Kinetic analysis of papaya proteinase omega |
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Authors: | IG Sumner A Vaughan R Eisenthal RW Pickersgill AJ Owen PW Goodenough |
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Affiliation: | Protein Engineering Department, AFRC Institute of Food Research, Reading Laboratory, Reading, UK. |
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Abstract: | Papaya proteinase omega (pp omega) has been purified from dried latex both by immunoaffinity and traditional methods. Kinetic analysis revealed that (1), the pp omega-catalysed hydrolysis of N-benzoyl-L-arginine p-nitroanilide (BApNA) has a lower specificity (kcat/Km) than the same reaction catalysed by papain; (2), the pp omega-catalysed hydrolysis of a tripeptide substrate having phenylalanine at the second position (S2-site) showed a more similar specificity to that catalysed by papain; (3), the significant difference between the two enzymes is that steady state kinetics with both L-BApNA and a tripeptide enables the identification in pp omega of other ionizations affecting binding. The active sites of papain and pp omega can therefore be distinguished by pH-dependence of kcat/Km. |
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