Iy. Sakharov et al., SUBSTRATE-SPECIFICITY OF COLLAGENOLYTIC PROTEASES FROM THE KING CRAB PARALITHODES CAMTSCHATICA, Comparative biochemistry and physiology. B. Comparative biochemistry, 107(3), 1994, pp. 411-417
Substrate specificity of two collagenolytic proteases from the king cr
ab Pavalithodes camtschatica has been studied. Both proteases are show
n to hydrolyze effectively type I and III collagens, gelatin and fibri
nogen. The variety of products formed during the enzymatic hydrolysis
of the proteins appeared to be different for crab proteases A and C. S
tudies on peptide hydrolysis demonstrated that protease A cleaves pref
erably peptide bonds with Arg and Lys as carbonyl components, while pr
otease C prefers hydrophobic amino acids. Kinetic constants of hydroly
sis for low molecular weight substrates in the presence of crab protea
ses have been determined. This allowed us to characterize collagenolyt
ic 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. Collagena
se substrates Pz-Pro-Leu-Gly-Pro-D-Arg and Z-Gly-Pro-Ala-Gly-Pro-Ala w
ere found to be resistant to both crab proteases.