Amylosucrase
| amylosucrase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.4.1.4 | ||||||||
| CAS number | 9032-11-5 | ||||||||
| 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 amylosucrase (EC 2.4.1.4) is an enzyme that catalyzes the chemical reaction
- sucrose + (1,4-alpha-D-glucosyl)n D-fructose + (1,4-alpha-D-glucosyl)n+1
Thus, the two substrates of this enzyme are sucrose and (1,4-alpha-D-glucosyl)n, whereas its two products are D-fructose and (1,4-alpha-D-glucosyl)n+1.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is sucrose:1,4-alpha-D-glucan 4-alpha-D-glucosyltransferase. Other names in common use include sucrose-glucan glucosyltransferase, and sucrose-1,4-alpha-glucan glucosyltransferase. This enzyme participates in starch and sucrose metabolism.
Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1G5A, 1JG9, 1JGI, 1MVY, 1MW0, 1MW1, 1MW2, 1MW3, 1S46, and 1ZS2.
References
- AVIGAD G, FEINGOLD DS, HESTRIN S (1957). "Enzymatic synthesis and reactions of a sucrose isomer alpha-D-galactopyranosyl-beta-D-fructofuranoside". J. Biol. Chem. 224 (1): 295&ndash, 307. PMID 13398406.
- Hehre EJ (1951). "Enzymic synthesis of polysaccharides: a biological type of polymerization". Adv. Enzymol. Relat. Subj. Biochem. Advances in Enzymology - and Related Areas of Molecular Biology. 11: 297&ndash, 337. doi:10.1002/9780470122563.ch6. ISBN 978-0-470-12256-3.
- Hehre EJ, Hamilton DM & Carlson AS (1949). "Synthesis of a polsaccharide of the starch glycogen class from sucrose by a cell-free, bacterial enzyme system (amylosucrase)". J. Biol. Chem. 177: 267&ndash, 279.