Cyclomaltodextrin glucanotransferase
| cyclomaltodextrin glucanotransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.4.1.19 | ||||||||
| CAS number | 9030-09-5 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, a cyclomaltodextrin glucanotransferase (EC 2.4.1.19) is an enzyme that catalyzes the chemical reaction of cyclizing part of a 1,4-alpha-D-glucan molecule through the formation of a 1,4-alpha-D-glucosidic bond.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is 1,4-alpha-D-glucan 4-alpha-D-(1,4-alpha-D-glucano)-transferase (cyclizing). Other names in common use include Bacillus macerans amylase, cyclodextrin glucanotransferase, alpha-cyclodextrin glucanotransferase, alpha-cyclodextrin glycosyltransferase, beta-cyclodextrin glucanotransferase, beta-cyclodextrin glycosyltransferase, gamma-cyclodextrin glycosyltransferase, cyclodextrin glycosyltransferase, cyclomaltodextrin glucotransferase, cyclomaltodextrin glycosyltransferase, konchizaimu, alpha-1,4-glucan 4-glycosyltransferase, cyclizing, BMA, CGTase, and neutral-cyclodextrin glycosyltransferase.
Structural studies
As of late 2007, 47 structures have been solved for this class of enzymes, with PDB accession codes 1A47, 1CDG, 1CGT, 1CGU, 1CGV, 1CGW, 1CGX, 1CGY, 1CIU, 1CXE, 1CXF, 1CXH, 1CXI, 1CXK, 1CXL, 1CYG, 1D3C, 1D7F, 1DED, 1DTU, 1EO5, 1EO7, 1I75, 1KCK, 1KCL, 1OT1, 1OT2, 1PAM, 1PEZ, 1PJ9, 1TCM, 1UKQ, 1UKS, 1UKT, 1V3J, 1V3K, 1V3L, 1V3M, 2CXG, 2DIJ, 3CGT, 4CGT, 5CGT, 6CGT, 7CGT, 8CGT, and 9CGT.
References
- DePinto JA, Campbell LL (1968). "Purification and properties of the amylase of Bacillus macerans". Biochemistry. 7 (1): 114–20. doi:10.1021/bi00841a015. PMID 5758537.
- Wild GM; Levine, Melvin L.; Norberg, Ethelda; Nordin, Philip; Pazur, John H.; Wild, Gene M. (1954). "Studies on the Schardinger dextrins. VII. Co-substrate specificity in coupling reactions of Macerans amylase". J. Am. Chem. Soc. 76 (9): 2387–2390. doi:10.1021/ja01638a027.
- Hehre EJ (1951). "Enzymic synthesis of polysaccharides: a biological type of polymerization". Adv. Enzymol. Relat. Subj. Biochem. 11: 297–337. doi:10.1002/9780470122563.ch6.
- SCHWIMMER S (1953). "Evidence for the purity of Schardinger dextrinogenase". Arch. Biochem. Biophys. 43 (1): 108–17. doi:10.1016/0003-9861(53)90089-7. PMID 13031665.