4-alpha-glucanotransferase
| 4-alpha-glucanotransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.25 | ||||||||
| CAS no. | 9032-09-1 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a 4-alpha-glucanotransferase (EC 2.4.1.25) is an enzyme that catalyzes a chemical reaction that transfers a segment of a 1,4-alpha-D-glucan to a new position in an acceptor carbohydrate, which may be glucose or a 1,4-alpha-D-glucan.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase. Other names in common use include disproportionating enzyme, dextrin glycosyltransferase, D-enzyme, debranching enzyme maltodextrin glycosyltransferase, amylomaltase, and dextrin transglycosylase. This enzyme participates in starch and sucrose metabolism in plants.[1][2] Studies of the enzyme from potato led to the discovery of cycloamylose.[3]
Structural studies
As of late 2007, 14 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1CWY, PDB: 1ESW, PDB: 1FP8, PDB: 1FP9, PDB: 1K1W, PDB: 1K1X, PDB: 1K1Y, PDB: 1LWH, PDB: 1LWJ, PDB: 1TZ7, PDB: 1X1N, PDB: 2OWC, PDB: 2OWW, and PDB: 2OWX.
References
- ↑ Critchley, Joanna H.; Zeeman, Samuel C.; Takaha, Takeshi; Smith, Alison M.; Smith, Steven M. (2001-04-01). "A critical role for disproportionating enzyme in starch breakdown is revealed by a knock-out mutation in Arabidopsis". The Plant Journal. 26 (1): 89–100. doi:10.1046/j.1365-313x.2001.01012.x. ISSN 1365-313X. PMID 11359613.
- ↑ Chia, Tansy; Thorneycroft, David; Chapple, Andrew; Messerli, Gaëlle; Chen, Jychian; Zeeman, Samuel C.; Smith, Steven M.; Smith, Alison M. (2004-03-01). "A cytosolic glucosyltransferase is required for conversion of starch to sucrose in Arabidopsis leaves at night". The Plant Journal. 37 (6): 853–863. doi:10.1111/j.1365-313X.2003.02012.x. ISSN 1365-313X. PMID 14996213.
- ↑ Takaha, Takeshi; Yanase, Michiyo; Takata, Hiroki; Okada, Shigetaka; Smith, Steven M. (1996-02-09). "Potato D-enzyme Catalyzes the Cyclization of Amylose to Produce Cycloamylose, a Novel Cyclic Glucan". Journal of Biological Chemistry. 271 (6): 2902–2908. doi:10.1074/jbc.271.6.2902. ISSN 0021-9258. PMID 8621678.
- Hehre EJ (1951). "Enzymic Synthesis of Polysaccharides: A Biological type of Polymerization". Advances in Enzymology and Related Areas of Molecular Biology. Vol. 11. pp. 297–337. doi:10.1002/9780470122563.ch6. ISBN 978-0-470-12256-3. PMID 24540594.
{{cite book}}: ISBN / Date incompatibility (help) - Lukomskaya, I. S. (1959). "Синтез oligosaccharides с alpha-1,6-bonds приготовлениями фермента от печени и мускула" [Synthesis of oligosaccharides with alpha-1,6-bonds by enzyme preparations from liver and muscle]. Doklady Akademii Nauk SSSR (in Russian). 129: 1172–1175.
- Pazur JH, Okada S (1968). "The isolation and mode of action of a bacterial glucanosyltransferase". J. Biol. Chem. 243 (18): 4732–8. doi:10.1016/S0021-9258(18)93179-0. PMID 4972097.
- Walker GJ, Whelan WJ (1959). "Synthesis of amylose by potato D-enzyme". Nature. 183 (4653): 46. Bibcode:1959Natur.183...46W. doi:10.1038/183046a0. PMID 13622683. S2CID 4289861.
- Whelan WH (1971). "Enzymic explorations of the structures of starch and glycogen". Biochem. J. 122 (5): 609–622. doi:10.1042/bj1220609. PMC 1176828. PMID 5001952.