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- W4236058159 abstract "Abstract 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." @default.
- W4236058159 created "2022-05-12" @default.
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- W4236058159 date "2004-03-05" @default.
- W4236058159 modified "2023-10-03" @default.
- W4236058159 title "Aminopeptidase P" @default.
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- W4236058159 doi "https://doi.org/10.1002/9781119951438.eibc0597" @default.
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