Lysozyme-catalysed hydrolysis of some beta-aryl di-N-acetylchitobiosides.
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ABSTRACT: 1. Four beta-aryl di-N-acetylchitobiosides and beta-S-phenyl di-N-acetylthiochitobioside have been prepared and shown to be substrates for hen's-egg-white lysozyme. 2. The lysozyme-catalysed hydrolysis of these substrates obeys Michaelis-Menten kinetics. 3. The Michaelis constants, K(m), for the beta-aryl di-N-acetyl-chitobiosides are almost independent of the aglycone, whereas the catalytic constants, k(cat.), show a marked dependence, giving a Hammett reaction constant, rho, equal to 1.2; this suggests the rate-determining step involves concerted acid-base or acid-nucleophilic catalysis. 4. This conclusion is supported by the Michaelis-Menten constants found for beta-S-phenyl di-N-acetylthiochitobioside. 5. A three-step reaction pathway is proposed, and mechanisms are suggested that would account for the evidence currently available.
SUBMITTER: Lowe G
PROVIDER: S-EPMC1271230 | biostudies-other | 1967 Sep
REPOSITORIES: biostudies-other
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