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Literature summary for 3.2.1.6 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
Search for more literature for 3.2.1.6

Cloned(Commentary)

Cloned (Comment) Organism
gene SU40-glu, DNA and amino acid sequence determination and analysis, phylogenetic analysis, overexpression in Escherichia coli strain BL21(DE3) Bacillus licheniformis

General Stability

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

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ slightly activating, 142% activity at 15 mM, slightly inhibitory at 25 mM with 86% of maximal activity Bacillus licheniformis

Metals/Ions

Metals/Ions Comment Organism Structure
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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis Q84GK1 gene SU40-glu
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) to homogeneity Bacillus licheniformis

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme acts as a bi-functional enzyme with single catalytic domain Bacillus licheniformis ?
-
 ?

Subunits

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

Synonyms

Synonyms Comment Organism
beta-1,3-1,4 glucanase
-
 Bacillus licheniformis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 recombinant enzyme Bacillus licheniformis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
85
-
 around 54% of total activity remains after 60 min at pH 8.0 Bacillus licheniformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 recombinant enzyme Bacillus licheniformis

pI Value

Organism Comment pI Value Maximum pI Value
Bacillus licheniformis sequence calculation
-
 5.78

General Information

General Information Comment Organism
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