Article
Kinetic and crystallographic analysis of mutant Escherichia coli aminopeptidase P: insights into substrate recognition and the mechanism of catalysis.
Biochemistry - 24 Jan 2006
Graham Stephen C, Lilley Penelope E, Lee Mihwa, Schaeffer Patrick M, Kralicek Andrew V, Dixon Nicholas E, Guss J Mitchell
Abstract excerpt
Aminopeptidase P (APPro) is a manganese-dependent enzyme that cleaves the N-terminal amino acid from polypeptides where the second residue is proline. APPro shares a similar fold, substrate specificity, and catalytic mechanism with methionine aminopeptidase and prolidase. To investigate the roles of conserved residues at the active site, seven mutant forms of APPro were characterized kinetically and structurally....
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