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- W170622370 abstract "This chapter discusses the structural chemistry and the biological aspects of pro-aminopeptidase processing protease. PA protease removes the N-terminal propeptide from proenzymes of A. caviae and V. proteolyticus aminopeptidase. Cleavage sites are at the Leu-Phe-Ser–Ala-Pro-Pro-Leu bond and the Ser-Phe-Val–Met-Pro-Pro-Leu bond, respectively. The N-terminal propeptide fragment, which was removed from the proenzyme by PA protease, could not be detected. This fact indicates that the removed propeptide region was degraded into smaller oligopeptides by PA protease and/or the activated aminopeptidase. The proenzyme of A. caviae aminopeptidase is also processed by other proteolytic enzymes such as trypsin, papain and thermolysin. The processing activities of these proteases are markedly lower than that of PA protease. The gene coding for a 63 kDa protein was cloned and sequenced. The deduced amino acid sequence of the preproenzyme encodes a 19-residue predicted signal peptide, 165-residue N-terminal propeptide, 297-residue mature protein and 109-residue C-terminal propeptide. Processing of the proenzyme involves a stepwise autoprocessing mechanism. It is found that the N-terminal propeptide is autocatalytically removed and the C-terminal propeptide is autoprocessed after the degradation of the N-terminal propeptide." @default.
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- W170622370 date "2004-01-01" @default.
- W170622370 modified "2023-10-16" @default.
- W170622370 title "Pro-aminopeptidase processing protease" @default.
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- W170622370 doi "https://doi.org/10.1016/b978-0-12-079611-3.50108-7" @default.
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