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Literature summary extracted from

  • Masilamani, R.; Sharma, O.P.; Muthuvel, S.K.; Natarajan, S.
    Cloning, expression of beta-1,3-1,4 glucanase from Bacillus subtilis SU40 and the effect of calcium ion on the stability of recombinant enzyme: in vitro and in silico analysis (2013), Bioinformation, 9, 958-962.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.6 gene SU40-glu, DNA and amino acid sequence determination and analysis, phylogenetic analysis, overexpression in Escherichia coli strain BL21(DE3) Bacillus licheniformis
3.2.1.73 gene SU40-glu, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Bacillus subtilis

General Stability

EC Number General Stability Organism
3.2.1.6 calcium ion has a general stabilizing effect on Bacillus beta-1,3-1,4 glucanases Bacillus licheniformis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.6 Ca2+ slightly activating, 142% activity at 15 mM, slightly inhibitory at 25 mM with 86% of maximal activity Bacillus licheniformis
3.2.1.73 Hg2+ complete inhibition Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.6 Ca2+ slightly activating, 142% activity at 15 mM, slightly inhibitory at 25 mM with 86% of maximal activity. Calcium ion has a general stabilizing effect on Bacillus beta-1,3-1,4 glucanases. Calcium is bound to the backbone carbonyl oxygens of Pro9, Gly45, Asp207 and carboxylate oxygen of Asp207 and two water molecules Bacillus licheniformis
3.2.1.73 additional information metal ions such as Mn2+, Na+, K+, Mg2+ and Zn2+ show little or no effect on the enzyme activity Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.6 24000
-
 x * 24200, about, sequence calculation, x * 24000, recombinant enzyme, SDS-PAGE Bacillus licheniformis
3.2.1.6 24200
-
 x * 24200, about, sequence calculation, x * 24000, recombinant enzyme, SDS-PAGE Bacillus licheniformis
3.2.1.73 24000
-
 x * 24000, recombinant enzyme, SDS-PAGE Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.6 Bacillus licheniformis Q84GK1 gene SU40-glu
-
3.2.1.73 Bacillus subtilis G0YW23 gene SU40-glu
-
3.2.1.73 Bacillus subtilis SU40 G0YW23 gene SU40-glu
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.6 recombinant enzyme from Escherichia coli strain BL21(DE3) to homogeneity Bacillus licheniformis
3.2.1.73 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity Bacillus subtilis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.6 37.85
-
 purified recombinant enzyme, pH 8.0, 60°C Bacillus licheniformis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.6 additional information the enzyme acts as a bi-functional enzyme with single catalytic domain Bacillus licheniformis ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Bacillus subtilis ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Bacillus subtilis SU40 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus subtilis ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus subtilis SU40 ?
-
 ?
3.2.1.73 xylan + H2O
-
 Bacillus subtilis ?
-
 ?
3.2.1.73 xylan + H2O
-
 Bacillus subtilis SU40 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.6 ? x * 24200, about, sequence calculation, x * 24000, recombinant enzyme, SDS-PAGE Bacillus licheniformis
3.2.1.6 More three-dimensional model, overview Bacillus licheniformis
3.2.1.73 ? x * 24000, recombinant enzyme, SDS-PAGE Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
3.2.1.6 beta-1,3-1,4 glucanase
-
 Bacillus licheniformis
3.2.1.73 beta-1,3-1,4 glucanase
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.6 60
-
 recombinant enzyme Bacillus licheniformis
3.2.1.73 60
-
-
 Bacillus subtilis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.6 85
-
 around 54% of total activity remains after 60 min at pH 8.0 Bacillus licheniformis
3.2.1.73 80
-
 purified recombinant enzyme, retains 54% activity at 80°C after incubation for 60 min Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.6 8
-
 recombinant enzyme Bacillus licheniformis
3.2.1.73 8
-
-
 Bacillus subtilis

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.6 Bacillus licheniformis sequence calculation
-
 5.78

General Information

EC Number General Information Comment Organism
3.2.1.6 additional information active site residues are Trp103, Asp104, Ile106, Ile108 and Glu109 in the beta-strand. Asp107 and Glu105 (as nucleophile) and Glu109 (as acid catalyst) are essential for enzyme activity. Molecular dynamics simulations and structure-function analysis, three-dimensional model, overview Bacillus licheniformis
3.2.1.73 additional information the enzyme amino acid sequence shares a conserved motif EIDIEF. The predicted three-dimensional homology model of the enzyme shows the presence of catalytic residues Glu105, Glu109, and Asp107, single disulfide bridge between Cys32 and Cys61 and three calcium binding site residues Pro9, Gly45 and Asp207. Molecular modelling and molecular dynamics simulation studies reveal that the absence of calcium ion fluctuate the active site residues which are responsible for thermostability. Molecular three-dimensional model of the enzyme with bound Ca2+, overview Bacillus subtilis