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Glycoside hydrolase family 42

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Beta-galactosidase
crystal structure of thermus thermophilus a4 beta-galactosidase
Identifiers
SymbolGlyco_hydro_42
PfamPF02449
Pfam clanCL0058
InterProIPR013529
SCOP21kwg / SCOPe / SUPFAM
CAZyGH42
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Beta-galactosidase trimerisation domain
crystal structure of thermus thermophilus a4 beta-galactosidase
Identifiers
SymbolGlyco_hydro_42M
PfamPF08532
Pfam clanCL0014
InterProIPR013738
SCOP21kwg / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Beta-galactosidase C-terminal domain
crystal structure of thermus thermophilus a4 beta-galactosidase
Identifiers
SymbolGlyco_hydro_42C
PfamPF08533
Pfam clanCL0369
InterProIPR013739
SCOP21kwg / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In molecular biology, glycoside hydrolase family 42 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]

The glycosyl hydrolase 42 family CAZY GH_42 comprises beta-galactosidase enzymes (EC 3.2.1.23). These enzyme catalyse the hydrolysis of terminal, non-reducing terminal beta-D-galactoside residues. The middle domain of these three-domain enzymes is involved in trimerisation.[8]

References

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  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. Bibcode:1995PNAS...92.7090H. 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): 695–6. doi:10.1042/bj3160695. 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. PMC 3965031. PMID 24270786.
  6. ^ "Glycoside Hydrolase Family 42". CAZypedia.org. Retrieved 2018-03-06.
  7. ^ CAZypedia Consortium (December 2018). "Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes" (PDF). Glycobiology. 28 (1): 3–8. doi:10.1093/glycob/cwx089. PMID 29040563.
  8. ^ Shimizu T, Kobayashi T, Ba-Thein W, Ohtani K, Hayashi H (1995). "Sequence analysis of flanking regions of the pfoA gene of Clostridium perfringens: beta-galactosidase gene (pbg) is located in the 3'-flanking region". Microbiology and Immunology. 39 (9): 677–86. doi:10.1111/j.1348-0421.1995.tb03256.x. PMID 8577281. S2CID 2650178.
This article incorporates text from the public domain Pfam and InterPro: IPR013529
This article incorporates text from the public domain Pfam and InterPro: IPR013739
This article incorporates text from the public domain Pfam and InterPro: IPR013738