Glycoside hydrolase family 13

Alpha amylase, N-terminal ig-like domain
crystal structure of thermoactinomyces vulgaris r-47 alpha-amylase 1 (tvai) mutant d356n/e396q complexed with p2, a pullulan model oligosaccharide
Identifiers
Symbol	Alpha-amylase_N
Pfam	PF02903
InterPro	IPR004185
SCOP2	1sma / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Alpha-amylase catalytic domain
cyclodextrin glucanotransferase (e.c.2.4.1.19) (cgtase)
Identifiers
Symbol	Alpha-amylase
Pfam	PF00128
Pfam clan	CL0058
InterPro	IPR006047
SCOP2	1ppi / SCOPe / SUPFAM
CAZy	GH13
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In molecular biology, glycoside hydrolase family 13 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]}

Enzymes containing this domain belong to family 13 (CAZY GH_13) of the glycosyl hydrolases. The maltogenic alpha-amylase is an enzyme which catalyses hydrolysis of (1-4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains in the conversion of starch to maltose. Other enzymes in this family include neopullulanase, which hydrolyses pullulan to panose, and cyclomaltodextrinase, which hydrolyses cyclodextrins.

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 13". 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.