Structure and cleavage pattern of a hyaluronate 3-glycanohydrolase in the glycoside hydrolase 79 family.
GH79 family
Glycosaminoglycan
Hyaluronidase
Hydrolysis pattern
Leech
Journal
Carbohydrate polymers
ISSN: 1879-1344
Titre abrégé: Carbohydr Polym
Pays: England
ID NLM: 8307156
Informations de publication
Date de publication:
01 Feb 2022
01 Feb 2022
Historique:
received:
09
08
2021
revised:
08
10
2021
accepted:
29
10
2021
entrez:
11
12
2021
pubmed:
12
12
2021
medline:
17
3
2022
Statut:
ppublish
Résumé
Hyaluronidases have attracted a great deal of interest in the field of medicine due to their fundamental roles in the breakdown of hyaluronan. However, little is known about the catalytic mechanism of the hyaluronate 3-glycanohydrolases. Here, we report the crystal structure and cleavage pattern of a leech hyaluronidase (LHyal), which hydrolyzes the β-1,3-glycosidic bonds of hyaluronan. LHyal exhibits the typical structural features of glycoside hydrolase 79 family but contains a variable 'exo-pocket' loop where basic residues R102 and K103 are the structural determinants of hyaluronan binding. Through analysis of the hydrolysis of even- and odd-numbered hyaluronan oligosaccharides, we demonstrate that hexasaccharide is the shortest natural substrate, which can be cleaved from both the reducing and non-reducing ends to release disaccharides, and pentasaccharides are the smallest fragments for recognition and hydrolysis. These observations provide new insights into the degradation of hyaluronan and the evolutionary relationships of the GH79 family enzymes.
Identifiants
pubmed: 34893255
pii: S0144-8617(21)01225-X
doi: 10.1016/j.carbpol.2021.118838
pii:
doi:
Substances chimiques
Hyaluronic Acid
9004-61-9
Hyaluronoglucosaminidase
EC 3.2.1.35
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
118838Informations de copyright
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