ArticleThe Journal of biological chemistry2009
Designed human serum hyaluronidase 1 variant, HYAL1DeltaL, exhibits activity up to pH 5.9.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Photoacid Generators for Biomedical Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Review
- Substitution of acidic residues near the catalytic Glu131 leads to human HYAL1 activity at neutral pH via charge-charge interactions.PloS one · 2024Article
- Photoreactive-proton-generating hyaluronidase/albumin nanoparticles-loaded PEG-hydrogel enhances antitumor efficacy and disruption of the hyaluronic acid extracellular matrix in AsPC-1 tumors.Materials today. Bio · 2021Article
- Hyaluronan digestion controls DC migration from the skin.The Journal of clinical investigation · 2014Article
- Emerging roles for hyaluronidase in cancer metastasis and therapy.Advances in cancer research · 2014Review
- Unbinding of hyaluronan accelerates the enzymatic activity of bee hyaluronidase.The Journal of biological chemistry · 2011Article
- Proteoglycomics: recent progress and future challenges.Omics : a journal of integrative biology · 2010Review
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Authors and funding
5 authors.
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Abstract
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 end of the substrate binding crevice of HYAL1 to be crucial for substrate hydrolysis. The stretch between cysteine residues 207 and 221, which normally contains 13 amino acids, could be replaced by a tetrapeptide sequence of alternating glycine serine residues, thereby yielding an active enzyme with an extended binding cleft. This variant exhibited hyaluronan degradation at elevated pH. This is indicative for appropriate substrate binding and proper positioning being decisively affected by sites far off from the active center.
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