containing 1.4 M trisodium citrate, 0.1 M sodium cacodylate, pH 6.5, 10% glycerol, and 0.5 mM ZnCl2, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement using the putative prolidase from Telmatobius sibiricus (PDB ID: 4FKC) as template
hanging drop vapour diffusion method, using 20% (v/v) polyethylene glycol 400, 0.15 M CaCl2, and 100 mM HEPES (pH 7.5)
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purified recombinant enzyme PfAPP both unliganded and in complex with inhibitor apstatin, hanging drop vapor diffusion method, mixing of 2:1 vl/v ratio of 6 mg/ml protein solution with reservoir containing 40-50% 2-methyl-2,4-pentanediol, and 0.1 M sodium cacodylate, pH 5.6-6.2, 3-7 days, X-ray diffraction structure determination and analysis at 2.30-2.35 A resolution. Crystals of the apstatin:PfAPP complex are obtained by soaking unliganded crystals in mother liquor supplemented with 2 mM apstatin for 1 h. For the unliganded PfAPP structure, the molecular replacement search model is prepared from the structure of human APP1 (PDB ID 3CTZ)
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purified recombinant enzyme, X-ray diffraction structure determination and analysis at 1.78-1.85 A resolution
purified recombinant His6-tagged enzyme, microbatch crystallization method, mixing of 0.001 ml of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with 0.001 ml of crstallization solution containing 30% v/v PEG400, 0.1 M sodium acetate, 0.2 M calcium acetate, pH 4.5, the pH is adjusted to pH 5.8 with acetic acid, X-ray diffraction structure determination and analysis at 3.4 A, molecular replacement based on the structure of human prolidase (PDB ID 2IW2)
XPD43 is crystallized to 1.83 A resolution using the microbatch-under-oil technique
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