Unusual structural features of the bacteriophage-associated hyaluronate lyase (hylp2)

The Journal of Biological Chemistry
Parul MishraVinod Bhakuni

Abstract

Hyaluronate lyases are a class of endoglycosaminidase enzymes, which are of considerable complexity and heterogeneity. Their primary function is to degrade hyaluronan and certain other glycosaminoglycans and facilitate the spread of disease. Among hyaluronate lyases, the bacteriophage-associated enzymes are unique as they have the lowest molecular mass, very low amino acid sequence homology with bacterial hyaluronate lyases, and exhibit absolute specificity for one type of glycosaminoglycan, i.e. hyaluronan. Despite such unique characteristics significant details on structural features of these lyases are not available. The Streptococcus pyogenes bacteriophage 10403 contains a gene, hylP2, which encodes for hyaluronate lyase (HylP2) in this organism. HylP2 was cloned, overexpressed, and purified to homogeneity. The recombinant HylP2 exists as a homotrimer of molecular mass about 110 kDa, under physiological conditions. Limited proteolysis and guanidine hydrochloride denaturation studies demonstrated that the N-terminal region of the protein is flexible, whereas the C-terminal portion has a compact conformation. The enzyme shows sequential unfolding, with the N-terminal unfolding first followed by the simultaneous unfolding and ...Continue Reading

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Citations

Jun 1, 2013·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Abdul Hamid KhanNasrullah Bangulzai
Jan 12, 2013·Current Protein & Peptide Science·Zuzanna Drulis-KawaRob Lavigne
Mar 25, 2017·Applied Microbiology and Biotechnology·Agnieszka LatkaZuzanna Drulis-Kawa
Oct 14, 2008·The Journal of Biological Chemistry·Parul Mishra, Vinod Bhakuni

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