title: Substrate specificity of collagenolytic proteases from the king crab Paralithodes camtschatica.
abstract: Substrate specificity of two collagenolytic proteases from the king crab Paralithodes camtschatica has been studied. Both proteases are shown to hydrolyze effectively type I and III collagens, gelatin and fibrinogen. The variety of products formed during the enzymatic hydrolysis of the proteins appeared to be different for crab proteases A and C. Studies on peptide hydrolysis demonstrated that protease A cleaves preferably peptide bonds with Arg and Lys as carbonyl components, while protease C prefers hydrophobic amino acids. Kinetic constants of hydrolysis for low molecular weight substrates in the presence of crab proteases have been determined. This allowed us to characterize collagenolytic protease A as a trypsin-like protease. By contrast, collagenolytic protease C was classified as chymotrypsin-like protease although this protease and bovine chymotrypsin are not completely similar. Collagenase substrates Pz-Pro-Leu-Gly-Pro-D-Arg and Z-Gly-Pro-Ala-Gly-Pro-Ala were found to be resistant to both crab proteases.
authors.affiliation: Department of Chemistry, Moscow State University, Russia.
authors.lastname: Sakharov IYu
authors.forename: F E
authors.initials: FE
authors.lastname: Litvin
authors.forename: O V
authors.initials: OV
authors.lastname: Mitkevitch
authors.forename: G P
authors.initials: GP
authors.lastname: Samokhin
authors.forename: Z D
authors.initials: ZD
authors.lastname: Bespalova
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003386:Brachyura / Q000378:metabolism*; D003094:Collagen / Q000737:chemistry / Q000378:metabolism*; D010450:Endopeptidases / Q000378:metabolism*; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D010446:Peptide Fragments; D003094:Collagen; D010450:Endopeptidases