Glycoside hydrolase family 42

Beta-galactosidase
crystal structure of thermus thermophilus a4 beta-galactosidase
Identifiers
Symbol	Glyco_hydro_42
Pfam	PF02449
Pfam clan	CL0058
InterPro	IPR013529
SCOP2	1kwg / SCOPe / SUPFAM
CAZy	GH42
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Beta-galactosidase trimerisation domain
crystal structure of thermus thermophilus a4 beta-galactosidase
Identifiers
Symbol	Glyco_hydro_42M
Pfam	PF08532
Pfam clan	CL0014
InterPro	IPR013738
SCOP2	1kwg / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Beta-galactosidase C-terminal domain
crystal structure of thermus thermophilus a4 beta-galactosidase
Identifiers
Symbol	Glyco_hydro_42C
Pfam	PF08533
Pfam clan	CL0369
InterPro	IPR013739
SCOP2	1kwg / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure 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

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