Purification and catalytic properties of lysozyme

Two side-chains. Asp 32 and Glu 35 are directly involved in the hydrolysis (Phillips, 1966). The carboxyl group of Glu 35, which is non-ionized and is located about 0.3 nm from the glucosidic oxygen atom between C-1 of NAM and C-4 of NAG, donates a proton to this oxygen and produces a C-l-OH in NAM and a 

Michaelis-Menten equations often do not apply for enzymatic reactions at surfaces, such as bacterial walls (McLaren and Packer, 1970). Precise kinetic parameters, which can only be obtained with well-characterized low molecular weight substrates, are complicated by non-productive binding of small substrates, i.e. binding outside of the catalytic site. 

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