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Literature summary extracted from

  • Mehta, D.; Satyanarayana, T.
    Dimerization mediates thermo-adaptation, substrate affinity and transglycosylation in a highly thermostable maltogenic amylase of Geobacillus thermoleovorans (2013), PLoS ONE, 8, e73612.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.133 expressed in Escherichia coli BL21(DE3) cells Geobacillus thermoleovorans

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.133 D109A the mutant shows increased affinity towards amylose, amylopectin and starch, and a decreased affinity towards alpha- and beta-cyclodextrin Geobacillus thermoleovorans
3.2.1.133 D109E the mutant does not show any effect on the binding affinity and substrate hydrolytic efficiency towards alpha- and beta-cyclodextrin but a strong decline in the affinity and substrate hydrolytic efficiency of the mutant enzyme towards amylopectin Geobacillus thermoleovorans

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.133 2-mercaptoethanol 69.9% residual activity at 10 mM Geobacillus thermoleovorans
3.2.1.133 Cu2+ complete inhibition at 1 mM Geobacillus thermoleovorans
3.2.1.133 diethyl dicarbonate 24.5% residual activity at 10 mM Geobacillus thermoleovorans
3.2.1.133 Hg2+ complete inhibition at 1 mM Geobacillus thermoleovorans
3.2.1.133 Mg2+ 84.21% residual activity at 1 mM Geobacillus thermoleovorans
3.2.1.133 additional information EGTA and EDTA have no observable effect on the activity Geobacillus thermoleovorans
3.2.1.133 N-bromosuccinamide complete inhibition at 1 mM Geobacillus thermoleovorans
3.2.1.133 Woodward's reagent K 72.4% residual activity at 10 mM Geobacillus thermoleovorans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.133 Al3+ 117.4% activity at 1 mM Geobacillus thermoleovorans
3.2.1.133 Co2+ 131.2% activity at 1 mM Geobacillus thermoleovorans
3.2.1.133 Mn2+ 145.1% activity at 1 mM Geobacillus thermoleovorans
3.2.1.133 additional information K+, Ni2+, Ca2+, and Ba2+ do not exert any observable effect on enzyme activity Geobacillus thermoleovorans
3.2.1.133 Na+ 123% activity at 1 mM Geobacillus thermoleovorans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.133 72500
-
 2 * 72500, SDS-PAGE Geobacillus thermoleovorans
3.2.1.133 145000
-
 dimer, gel filtration Geobacillus thermoleovorans
3.2.1.133 725000
-
 1 * 725000, SDS_PAGE Geobacillus thermoleovorans

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.133 Geobacillus thermoleovorans G8N704
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.133 Ni2+-NTA agarose resin column chromatography, and Sephacryl S-200 gel filtration Geobacillus thermoleovorans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.133 acarbose + H2O
-
 Geobacillus thermoleovorans D-glucose + acarviosine-glucose
-
 ?
3.2.1.133 alpha-cyclodextrin + H2O
-
 Geobacillus thermoleovorans maltose + D-glucose
-
 ?
3.2.1.133 amylopectin + H2O
-
 Geobacillus thermoleovorans maltose + ?
-
 ?
3.2.1.133 amylose + H2O
-
 Geobacillus thermoleovorans maltose + ?
-
 ?
3.2.1.133 beta-cyclodextrin + H2O
-
 Geobacillus thermoleovorans maltose + D-glucose
-
 ?
3.2.1.133 additional information the dimeric enzyme transglycosylates hydrolytic products of G4/G5 and acarbose, while the monomeric form does not because of the lack of extra sugar-binding space formed due to dimerization Geobacillus thermoleovorans ?
-
 ?
3.2.1.133 pullulan + H2O
-
 Geobacillus thermoleovorans ?
-
 ?
3.2.1.133 soluble starch + H2O the enzyme displays less hydrolytic action on raw starches than on soluble starch Geobacillus thermoleovorans maltose + ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.133 homodimer 2 * 72500, SDS-PAGE Geobacillus thermoleovorans
3.2.1.133 monomer 1 * 725000, SDS_PAGE Geobacillus thermoleovorans

Synonyms

EC Number Synonyms Comment Organism
3.2.1.133 glucan-1,4-alpha-maltohydrolase
-
 Geobacillus thermoleovorans
3.2.1.133 maltogenic amylase
-
 Geobacillus thermoleovorans
3.2.1.133 MAmy
-
 Geobacillus thermoleovorans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.133 80
-
-
 Geobacillus thermoleovorans

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.133 40 100 about 35% activity at 40°C, about 60% activity at 50°C, about 80% activity at 90°C, about 35% activity at 70°C, 100% activity at 80°C, about 97% activity at 90°C, and about 75% activity at 100°C Geobacillus thermoleovorans

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.133 90
-
 the half-life values of the monomeric enzyme at 80, 90 and 100°C are 35.7, 8.2 and 3.12 h, respectively. The half-life values of the dimeric enzyme at 80, 90 and 100°C are 55.7, 12.63 and 3.58 h, respectively Geobacillus thermoleovorans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.133 0.005
-
 amylopectin mutant enzyme D109E, at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 0.021
-
 soluble starch mutant enzyme D109E, at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 0.022
-
 amylose mutant enzyme D109E, at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 0.04
-
 amylose dimeric enzyme form, at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 0.04
-
 amylopectin dimeric enzyme form, at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 0.04
-
 soluble starch dimeric enzyme form, at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 0.1
-
 alpha-cyclodextrin monomeric enzyme form, at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 0.1
-
 amylopectin mutant enzyme D109A, at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 0.12
-
 beta-cyclodextrin monomeric enzyme form, at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 0.12
-
 soluble starch mutant enzyme D109A, at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 0.13
-
 amylose mutant enzyme D109A, at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 0.17
-
 amylopectin monomeric enzyme form, at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 0.2
-
 soluble starch monomeric enzyme form, at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 0.21
-
 amylose monomeric enzyme form, at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 0.49
-
 beta-cyclodextrin mutant enzyme D109A at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 0.66
-
 beta-cyclodextrin mutant enzyme D109E at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 0.75
-
 alpha-cyclodextrin mutant enzyme D109A, at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 1.33
-
 beta-cyclodextrin dimeric enzyme form, at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 1.39
-
 alpha-cyclodextrin mutant enzyme D109E, at pH 7.0 and 80°C Geobacillus thermoleovorans
3.2.1.133 2.78
-
 alpha-cyclodextrin dimeric enzyme form, at pH 7.0 and 80°C Geobacillus thermoleovorans

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.133 5 9 the enzyme is active over a wide range of pH between 5.0 and 9.0 (more than 90% activity) but the activity drastically declines at pH 4.0 and 10.0 to 20 and less than 5%, respectively Geobacillus thermoleovorans

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.133 5 8 there is no loss in the activity of the enzyme till 14 days of incubation at pH 7.0 and 8.0, but it decreases drastically after 8 days at pH 5.0 and 6.0 Geobacillus thermoleovorans