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2.4.1.25: 4-alpha-glucanotransferase

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

Word Map on EC 2.4.1.25

Reaction

maltononaose
+
maltotriose
=
maltoundecaose
 +
D-glucose

Synonyms

(1->4)-alpha-D-glucan:(1->4)-alpha-D-glucan 4-alpha-D-glycosyltransferase, 4-alpha-D-alpha-glucanotransferase, 4-alpha-glucanotransferase, 4-alpha-GTase, 4alphaGT, 4alphaGTase, AgtA, AgtB, alpha-1,4-glucanotransferase, alpha-1,4-transferase, alpha-amylase-like transglycosylase, alpha-glucanotransferase, alphaGT, alphaGTase, AMase, amylmaltase, amylomaltase, At2g40840, CGTase, Cqm1, D-enzyme, debranching enzyme, debranching enzyme maltodextrin glycosyltransferase, dextrin glycosyltransferase, dextrin glycosyltransferase,, dextrin transglycosylase, disproportionating enzyme, DPE1, DPE2, EC 2.4.1.3, exo-MGTase, GDE, GH77, GH77 amylomaltase, glycogen debranching enzyme, GTase, MalQ, maltodextrin glycosyltransferase, maltosyltransferase, MgtA, MmtA, More, MQ-01, MTase, oligo-1,4-1,4-glucantransferase, PyAMase, TAalphaGT, TAalphaGTase, TLGT, TmalphaGT, TreX, TS alpha GTase, TSalphaGT

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.25 4-alpha-glucanotransferase

Crystallization

Crystallization on EC 2.4.1.25 - 4-alpha-glucanotransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 2.0 M ammonium sulfate and 0.1 M bis-tris methane (pH 6.5)
sitting drop vapor diffusion method, using 0.1 M bis-Tris pH 5.5 and 2.0 M ammonium sulfate
hanging drop vapor diffusion method, using 20% (w/v) PEG-3350
TreX in complex with an acarbose ligand, microbatch method under oil at 18°C, dimeric crystal from 16% PEG 8000, 0.2 M NaCl, and 0.1 M CHES buffer, pH 9.5, tetrameric crystal form from 2.2 M ammonium phosphate and 0.1 M Tris-HCl buffer, pH 8.5. For the acarbose intermediate complex crystal, 0.1% acarbose is added to the protein, followed by incubation for 1 h prior to the setup of the crystal in 8% PEG 3000, 0.2M lithium sulfate, and 0.1 M imidazole buffer, pH 8.0, cyroprotection by 20% glycerol in mother liquor, in both crystal forms, the asymmetric unit consists of one dimer, X-ray diffraction structure determination and analysis at 2.8-3.0 A resolution
hanging-drop vapour-diffusion method. Crystal diffracts to 2.0 A resolution and belongs to space group C222(1), with unit-cell parameters a = 69.7, b = 120.3, c = 174.2 A
-
crystallized in 2 forms, I and II, form I crystals belongs to hexagonal space group P6(4)22, form II crystals to orthorhombic space group P2(1)2(1)2
hanging drop vapor diffusion method at 25°C, crystal structure of the enzyme with and without an inhibitor, acarbose. The acarbose-bound structure clarifies that Glu123 and Asp214 are the catalytic nucleophile and acid/base catalyst, respectively
Gtase, hanging drop method, inhibitor complex,crystals belong to space group I222, unit-cell dimensions a = 92.6 A, b = 180.3 A, c = 199.2 A, free Gtase crystals a = 94.5 A, b = 181.4 A, c = 197.3 A
-
hanging-drop vapor-diffusion method
crystals belong to space group P6(4) with cell parameters a = b = 154 A and c = 64 A
-
to 2.3 A resolution. Structure shows a pattern of conformational flexibility in the 250s loop with higher B-factor. The conformational flexibility of the loop may be involved in substrate binding in the GH77 family
purified recombinant enzyme, hanging drop vapour diffusion method, 0.003 ml of protein solution containing 10 mM MES-NaOH, pH 6.5, with 1 mM dithiothreitol is mixed with 0.001-0.003 ml of reservoir solution containing 0.4-0.8 M sodium malonate, pH 5.6, and 1 mM dithiothreitol, equilibration against reservoir solution at room temperature, 1 week, for enzyme-acarbose complexing the crystals are soaked in 0.5 ml of 0.8 M sodium malonate, pH 5.6, with 5 mg/ml acarbose and with or without and 4-deoxyglucose, for 30 min, X-ray diffraction structure determination and analysis at 1.9-2.5 A resolution