http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID99883
Outgoing Links
| Predicate | Object |
|---|---|
| abstract | Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. |
| title | CBM20_alpha_amylase |
| isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/32048009 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7209292 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/22601033 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/23417590 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8468868 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/6496778 |
| type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
| Predicate | Subject |
|---|---|
| has component | http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCD8Q9M3 |
Total number of triples: 10.