Isomaltulose synthase
| isomaltulose synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.4.99.11 | ||||||||
| CAS no. | 159940-49-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, an isomaltulose synthase (EC 5.4.99.11) is an enzyme that catalyzes the chemical reaction
- sucrose 6-O-Alpha-D-Glucopyranosyl-D-Fructofuranose
Hence, this enzyme has one substrate, sucrose (table sugar), and one product, 6-O-Alpha-D-Glucopyranosyl-D-Fructofuranose (also known as isomaltulose or Palatinose). It converts the α-1,2 glycosidic linkage between glucose and fructose in sucrose into the α-1,6 glycosidic linkage between glucose and fructose in isomaltulose.
This enzyme belongs to the family of isomerases. The systematic name of this enzyme class is sucrose glucosylmutase. Other names in common use include sucrose isomerase, sucrose alpha-glucosyltransferase, and trehalulose synthase.
The isomaltulose synthase of the bacterium Protaminobacter rubrum is commonly used in the industrial production of isomaltulose.[1]
Structural studies
[edit]As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1M53, 1ZJA, 1ZJB, 2PWD, 2PWE, 2PWF, and 2PWG.
References
[edit]- ^ Ravaud, Stéphanie; Watzlawick, Hildegard; Haser, Richard; Mattes, Ralf; Aghajari, Nushin (2006-01-01). "Overexpression, purification, crystallization and preliminary diffraction studies of the Protaminobacter rubrum sucrose isomerase SmuA". Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 62 (Pt 1): 74–76. doi:10.1107/S1744309105041758. PMC 2150920. PMID 16511267.
- Cheetham PS (1984). "The extraction and mechanism of a novel isomaltulose-synthesizing enzyme from Erwinia rhapontici". Biochem. J. 220 (1): 213–20. doi:10.1042/bj2200213. PMC 1153612. PMID 6743261.
- Cheetham PS, Imber CE, Isherwood J (1982). "The formation of isomaltulose by immobilized Erwinia rhapontici". Nature. 299 (5884): 628–631. Bibcode:1982Natur.299..628C. doi:10.1038/299628a0. S2CID 4355243.
