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Function Of The Signal Peptide And N- And C-Terminal Propeptides In The Leucine Aminopeptidase From Aeromonas Proteolytica, Krzysztof Bzymek, Ventris D'Souza, Guanjing Chen, Heidi Campbell, Alice Mitchell, Richard Holz
Function Of The Signal Peptide And N- And C-Terminal Propeptides In The Leucine Aminopeptidase From Aeromonas Proteolytica, Krzysztof Bzymek, Ventris D'Souza, Guanjing Chen, Heidi Campbell, Alice Mitchell, Richard Holz
Richard C. Holz
The leucine aminopeptidase from Aeromonas proteolytica (also known as Vibrio proteolyticus) (AAP) is a metalloenzyme with broad substrate specificity. The open reading frame (ORF) for AAP encodes a 54 kDa enzyme, however, the extracellular enzyme has a molecular weight of 43 kDa. This form of AAP is further processed to a mature, thermostable 32 kDa form but the exact nature of this process is unknown. Over-expression of different forms of AAP in Escherichia coli (with AAP's native leader sequence, with and without the N- and/or C-terminal propeptides, and as fusion protein) has allowed a model for the processing of wild-type …