Yongyuth YuthavongWichai SuttimoolMahidol University2018-06-012018-06-011978-03-14BBA - Enzymology. Vol.523, No.1 (1978), 198-206000527442-s2.0-0017837080https://repository.li.mahidol.ac.th/handle/20.500.14594/13103Rate constants for acylation of papain (EC 3.4.22.2) by specific substrates and its subsequent deacylation are derived from kinetic analysis of the reactions in the presence of aminoacetonitrile and methanol. Methyl and ethyl hippurate and methyl N-benzyloxycarbonylglycinate have marginally higher values of rate constants for acylation than for deacylation, while the reverse is true for ethyl N-benzoyl-l-arginate. Both acylation and deacylation are rate-determinating for these substrates, while only deacylation is rate-determining for methyl-N-acetyl-l-phenylalanylglycinate. Deacylation is the only rate-determining step for p-nitrophenyl esters of hippuric acid, N-benzyloxycarbonylglycine and N-acetyl-l-phenylalanylglycine. These results are discussed in relation to those from inactivation of the enzyme by alkylating agent in the presence of substrate. © 1978.Mahidol UniversityMedicineArticleSCOPUS10.1016/0005-2744(78)90022-0