Germination-specific cortex-lytic enzymes from Clostridium perfringens S40 spores: time of synthesis, precursor structure and regulation of enzymatic activity.
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.
Urakami
K
K
Department of Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Japan.
Miyata
S
S
Moriyama
R
R
Sugimoto
K
K
Makino
S
S
D000581:Amidohydrolases / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003016:Clostridium perfringens / Q000201:enzymology* / Q000235:genetics / Q000502:physiology*; D004792:Enzyme Precursors / Q000737:chemistry; D015964:Gene Expression Regulation, Bacterial; D013058:Mass Spectrometry / Q000379:methods; D009113:Muramidase / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D013171:Spores, Bacterial / Q000201:enzymology / Q000502:physiology
D004792:Enzyme Precursors; D009113:Muramidase; D000581:Amidohydrolases; C019665:amidase