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.

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

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Release 2023.1 (January 2023)