| Glucan 1,6-α-isomaltosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.1.94 | ||||||||
| CAS no. | 56467-68-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Glucan 1,6-α-isomaltosidase (EC 3.2.1.94, exo-isomaltohydrolase, isomalto-dextranase, isomaltodextranase, G2-dextranase, 1,6-α-D-glucan isomaltohydrolase) is an enzyme with systematic name 6-α-D-glucan isomaltohydrolase.[1][2] It catalyses hydrolysis of (1→6)-β-D-glucosidic linkages in polysaccharides, to remove successive isomaltose units from the non-reducing ends of the chains
Optimum activity is on those 1,6-α-D-glucans containing 6, 7 and 8 glucose units.
References
- ↑ Sawai T, Toriyama K, Yano K (January 1974). "A bacterial dextranase releasing only isomaltose from dextrans". Journal of Biochemistry. 75 (1): 105–12. PMID 4826536.
- ↑ Sawai T, Niwa Y (1975). "Transisomaltosylation activity of a bacterial isomaltodextranase". Agric. Biol. Chem. 39: 1077–1083. doi:10.1271/bbb1961.39.1077.
External links
- Glucan+1,6-alpha-isomaltosidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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