Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant Lam81A in Escherichia coli strain BL21 | Thermobifida fusca |
Protein Variants | Comment | Organism |
---|---|---|
D422A | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
D422E | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
D424A | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
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 |
D424H/S501A | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
E499A | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
E499D | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
E503A | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
E503D | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
F425A | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
F425Y | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
H423A | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
H426A | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
N421A | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
S500A | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
S501A | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
S502A | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
W404A | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
W444A | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
Y427A | site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme | Thermobifida fusca |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics of wild-type and mutant enzymes, overview | Thermobifida fusca |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermobifida fusca | - |
- |
- |
Thermobifida fusca YX-ER1 | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
substrate specificities of wild-type and mutant enzymes, overview | Thermobifida fusca |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-glucan + H2O | - |
Thermobifida fusca | ? | - |
? | |
beta-glucan + H2O | - |
Thermobifida fusca YX-ER1 | ? | - |
? | |
carboxymethylcellulose + H2O | - |
Thermobifida fusca | ? | - |
? | |
laminarin + H2O | - |
Thermobifida fusca | ? | - |
? | |
laminarin + H2O | - |
Thermobifida fusca YX-ER1 | ? | - |
? | |
lichenan + H2O | - |
Thermobifida fusca | ? | - |
? | |
lichenan + H2O | - |
Thermobifida fusca YX-ER1 | ? | - |
? | |
additional information | substrate specificities of wild-type and mutant enzymes, overview | Thermobifida fusca | ? | - |
? | |
additional information | substrate specificities of wild-type and mutant enzymes, overview | Thermobifida fusca YX-ER1 | ? | - |
? | |
pachyman + H2O | - |
Thermobifida fusca | ? | - |
? | |
pachyman + H2O | - |
Thermobifida fusca YX-ER1 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
beta-1,3-glucanase | - |
Thermobifida fusca |
Lam81A | - |
Thermobifida fusca |
More | Lam81A is a single domain family 81 beta-1,3-endoglucanase | Thermobifida fusca |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
assay at | Thermobifida fusca |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.8 | - |
assay at | Thermobifida fusca |