Proteinases of Streptomyces fradiae. III. Catalytic and some physico- chemical properties of keratinolytic proteinase.
It has been shown that keratinase--proteinase PIV, the main enzyme of the proteolytic system of S. fradiae, is characterized by high effectiveness in its action on AcAla3OMe--exceeding elastase in catalytic effectiveness several times. This proteinase also cleaves ester and amide bonds formed by the residues of aromatic and basic amino acids, but with a lower effectiveness than chymotrypsin or trypsin. It has also been shown that proteinase IV is a typical serine enzyme highly sensitive to DFP, acting in strongly alkaline pH (about 11.2), with molecular weight 24 kDa and does not contain cysteine.
Galas
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Institute of Technical Biochemistry, Technical University, Lódź, Poland.
Kałuźewska
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D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002384:Catalysis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004549:Elastin / Q000378:metabolism; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007633:Keratins / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D011480:Protease Inhibitors / Q000494:pharmacology; D011489:Protein Denaturation; D012697:Serine Endopeptidases / Q000737:chemistry*; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity
D000596:Amino Acids; D010455:Peptides; D011480:Protease Inhibitors; D007633:Keratins; D004549:Elastin; D012697:Serine Endopeptidases