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Literature summary for 3.2.1.73 extracted from

  • Liu, W.; Lin, Y.; Jeng, W.; Chen, J.; Wang, A.; Shyur, L.
    Engineering of dual-functional hybrid glucanases (2012), Protein Eng. Des. Sel., 25, 771-780.
    View publication on PubMed
Search for more literature for 3.2.1.73

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Fibrobacter succinogenes

Protein Variants

Protein Variants Comment Organism
additional information engineering of dual-functional hybrid glucanases from a truncated and mutated 1,3-1,4-beta-D-glucanase gene TFsW203F from Fibrobacter succinogenes, and a 1,3-beta-D-glucanase gene TmLam from hyperthermophilic Thermotoga maritima used as target enzymes, by ligating substrate-binding domains (TmB1 and TmB2) and the catalytic domain (TmLamCD) of TmLam to the N- or C-terminus of TFsW203F to create four hybrid enzymes, TmB1-TFsW203F, TFsW203F-TmB2, TmB1-TFsW203F-TmB2 and TFsW203F-TmLamCD, creation of desirable hybrid enzymes with economic benefits for industrial applications. Improved thermal tolerance of the hybrid enzyme TFsW203FTmLamCD, fluorescence and circular dichroism spectrometric analyses, overview. Kinetic properties of parental TFsW203F and mutant hybrid glucanases Fibrobacter succinogenes
W203F site-directed mutagenesis, truncated and mutated 1,3–1,4-beta-D-glucanase, no activity with laminarin Fibrobacter succinogenes

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information 5.3 mg/ml for mutant TFsW203F with lichenan, pH 6.0-7.0, 45°C. Kinetic properties of parental TFsW203F and mutant hybrid glucanases, overview Fibrobacter succinogenes

Organism

Organism UniProt Comment Textmining
Fibrobacter succinogenes
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Fibrobacter succinogenes

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
626
-
 substrate lichenan, pH 6.0-7.0, 45°C, mutant TFsW203F Fibrobacter succinogenes

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
laminarin + H2O
-
 Fibrobacter succinogenes ?
-
 ?
lichenan + H2O
-
 Fibrobacter succinogenes ?
-
 ?

Synonyms

Synonyms Comment Organism
1,3-1,4-beta-D-glucanase
-
 Fibrobacter succinogenes
Lichenase
-
 Fibrobacter succinogenes

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
 assay at Fibrobacter succinogenes

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30 90 temperature effects on mutant W203F and on W203F mutant bifunctional hybrid enzymes, the latter is more resistant to heat treatment than the parental TFsW203F, overview Fibrobacter succinogenes

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
10100
-
 lichenan pH 6.0-7.0, 45°C, mutant TFsW203F Fibrobacter succinogenes

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 7 assay at Fibrobacter succinogenes

General Information

General Information Comment Organism
additional information Glu56, Asp58 and Glu60 residues located in the active site cavity of the enzyme play key roles in enzyme catalysis, functioning as general acid-base residues, structure and functional relationships of Fsbeta-glucanase Fibrobacter succinogenes
physiological function fibrolytic enzyme which plays an important role in the hydrolysis of polysaccharide components. It is responsible for precisely hydrolyzing beta-1,4-glycosidic bonds adjacent to the beta-1,3-linkages in lichenan or mixed-linked beta-D-glucans, yielding mainly cellotriose, cellotetraose and cellopentaose Fibrobacter succinogenes