The prolyl aminopeptidase from Lactobacillus delbrueckii subsp. bulgaricus belongs to the α/β hydrolase fold family

1999 
Abstract Prolyl aminopeptidase (PepIP) of Lactobacillus delbrueckii subsp. bulgaricus displays the Gly-x-Ser-x-Gly-Gly consensus motif surrounding the catalytic serine of the prolyl oligopeptidases family. Sequence comparison revealed that this motif and two other domains appear well conserved among bacterial PepIPs and members of the α/β hydrolase fold family. Secondary structural predictions of PepIP were performed from amino acid sequence and corroborated by circular dichroism analysis. These predictions well matched the core structure of α/β hydrolases organised in eight β-sheets connected by α-helices. We obtained 26 mutants of PepIP by chemical or site-directed mutagenesis. Most substitutions associated with stable and inactive mutant proteins were mainly located in the three conserved boxes (including the catalytic serine motif). Taken together, our results strongly suggest that PepIP belongs to the α/β hydrolase fold family and that Ser 107 , Asp 246 and His 273 constitute the catalytic triad of the enzyme.
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