The Enzyme Database

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EC 2.4.1.19     
Accepted name: cyclomaltodextrin glucanotransferase
Reaction: Cyclizes part of a (1→4)-α-D-glucan chain by formation of a (1→4)-α-D-glucosidic bond
For diagram of glycoprotein biosynthesis, click here
Other name(s): Bacillus macerans amylase; cyclodextrin glucanotransferase; α-cyclodextrin glucanotransferase; α-cyclodextrin glycosyltransferase; β-cyclodextrin glucanotransferase; β-cyclodextrin glycosyltransferase; γ-cyclodextrin glycosyltransferase; cyclodextrin glycosyltransferase; cyclomaltodextrin glucotransferase; cyclomaltodextrin glycosyltransferase; konchizaimu; α-1,4-glucan 4-glycosyltransferase, cyclizing; BMA; CGTase; neutral-cyclodextrin glycosyltransferase; 1,4-α-D-glucan 4-α-D-(1,4-α-D-glucano)-transferase (cyclizing)
Systematic name: (1→4)-α-D-glucan:(1→4)-α-D-glucan 4-α-D-[(1→4)-α-D-glucano]-transferase (cyclizing)
Comments: Cyclomaltodextrins (Schardinger dextrins) of various sizes (6,7,8, etc. glucose units) are formed reversibly from starch and similar substrates. Will also disproportionate linear maltodextrins without cyclizing (cf. EC 2.4.1.25, 4-α-glucanotransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-09-5
References:
1.  DePinto, J.A. and Campbell, L.L. Purification and properties of the amylase of Bacillus macerans. Biochemistry 7 (1968) 114–120. [PMID: 5758537]
2.  French, D., Levine, M.L., Norberg, E., Norden, P., Pazur, J.H. and Wild, G.M. Studies on the Schardinger dextrins. VII. Co-substrate specificity in coupling reactions of Macerans amylase. J. Am. Chem. Soc. 76 (1954) 2387–2390.
3.  Hehre, E.J. Enzymic synthesis of polysaccharides: a biological type of polymerization. Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 297–337. [PMID: 24540594]
4.  Schwimmer, S. Evidence for the purity of Schardinger dextrinogenase. Arch. Biochem. Biophys. 43 (1953) 108–117. [DOI] [PMID: 13031665]
[EC 2.4.1.19 created 1961]
 
 


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