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Literature summary extracted from

  • Kang, Y.N.; Tanabe, A.; Adachi, M.; Utsumi, S.; Mikami, B.
    Structural analysis of threonine 342 mutants of soybean beta-amylase: role of a conformational change of the inner loop in the catalytic mechanism (2005), Biochemistry, 44, 5106-5116.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.2 expression of wild-type and mutant enzymes in Escherichia coli strain JM105 Glycine max

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.2 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 Glycine max

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.2 T342A site-directed mutagenesis, structural analysis of mutant active site conformation Glycine max
3.2.1.2 T342S site-directed mutagenesis, structural analysis of mutant active site conformation Glycine max
3.2.1.2 T342V site-directed mutagenesis, structural analysis of mutant active site conformation Glycine max

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.2 additional information
-
 additional information
-
 Glycine max
3.2.1.2 0.26
-
 amylopectin pH 5.4, 37°C, recombinant mutant T342A Glycine max
3.2.1.2 0.39
-
 amylopectin pH 5.4, 37°C, recombinant mutant T342S Glycine max
3.2.1.2 1.84
-
 amylopectin pH 5.4, 37°C, recombinant mutant T342V Glycine max
3.2.1.2 1.94
-
 amylopectin pH 5.4, 37°C, recombinant wild-type enzyme Glycine max

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.2 Glycine max P10538
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.2 recombinant wild-type and mutant enzymes from Escherichia coli strain JM105 Glycine max

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.2 (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 active site structure, carbohydrate binding subsites, role of a conformational change of the inner loop in the catalytic mechanism, T342 is involved, overview Glycine max
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.2 amylopectin + H2O from potato Glycine max maltose + ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.2 37
-
 assay at Glycine max

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.2 0.24
-
 amylopectin pH 5.4, 37°C, recombinant mutant T342V Glycine max
3.2.1.2 0.75
-
 amylopectin pH 5.4, 37°C, recombinant mutant T342A Glycine max
3.2.1.2 3.5
-
 amylopectin pH 5.4, 37°C, recombinant mutant T342S Glycine max
3.2.1.2 98.4
-
 amylopectin pH 5.4, 37°C, recombinant mutant T342V Glycine max
3.2.1.2 1280
-
 amylopectin pH 5.4, 37°C, recombinant wild-type enzyme Glycine max

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.2 5.4
-
-
 Glycine max