Aminopeptidase P
J Mitchell Guss
University of Sydney, Department of Biochemistry, NSW, Australia, 2006
Search for more papers by this authorHans C Freeman
University of Sydney, Department of Biochemistry, NSW, Australia, 2006
Search for more papers by this authorJ Mitchell Guss
University of Sydney, Department of Biochemistry, NSW, Australia, 2006
Search for more papers by this authorHans C Freeman
University of Sydney, Department of Biochemistry, NSW, Australia, 2006
Search for more papers by this authorAbstract
Aminopeptidase P is a metalloprotease, which specifically cleaves the N-terminal residue of a peptide if the second residue is proline. The enzyme is a member of the pita-bread fold family of metalloenzymes that includes methionine aminopeptidase and prolidase. Escherichia coli aminopeptidase P is a tetramer in crystals and in solution. Each subunit has a dinuclear manganese (Mn) centre at its active site. A hydroxide ion that bridges the Mn atoms has been identified as the nucleophile in the enzymatic reaction.
3D Structure
Schematic representation of the structure of AMPP showing the monomer as a ribbon representation. The chain is ramp-colored from blue at the N-terminus to red at the C-terminus. The Mn ions in the active site are shown as magenta spheres. Prepared with programs MOLSCRIPT44 and RASTER3D.45 PDB code: 1AZ9.
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