title: Mode of action of Clostridium perfringens initiation protein (spore-lytic enzyme).
abstract: The extracellular initiation protein (IP; spore germination enzyme) produced by Clostridium perfringens was further purified and characterized. IP hydrolysed spore cortical fragments with the release of free amino groups. End group analysis of hydrolysed fragments indicated the presence of N-terminal alanine but no reducing sugars. Molecular weight analysis of IP- and lysozyme-treated fluorescamine-labelled cortical fragments indicated that IP acts only on peptidoglycan chains containing cross-linked peptide subunits. IP failed to hydrolyse a number of nitrophenyl-conjugated glucopyranosides and galactopyranosides. The results indicate that IP is an N-acetylmuramyl-L-alanine amidase.
mesh_terms: D000581:Amidohydrolases / Q000378:metabolism*; D003016:Clostridium perfringens / Q000201:enzymology*; D005450:Fluorescamine; D006868:Hydrolysis; D007700:Kinetics; D008970:Molecular Weight; D009077:Mucins / Q000494:pharmacology; D009113:Muramidase / Q000378:metabolism; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000302:isolation & purification / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism; D010448:Peptide Initiation Factors; D010457:Peptidoglycan / Q000378:metabolism; D013053:Spectrophotometry; D013171:Spores, Bacterial / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D009077:Mucins; D010446:Peptide Fragments; D010448:Peptide Initiation Factors; D010457:Peptidoglycan; D005450:Fluorescamine; D009113:Muramidase; D000581:Amidohydrolases; D009238:N-Acetylmuramoyl-L-alanine Amidase