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ABSTRACT:
SUBMITTER: Reitinger S
PROVIDER: S-EPMC2740539 | biostudies-literature | 2009 Jul
REPOSITORIES: biostudies-literature
Reitinger Stephan S Müllegger Johannes J Greiderer Brigitte B Nielsen Jens Erik JE Lepperdinger Günter G
The Journal of biological chemistry 20090528 29
Hyaluronidases from diverse species and sources have different pH optima. Distinct mechanisms with regard to dynamic structural changes, which control hyaluronidase activity at varying pH, are unknown. Human serum hyaluronidase 1 (HYAL1) is active solely below pH 5.1. Here we report the design of a HYAL1 variant that degrades hyaluronan up to pH 5.9. Besides highly conserved residues in close proximity of the active site of most hyaluronidases, we identified a bulky loop formation located at the ...[more]