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Literature summary for 3.4.11.9 extracted from

  • Li, X.; Lou, Z.; Li, X.; Zhou, W.; Ma, M.; Cao, Y.; Geng, Y.; Bartlam, M.; Zhang, X.C.; Rao, Z.
    Structure of human cytosolic X-prolyl aminopeptidase: a double Mn(II)-dependent dimeric enzyme with a novel three-domain subunit (2008), J. Biol. Chem., 283, 22858-22866.
    View publication on PubMed
Search for more literature for 3.4.11.9

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapour diffusion method, using 20% (v/v) polyethylene glycol 400, 0.15 M CaCl2, and 100 mM HEPES (pH 7.5) Homo sapiens

Protein Variants

Protein Variants Comment Organism
E41A 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 Homo sapiens
W477E the mutant, designed to block dimer formation, shows only 6% of the wild type activity Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
EDTA the activity of the enzyme drops to 10% after treatment with 50 mM EDTA Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.078
-
 bradykinin wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C Homo sapiens
0.308
-
 L-Arg-L-Pro-L-Pro wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Homo sapiens 5829
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ the enzyme is double Mn2+-dependent for its activity Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
 2 * 70000, X-ray crystallography Homo sapiens
140000
-
 X-ray crystallography Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA resin column chromatography and Hitrap Q HP affinity column chromatography Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
bradykinin + H2O
-
 Homo sapiens L-Arg + des-Arg-bradykinin
-
 ?
L-Arg-L-Pro-L-Pro + H2O
-
 Homo sapiens L-Arg + L-Pro-L-Pro
-
 ?
L-prolyl-peptide + H2O X-prolyl aminopeptidase catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides Homo sapiens L-proline + peptide
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 70000, X-ray crystallography Homo sapiens

Synonyms

Synonyms Comment Organism
aminopeptidase P
-
 Homo sapiens
AP-P
-
 Homo sapiens
X-prolyl aminopeptidase
-
 Homo sapiens
XPNPEP1
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.8
-
 bradykinin wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C Homo sapiens
7.7
-
 L-Arg-L-Pro-L-Pro wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C Homo sapiens