| Fructan β-fructosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.1.80 | ||||||||
| CAS no. | 37288-56-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Fructan β-fructosidase ( EC 3.2.1.80, exo-β-D-fructosidase, exo-β-fructosidase, polysaccharide β-fructofuranosidase, fructan exohydrolase) is an enzyme with systematic name β-D-fructan fructohydrolase. [1] [2] It catalyses the hydrolysis of terminal, non-reducing (2→1)- and (2→6)-linked β-D-fructofuranose residues in fructans.
It hydrolyses inulin and levan, and also sucrose.
- ^ DaCosta T, Gibbons RJ (June 1968). "Hydrolysis of levan by human plaque streptococci". Archives of Oral Biology. 13 (6): 609–17. doi: 10.1016/0003-9969(68)90139-8. PMID 5244285.
- ^ Jacques NJ, Morrey-Jones JG, Walker GJ (July 1985). "Inducible and constitutive formation of fructanase in batch and continuous cultures of Streptococcus mutans". Journal of General Microbiology. 131 (7): 1625–33. doi: 10.1099/00221287-131-7-1625. PMID 4045423.
- Fructan+beta-fructosidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
 | This enzyme-related article is a stub. You can help Wikipedia by expanding it. |
| Fructan β-fructosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.1.80 | ||||||||
| CAS no. | 37288-56-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Fructan β-fructosidase ( EC 3.2.1.80, exo-β-D-fructosidase, exo-β-fructosidase, polysaccharide β-fructofuranosidase, fructan exohydrolase) is an enzyme with systematic name β-D-fructan fructohydrolase. [1] [2] It catalyses the hydrolysis of terminal, non-reducing (2→1)- and (2→6)-linked β-D-fructofuranose residues in fructans.
It hydrolyses inulin and levan, and also sucrose.
- ^ DaCosta T, Gibbons RJ (June 1968). "Hydrolysis of levan by human plaque streptococci". Archives of Oral Biology. 13 (6): 609–17. doi: 10.1016/0003-9969(68)90139-8. PMID 5244285.
- ^ Jacques NJ, Morrey-Jones JG, Walker GJ (July 1985). "Inducible and constitutive formation of fructanase in batch and continuous cultures of Streptococcus mutans". Journal of General Microbiology. 131 (7): 1625–33. doi: 10.1099/00221287-131-7-1625. PMID 4045423.
- Fructan+beta-fructosidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
|
| This enzyme-related article is a stub. You can help Wikipedia by expanding it. |