Cyclomaltodextrin glucanotransferase

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cyclomaltodextrin glucanotransferase
Identifiers
EC number2.4.1.19
CAS number9030-09-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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[edit]

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[edit]

  • 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 G.M.; 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. Advances in Enzymology - and Related Areas of Molecular Biology. 11. pp. 297–337. doi:10.1002/9780470122563.ch6. ISBN 9780470122563. PMID 24540594.
  • 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.