Literature summary for 3.4.11.9 extracted from

Graham, S.C.; Lee, M.; Freeman, H.C.; Guss, J.M.
An orthorhombic form of Escherichia coli aminopeptidase P at 2.4 A resolution (2003), Acta Crystallogr. Sect. D, 59, 897-902.

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Cloned(Commentary)

Cloned (Comment)	Organism
overexpression in Escherichia coli	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mn2+	2 ions per enzyme molecule, ligand binding structure determination	Escherichia coli
additional information	the active site contains a dinuclear metal binding site, the enzyme contains 12 metal atoms per molecule, 2 of which are Mn2+ ions	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme from Escherichia coli	Escherichia coli

Subunits

Subunits	Comment	Organism
hexamer	arranged in 2 types of tetramers, one tetramer comprises 4 crystallographically independent subunits, while the other tetramer comprises 2 pairs of subunits related by a crystallographic 2fold axis	Escherichia coli

Synonyms

Synonyms	Comment	Organism
aminopeptidase P	-	Escherichia coli
AMPP	-	Escherichia coli
More	the enzyme belongs to the peptidase family M24	Escherichia coli

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Release 2023.1 (January 2023)