Germination-specific cortex-lytic enzymes from Clostridium perfringens S40 spores: time of synthesis, precursor structure and regulation of enzymatic activity |
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Authors: | Urakami K Miyata S Moriyama R Sugimoto K Makino S |
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Affiliation: | Department of Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Japan. |
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Abstract: | Germination-specific enzymes, an amidase and a muramidase, of Clostridium perfringens S40 were synthesized at the time of forespore formation during sporulation. The amidase had a unique precursor structure consisting of four domains: the N-terminal pre-sequence, the N-terminal pro-sequence, mature enzyme and the C-terminal pro-sequence. The N-terminal pre-sequence and the C-terminal pro-sequence were sequentially processed at the time of development of phase-bright spores, and the resulting inactive pro-enzyme was activated by cleavage of the N-terminal pro-sequence with a specific protease during germination. A possible mechanism for the regulation of activity of muramidase, which is produced as a mature form and does not need processing for activation, is presented. |
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Keywords: | Clostridium perfringens spore Spore-lytic enzyme Germination Precursor structure |
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