In vitro mutagenesis of PH-20 hyaluronidase from human sperm.

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Arming S, Strobl B, Wechselberger C, Kreil G

In vitro mutagenesis of PH-20 hyaluronidase from human sperm.

Eur J Biochem. 1997 Aug 1;247(3):810-4.

PubMed ID

9288901 [ View in PubMed

]

Abstract

The cDNA encoding PH-20 hyaluronidase from human sperm has been mutated at five positions by in vitro mutagenesis. We have changed three acidic amino acids and two arginine residues that are conserved in the sequence of mammalian PH-20 polypeptides as well as in the hyaluronidases from bee and hornet venom. Of the former, the mutants [Gln113]PH-20 and [Gln249]PH-20 had no detectable enzymatic activity; the mutant [Asn111]PH-20 had about 3% activity. The mutant [Thr252]PH-20 was also inactive, while [Gly176]PH-20 had only about 1% activity. This indicates that the PH-20 hyaluronidases, like numerous enzymes that hydrolyze glycosidic bonds, have acidic amino acids in their active site. Moreover, for the binding of the substrate, the polyanion hyaluronan, arginine residues appear to be essential.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Hyaluronic acid	Hyaluronan and proteoglycan link protein 1	Protein	Humans	Unknown	Binder	Details

Polypeptides

Name	UniProt ID
Hyaluronidase PH-20	P38567	Details