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2.4.1.18: 1,4-alpha-glucan branching enzyme

This is an abbreviated version!
For detailed information about 1,4-alpha-glucan branching enzyme, go to the full flat file.

Word Map on EC 2.4.1.18

Reaction

2 1,4-alpha-D-glucan =

alpha-1,4-D-glucan-alpha-1,6-(alpha-1,4-D-glucan)
+
H2O

Synonyms

(1-4)-alpha-D-glucan:(1-4)-alpha-D-glucan 6-alpha-D-[(1-4)-alpha-D-glucano]-transferase, 1,4-alpha-glucan branching enzyme, 1,4-alpha-glucan branching enzyme 1, AGBE, alpha-1,4->alpha-1,6-glycosyltransferase, alpha-1,4-glucan branching enzyme, alpha-1,4-glucan:alpha-1,4-glucan 6-glycosyltransferase, alpha-1,4-glucan:alpha-1,4-glucan-6-glycosyltransferase, alpha-glucan branching enzyme, alpha-glucan-branching glycosyltransferase, amylo-(1,4-1,6)-transglycosylase, amylo-(1,4->1,6)-transglycosylase, amylose isomerase, BBE, BE, BE-01, BE-02, BE-II, BE1, BE2, BE3, BEI, BEII, BEIIa, BEIIb, BGE, branching enzyme, branching factor, enzymatic, branching glycosyltransferase, ChlBE, Dg GBE, Dr GBE, enzyme Q, full-length starch branching enzyme II, GBE, GBE1, GBE1 enzyme, GH13 GBE, GH57-type glycogen branching enzyme, GlgB, glucan transferase, glucosan transglycosylase, glycogen branching enzyme, glycogen branching enzyme GBE1, glycosyltransferase, alpha-glucan-branching, HosBE, IbSBEI, mSBEIIa, ORF Rv1326c, PH1386, PhGBE, PvSBE1, PvSBE2, Q-enzyme, QE, rBEI, rice branching enzyme I, RMEBE, RoBE, SBE, SBE A, SBE B, SBE I, SBE IIa, SBE Iib, SBE-I, SBE1, SBEI, SBEII, SBEIIA, SBEIIB, ScoBE, SmGBE, starch branching enzyme, starch branching enzyme I, starch branching enzyme II, starch branching enzyme IIa, starch branching enzyme IIb, starch branching enzyme SBE I, starch branching enzyme SBE IIb, starch branching enzyme-I, starch-branching enzyme, starch-branching enzyme Ia, starch-branching enzyme IIa, starch-branching enzyme IIb, starch-branching enzymes IIa, starch-branching enzymes IIb, starch-branching-enzyme, TK1436, VsbeII

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.18 1,4-alpha-glucan branching enzyme

Crystallization

Crystallization on EC 2.4.1.18 - 1,4-alpha-glucan branching enzyme

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of truncated branching enzyme mutant DELTA112 in complex with linear oligosaccharides maltoheptaose and maltohexaose, X-ray diffraction structure determination and analysis
hanging drop method, active N-terminally truncated form missing the first 107 amino acids
-
crystal structure of full-length protein at 2.33 A resolution. The enzyme contains four domains: N1 beta-sandwich, N2 beta-sandwich, a central (beta/alpha)8 domain that houses the catalytic site, and a C-terminal beta-sandwich. The N1 beta-sandwich, which is formed by the first 105 amino acids and superimposes well with the N2 beta-sandwich, has an influence in substrate binding in the amylase assay
determination of the crystal structure of branching enzyme I at a resolution of 1.9 A by molecular replacement using the Escherichia coli glycogen branching enzyme as a search model. Branching enzyme I is roughly ellipsoidal in shape with two globular domains that form a prominent groove proposed to serve as the alphha-polyglucan-binding site. Amino acid residues Asp344 and Glu399, postulated to play an essential role in catalysis, are located at a central cleft in the groove
mutant E399Q in complex with maltopentaose at a resolution of 2.2 A. Maltopentaose binds to a hydrophobic pocket formed by the N-terminal helix, carbohydrate-binding module 48, and alpha-amylase domain. In addition, glucose moieties can be observed at molecular surfaces on the N-terminal helix alpha2 and carbohydrate-binding module 48
sitting drop method, 20°C
sitting-drop vapor-diffusion method, pH 9.3, crystals belong to P2(1) space group
in the native state and in complex with glucose and substrate mimetics, to 2.4 A, 2.9 A, and 1.9 A resolution, respectively. The structure encompasses a distorted (beta/alpha)7-barrel juxtaposed to a C-terminal alpha-helical domain, which also participates in the formation of the active-site cleft. The active site comprises two acidic catalytic residues, Glu183 and Asp354, the polarizer His10, aromatic gate-keepers Trp28, Trp270, Trp407, and Trp416 and the residue Tyr233, which is fully conserved among GH13- and GH57-type branching enzymes