[Substrate specificity of collagenolytic proteases from the hepatopancreas of the of the Kamchatka crab].
The substrate specificity of two isozymes of collagenolytic protease of the crab (Paralithodes camtschatica) was studied. It was found that both proteases can effectively hydrolyze type I and III collagens, as well as gelatin, the set of products yielded by enzymatic hydrolysis being different for isozymes A and C. Hydrolysis of some well-known peptides revealed that isozyme A predominantly cleaves the peptide bonds containing arginine and lysine residues, whereas isozyme C predominantly hydrolyzes bonds containing hydrophobic amino acids. The catalytic constants for the hydrolysis of several low molecular weight substrates in the presence of P. camtschatica proteases were determined, which allowed to attribute isozyme A to trypsin-like, and isozyme C to chymotrypsin-like proteinases. The peptide substrates of collagenase, Pz-Pro-Leu-Gly-Pro-D-Arg and Z-Gly-Pro-Ala-Gly-Pro-Ala are not hydrolyzed isozymes of crab collagenolytic protease.
Sakharov
I Iu
IIu
Litvin
F E
FE
D000595:Amino Acid Sequence; D000818:Animals; D003386:Brachyura; D002384:Catalysis; D002918:Chymotrypsin / Q000378:metabolism; D003094:Collagen / Q000378:metabolism*; D010450:Endopeptidases / Q000378:metabolism*; D005780:Gelatin / Q000378:metabolism; D006868:Hydrolysis; D007527:Isoenzymes / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D010179:Pancreas / Q000201:enzymology; D013379:Substrate Specificity; D014357:Trypsin / Q000378:metabolism
D007527:Isoenzymes; D005780:Gelatin; D003094:Collagen; D010450:Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin