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Literature summary for 3.2.1.39 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 3.2.1.39

Cloned(Commentary)

Cloned (Comment) Organism
gene TmLam, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Thermotoga maritima

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 mutant hybrid glucanases Thermotoga maritima

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information 8.3 mg/ml with lichenan and 1.3 mg/ml with laminarin, pH 6.0-7.0, 45°C, wild-type catalytic enzyme domain, kinetic properties of mutant hybrid glucanases, overview Thermotoga maritima

Organism

Organism UniProt Comment Textmining
Thermotoga maritima
-
 gene TmLam
-
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
 gene TmLam
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by ncikel affiniyt chromatography Thermotoga maritima

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
laminarin + H2O the mutant enzyme W203F fused to 1,3-beta-D-glucanase catalytic domain shows a 3.6fold increase in specific activity against laminarin as compared with the 1,3-beta-D-glucanase catalytic domain alone with laminaritriose as the major product Thermotoga maritima laminaritriose + ? major product ?
laminarin + H2O the mutant enzyme W203F fused to 1,3-beta-D-glucanase catalytic domain shows a 3.6fold increase in specific activity against laminarin as compared with the 1,3-beta-D-glucanase catalytic domain alone with laminaritriose as the major product Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 laminaritriose + ? major product ?
lichenan + H2O
-
 Thermotoga maritima ?
-
 ?
lichenan + H2O
-
 Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 ?
-
 ?

Synonyms

Synonyms Comment Organism
1,3-beta-D-glucanase
-
 Thermotoga maritima
laminarinase
-
 Thermotoga maritima
TmLam
-
 Thermotoga maritima

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
95
-
-
 Thermotoga maritima

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30 90 temperature effects on wild-type and mutant hybrid enzymes, overview Thermotoga maritima

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
38
-
 lichenan pH 6.0-7.0, 45°C, wild-type catalytic enzyme domain Thermotoga maritima
109
-
 Laminarin pH 6.0-7.0, 45°C, wild-type catalytic enzyme domain Thermotoga maritima

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 8
-
 Thermotoga maritima

General Information

General Information Comment Organism
evolution the thermostable laminarinase is composed of a GH family 16 catalytic domain flanked by two family 4 carbohydrate-binding modules (CBM4-1 and CBM4-2) at each terminus Thermotoga maritima
physiological function fibrolytic enzyme which plays an important role in the hydrolysis of polysaccharide components. It hydrolyzes internal beta-1,3-glycosidic linkages in beta-1,3-glucans, which form the main component of the cell wall in yeasts and filamentous fungi and the major structural and storage polysaccharide in marine macroalgae such as Laminaria saccharina Thermotoga maritima