Glycoside hydrolase family 56

Hyaluronidase
crystal structure of bee venom hyaluronidase in complex with hyaluronic acid tetramer
Identifiers
Symbol Glyco_hydro_56
Pfam PF01630
Pfam clan CL0058
InterPro IPR018155
SCOP 1fcv
SUPERFAMILY 1fcv
OPM superfamily 117
OPM protein 1fcq
CAZy GH56
Membranome 1078

In molecular biology, glycoside hydrolase family 56 is a family of glycoside hydrolases.

Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families.[1][2][3] This classification is available on the CAZy web site,[4][5] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[6][7]

Glycoside hydrolase family 56 CAZY GH_56 includes enzymes with hyaluronidase EC 3.2.1.35 activity. The venom of Apis mellifera (Honeybee) contains several biologically-active peptides and two enzymes, one of which is a hyaluronidase.[8] The amino acid sequence of bee venom hyaluronidase contains 349 amino acids, and includes four cysteines and a number of potential glycosylation sites.[8] The sequence shows a high degree of similarity to PH-20, a membrane protein of mammalian sperm involved in sperm-egg adhesion, supporting the view that hyaluronidases play a role in fertilisation.[8]

PH-20 is required for sperm adhesion to the egg zona pellucida; it is located on both the sperm plasma membrane and acrosomal membrane.[9] The amino acid sequence of the mature protein contains 468 amino acids, and includes six potential N-linked glycosylation sites and twelve cysteines, eight of which are tightly clustered near the C-terminus.[9]

References

  1. ↑ Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G (July 1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proceedings of the National Academy of Sciences of the United States of America. 92 (15): 7090–4. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375.
  2. ↑ Davies G, Henrissat B (September 1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–9. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
  3. ↑ Henrissat B, Bairoch A (June 1996). "Updating the sequence-based classification of glycosyl hydrolases". The Biochemical Journal. 316 ( Pt 2) (Pt 2): 695–6. PMC 1217404. PMID 8687420.
  4. ↑ "Home". CAZy.org. Retrieved 2018-03-06.
  5. ↑ Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, Henrissat B (January 2014). "The carbohydrate-active enzymes database (CAZy) in 2013". Nucleic Acids Research. 42 (Database issue): D490–5. doi:10.1093/nar/gkt1178. PMID 24270786.
  6. ↑ "Glycoside Hydrolase Family 56". CAZypedia.org. Retrieved 2018-03-06.
  7. ↑ "Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes". Glycobiology. 28 (1): 3–8. December 2018. doi:10.1093/glycob/cwx089. PMID 29040563.
  8. 1 2 3 Gmachl M, Kreil G (1993). "Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm". Proc. Natl. Acad. Sci. U.S.A. 90 (8): 3569–3573. doi:10.1073/pnas.90.8.3569. PMC 46342. PMID 7682712.
  9. 1 2 Lathrop WF, Carmichael EP, Myles DG, Primakoff P (1990). "cDNA cloning reveals the molecular structure of a sperm surface protein, PH-20, involved in sperm-egg adhesion and the wide distribution of its gene among mammals". J. Cell Biol. 111 (6): 2939–2949. doi:10.1083/jcb.111.6.2939. PMC 2116349. PMID 2269661.
This article incorporates text from the public domain Pfam and InterPro: IPR018155
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