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Literature summary for 3.4.11.9 extracted from

  • Graham, S.C.; Bond, C.S.; Freeman, H.C.; Guss, J.M.
    Structural and functional implications of metal ion selection in aminopeptidase P, a metalloprotease with a dinuclear metal center (2005), Biochemistry, 44, 13820-13836.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
Mn(II)-form of enzyme and substituted with Mg2+, Zn2+, Ca2+, Na+ and apo-enzyme in complex with L-Val-L-Pro-L-Leu Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
L-Pro-L-Leu product inhibition, a third metal binding site is formed by two conserved His-residues and L-Pro-L-Leu Escherichia coli
Zn2+ strong Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ required Escherichia coli
additional information not activating: Mg2+, Zn2+, Na+, Ca2+ Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P15034
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