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Literature summary extracted from

  • McGrath, C.; Vuong, T.; Wilson, D.
    Site-directed mutagenesis to probe catalysis by a Thermobifida fusca beta-1,3-glucanase (Lam81A) (2009), Protein Eng. Des. Sel., 22, 375-382.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.39 expression of wild-type and mutant Lam81A in Escherichia coli strain BL21 Thermobifida fusca

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.39 D422A site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca
3.2.1.39 D422E site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca
3.2.1.39 D424A site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca
3.2.1.39 D424H site-directed mutagenesis, the mutation alters the substrate specificity by increasing the rate of cleavage of mixed-linkage beta-glucan and carboxymethylcellulose 60fold and 16fold, respectively, compared to the wild-type enzyme Thermobifida fusca
3.2.1.39 D424H/S501A site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca
3.2.1.39 E499A site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca
3.2.1.39 E499D site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca
3.2.1.39 E503A site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca
3.2.1.39 E503D site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca
3.2.1.39 F425A site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca
3.2.1.39 F425Y site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca
3.2.1.39 H423A site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca
3.2.1.39 H426A site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca
3.2.1.39 N421A site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca
3.2.1.39 S500A site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca
3.2.1.39 S501A site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca
3.2.1.39 S502A site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca
3.2.1.39 W404A site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca
3.2.1.39 W444A site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca
3.2.1.39 Y427A site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme Thermobifida fusca

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.39 additional information
-
 additional information kinetics of wild-type and mutant enzymes, overview Thermobifida fusca

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.39 Thermobifida fusca
-
-
-
3.2.1.39 Thermobifida fusca YX-ER1
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.39 laminariheptaose + 3 H2O = laminaritriose + 2 laminaribiose D422, E499 and E503 are involved in catalysis.E499 is the catalytic base, F425 plays a major role in substrate binding possibly mediated by aromatic ring stacking with the sugar substrate Thermobifida fusca
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.39 additional information
-
 substrate specificities of wild-type and mutant enzymes, overview Thermobifida fusca

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.39 beta-glucan + H2O
-
 Thermobifida fusca ?
-
 ?
3.2.1.39 beta-glucan + H2O
-
 Thermobifida fusca YX-ER1 ?
-
 ?
3.2.1.39 carboxymethylcellulose + H2O
-
 Thermobifida fusca ?
-
 ?
3.2.1.39 laminarin + H2O
-
 Thermobifida fusca ?
-
 ?
3.2.1.39 laminarin + H2O
-
 Thermobifida fusca YX-ER1 ?
-
 ?
3.2.1.39 lichenan + H2O
-
 Thermobifida fusca ?
-
 ?
3.2.1.39 lichenan + H2O
-
 Thermobifida fusca YX-ER1 ?
-
 ?
3.2.1.39 additional information substrate specificities of wild-type and mutant enzymes, overview Thermobifida fusca ?
-
 ?
3.2.1.39 additional information substrate specificities of wild-type and mutant enzymes, overview Thermobifida fusca YX-ER1 ?
-
 ?
3.2.1.39 pachyman + H2O
-
 Thermobifida fusca ?
-
 ?
3.2.1.39 pachyman + H2O
-
 Thermobifida fusca YX-ER1 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.39 beta-1,3-glucanase
-
 Thermobifida fusca
3.2.1.39 Lam81A
-
 Thermobifida fusca
3.2.1.39 More Lam81A is a single domain family 81 beta-1,3-endoglucanase Thermobifida fusca

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.39 50
-
 assay at Thermobifida fusca

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.39 6.8
-
 assay at Thermobifida fusca