Abstract
Hyaluronate lyase produced by group B streptococci (GBS) degrades hyaluronan completely to unsaturated disaccharide units and also cleaves unsulfated regions of chondroitin sulfate. The enzyme is rapidly inactivated by diethyl pyrocarbonate and enzymatic activity is restored by treatment with hydroxylamine, suggesting that a histidine residue is present in the active site. Amino acid sequence comparisons of GBS hyaluronate lyase and four other related enzymes revealed that one of the 16 histidine residues of the enzyme (His-479) is present in a highly conserved region. Conversion of His-479 to a glycine by site-directed mutagenesis resulted in a complete loss of enzymatic activity of the modified protein. We propose that His-479 is in the active site of GBS hyaluronate lyase and participates in the initial abstraction of hydrogen ions from the glucuronic acid residues of hyaluronan.
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