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3.2.1.2: beta-amylase

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

Word Map on EC 3.2.1.2

Reaction

(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose
+
H2O
=
(alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose
 +
alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose

Synonyms

(1-4)-alpha-D-glucan maltohydrolase, 1,4-alpha-D-glucan malto-hydrolase, 1,4-alpha-D-glucan maltohydrolase, 1-4-alpha-glucan maltohydrolase, alpha-1,4-glucan maltohydrolase, amylase, beta-, ARATH, BAM-1, BAM-2, BAM-3, BAM-5, BAM-6, BAM-7, BAM-8, BAM-9, BAM1, BAM3, BAM4, BCB, beta amylase, beta-amylase, beta-amylase 1, beta-amylase I, beta-amylase1, beta-amylase2, beta-amylase8, BMY, Bmy1, Bmy2, Cs-COR018, CT-BMY, glycogenase, More, PF0870, saccharogen amylase, saccharogenamylase, SBA, Sd1, Sd2H, Sd2L, spoII, TCMA, TR-BAMY, type I beta-amylase, type II beta-amylase

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.2 beta-amylase

Crystallization

Crystallization on EC 3.2.1.2 - beta-amylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
beta-amylase complexed with the inhibitors glucose, maltose and O-alpha-D-glucopyranosyl(1-4)O-alpha-D-glucopyranosyl(1-4)D-xylopyranose and the affinity-labeling reagents 2,3-epoxypropyl-alpha-D-glucopyranoside and 3,4-epoxybutyl-alpha-D-glucopyranoside, X-ray analysis
crystal structure determined by the multiple isomorphous replacement method
-
purified recombinant wild-type and mutant T47M/Y164E/T328N, hanging drop vapour diffusion method, 18°C, 0.005 ml of 15 mg/ml protein in 0.05 M sodium acetate is mixed with 0.005 ml mother liquor containing 15% PEG 6000, 5% saturated ammonium sulfate, 0.1 M phosphate, pH 6.5, crystallization of mutants Y164E and Y164F in the same way except for usage of 0.1 M sodium acetate buffer, pH 4.6, instead of phosphate buffer, X-ray diffraction structure determination and analysis at 1.72-1.95 A resolution, active site structure modelling
X-ray crystal structures of wild-type enzyme complexed with maltose and of E172A catalytic site mutant complexed with maltopentaose
crystal structure of mutant enzyme W55R
high-resolution crystal structure for catalytic active enzyme and for the enzyme complexes with either beta-maltose or maltal
-
purified recombinant mutant enzymes, mutant enzyme E186Q in complex with substrate maltopentaose, and mutant enzyme E380Q in complex with product maltose, hanging drop vapour diffusion method, 20 mg/ml protein in 45-50% w/v ammonium sulfate, 0.1 M sodium acetate, pH 5.4, 1 mM EDTA, and 18 mM 2-methyl-2,4-pentanediol, equilibration against 1 ml mother liquor, 4°C, soaking of crystals in 30 mM ligand solution, cryoprotection of crystals with 30% v/v glycerol in crystallization solution, X-ray diffraction structure determination and analysis at 1.6 and 1.9 A resolution, respectively, active site structure modelling
purified recombinant T342 mutant enzymes, hanging drop vapour diffusion method, 0.005 ml of 10 mg/ml protein solution is mixed with 0.005 ml of reservoir solution containing 40-50% w/v ammonium sulfate, 1 mM EDTA, 18 mM 2-methyl-2,4-pentanediol, and 0.1 M sodium acetate, pH 5.4, equilibration against 1 ml of reservoir solution, 4°C, gradual soaking of crystals in 0.1 M sodium acetate, pH 6.1, 50% w/v ammonium sulfate, 1 mM EDTA, 20 mM DTT, 0.3 M maltose, and 30% v/v glycerol, X-ray diffraction structure determination and analysis at 1.12-1.6 A resolution, active site structure modelling
wild-type, M51T, E178Y and N340T mutant SBA, complexed with maltose, hanging-drop vapor diffusion method, X-ray analysis
mutant M185L/S295A/I297V/S350P/S351P/Q352D/A376S
-