Inulin fructotransferase (DFA-III-forming)
| Inulin fructotransferase (DFA-III-forming) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.2.2.18 | ||||||||
| CAS number | 50936-42-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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In enzymology, an inulin fructotransferase (DFA-III-forming) (EC 4.2.2.18) is an enzyme that catalyzes the chemical reaction
- Produces alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride (DFA III) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is 2,1-beta-D-fructan lyase (alpha-D-fructofuranose-beta-D-fructofuranose-1,2':2,3'-dianhydride- forming). Other names in common use include inulin fructotransferase (DFA-III-producing), inulin fructotransferase (depolymerizing), inulase II, inulinase II, inulin fructotransferase (depolymerizing,, difructofuranose-1,2':2,3'-dianhydride-forming), inulin D-fructosyl-D-fructosyltransferase, (1,2':2,3'-dianhydride-forming), inulin D-fructosyl-D-fructosyltransferase (forming, and alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride).
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2INU and 2INV.
References
- Uchiyama T (1975). "Action of Arthrobacter ureafaciens inulinase II on several oligofructans and bacterial levans". Biochim. Biophys. Acta. 397 (1): 153–63. doi:10.1016/0005-2744(75)90189-8. PMID 1148257.
- Uchiyama T; Niwa S; Tanaka K (1973). "Purification and properties of Arthrobacter ureafaciens inulase II". Biochim. Biophys. Acta. 315: 412–420. doi:10.1016/0005-2744(73)90271-4.