Identification of Critical Residues in the Active Site of Porcine Membrane-Bound Aminopeptidase P

• Published in: Biochemistry (Easton) Vol. 39; no. 49; pp. 15129 - 15135
• Main Authors: Cottrell, Graeme S, Hyde, Ralph J, Lim, Jaeseung, Parsons, Mark R, Hooper, Nigel M, Turner, Anthony J
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 12.12.2000
• Subjects: Amino Acid Sequence; Amino Acids, Dicarboxylic - genetics; Aminopeptidases - metabolism; Animals; Bradykinin - metabolism; Catalytic Domain; Computer Simulation; Histidine - genetics; Kinetics; Ligands; Membrane Proteins - metabolism; Models, Molecular; Molecular Sequence Data; Mutation; Oligopeptides - metabolism; Sequence Homology, Amino Acid; Swine

The membrane-bound form of mammalian aminopeptidase P (AP-P; EC 3.4.11.9) is a mono-zinc-containing enzyme that lacks any of the typical metal binding motifs found in other zinc metalloproteases. To identify residues involved in metal binding and catalysis, sequence and structural information was us...