Elastolytic activity of MAP1, a protease from Myxococcus xanthus.
MAP1, a protease isolated from Myxococcus xanthus, is demonstrated to be an elastase. Although its elastolytic activity is lower than that of other well-known elastases, the size distribution of solubilized elastin peptides is similar. MAP1 as pancreatic elastase releases peptides with molecular weights higher than 10,000. However, the specificity of MAP1 is different since this enzyme cannot hydrolyze alanine oligomers as do pancreatic and Pseudomonas aeruginosa elastases.
Laboratoire de Biotechnologie, Faculté des Sciences de Limoges, France.
L
L
Dumont
B
B
Verneuil
R
R
Julien
J
J
Wallach
D000818:Animals; D001011:Aorta / Q000378:metabolism; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D003217:Conductometry; D004549:Elastin / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D016941:Myxococcus xanthus / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000378:metabolism*; D012680:Sensitivity and Specificity; D013379:Substrate Specificity
D004549:Elastin; C088847:Myxococcus xanthus alkaline protease 1; D010196:Pancreatic Elastase