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Arginine 115 in the subsite F of human lysozyme (peptidoglycan N-acetylmuramoylhydrolase, EC 3.2.1.17) was replaced with lysine, histidine, glutamine or glutamine acid by site-directed mutagenesis. The conversions which conserve positive charge, Arg115 to Lys or His (at acidic pH), have little affected on either the kinetic parameters for Micrococcus lysodeikticus cells or the activity against glycol chitin, nor on the cleavage patterns of hexa(N-acetylglucosamine) [(GlcNAc)6] and penta(N-acetylglucosamine) [(GlcNAc)5]. On the other hand, the conversions which cause loss of the positive charge, Arg115 to His (neutral and alkaline pH), Gln or Glu, not only reduced the activity against glycol chitin but also changed the cleavage patterns for (GlcNAc)6 and (GlcNAc)5. These results suggest that Arg115 is structurally required not for the specific hydrogen bonding interaction with a sugar residue but for the positively charged character in the construction of subsite F in human lysozyme.
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