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3.2.1.20: alpha-glucosidase

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

Word Map on EC 3.2.1.20

Reaction

maltotetraose
+ 3 H2O = 4 alpha-D-glucose

Synonyms

6-phospho-alpha-glucosidase, AAGR-1, AAGR-2, AAGR-3, AAGR-4, acid alpha-glucosidase, acid alpha-glucoside hydrolase, acid GAA, acid maltase, acidic alpha-glucosidase, AG, AgdB, AGL, AglA, aGlu, alglucosidase alfa, alpha-1,4-glucosidase, alpha-D-glucosidase, alpha-D-glucoside glucohydrolase, alpha-GD, alpha-glucopyranosidase, alpha-glucosid-specific GH4 enzyme, alpha-glucosidase, alpha-glucosidase B, alpha-glucosidase I, alpha-glucosidase II, alpha-glucosidase III, alpha-glucosidase MAL12, alpha-glucosidase MAL32, alpha-glucosidase type I, alpha-glucosidase type IV, alpha-glucoside glucohydrolase, alpha-glucoside hydrolase, alpha-transglucosidase, alphaGlu1, alphaGlu2, alphaGlu3, alphaGluFa, Amy112, CHEI, CWH41, exo-alpha-l, 4-glucosidase, exo-alpha-l,4-glucosidase, GAA, GH13 alpha-glucosidase, GluA, glucoamylase, glucoinvertase, glucosidoinvertase, glucosidosucrase, GlyFa1, GlyFa2, GSJ, HBG III, HBGase I, HBGase II, HBGase III, high pI alpha-glucosidase, intestinal alpha-glucosidase, intestinal maltase, JHGase I, MAL12, MAL2, MAL32, MalA, MalH, maltase, maltase glucoamylase, maltase-glucoamylase, maltodextrin glucosidase, MalZ, MGAM, More, myozyme, NAG, neutral alpha-glucosidase, PalH, Pars_2044, phospho-alpha-glucosidase, R-glucosidase, recombinant human GAA, rhGAA, Saci1160, st2525, Ta0298, TcaAG, TtGluA

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.20 alpha-glucosidase

Crystallization

Crystallization on EC 3.2.1.20 - alpha-glucosidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
10 mg/ml purified protein with 5 mM inhibitor D-(+)-glucono-1,5-lactone, hanging drop vapour diffusion method, 1 ml reservoir solution containing 20% v/v 2-propanol, 20% w/v PEG 4000, 0.1 M sodium citrate, pH 5.6, plus 0.01 ml of a solution consisting of 0.004 ml reservoir solution, 0.005 ml protein solution, containing 1% protein w/v in 10 mM phosphate, pH 7.0, and 0.001 ml inhibitor 50 mM, 2-3 weeks, X-ray diffraction structure determination at 2.5 A resolution
-
crystal structure of the enzyme is determined to a 2.0 A resolution, by X-ray crystallography
apoenzyme and enzyme complexed with acarbose, X-ray diffraction structure determination and anaylsis at 2.0 A and 1.9 A resolution, respectively
purified recombinant wild-type and selenomethionine-labeled enzyme, hanging drop vapour diffusion method, 2-5 mg/ml protein in 20 mM Tris-HCl, pH 7.5, and 20 mM NaCl, 0.002 ml protein solution is mixed with 0.003 ml reservoir solution and equilibrated against 1 ml reservoir solution, different compositions of the reservoir solution result in different crystal forms, overview, X-ray diffraction structure determination and analysis of the different crystal forms at 2.5-4.2 A resolution
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purified recombinant wild-type and selenomethionine-labeled enzyme, hanging drop vapour diffusion method, hexameric crystal form, X-ray diffraction structure determination and analysis of the different crystal forms at 2.5 A resolution, structure modelling of domains, full-length enzyme, and active site