Protein Variants | Comment | Organism |
---|---|---|
C106A/C159A | kcat/KM for p-nitrophenyl cellobiose is 1.3fold higher than wild-type value. Activity towards carboxymethyl cellulose is increased by 1.7fold | Pyrococcus horikoshii |
C106A/C159A/C372A/C412A | kcat/KM for p-nitrophenyl cellobiose is 1.4fold higher than wild-type value. Activity towards carboxymethyl cellulose is increased by 2.1fold | Pyrococcus horikoshii |
C372/AC412A | kcat/KM for p-nitrophenyl cellobiose is 2.9fold higher than wild-type value. Activity towards carboxymethyl cellulose is increased by 1.6fold | Pyrococcus horikoshii |
additional information | preparation of a fusion enzyme so that the thermostable chitin-binding domain of chitinase from Pyrococcus furiosus is joined to the C-terminus of EGPh and its variants. The fusion enzymes show stronger activities than the wild-type EGPh toward both carboxymethyl cellulose and crystalline cellulose (Avicel) | Pyrococcus horikoshii |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.35 | - |
p-nitrophenyl cellobiose | 50°C, mutant enzyme C372A/C412A | Pyrococcus horikoshii | |
0.46 | - |
p-nitrophenyl cellobiose | 50°C, mutant enzyme C106A/C159A | Pyrococcus horikoshii | |
0.78 | - |
p-nitrophenyl cellobiose | 50°C, mutant enzyme C106A/C159A/C372A/C412A | Pyrococcus horikoshii | |
0.95 | - |
p-nitrophenyl cellobiose | 50°C, wild-type enzyme | Pyrococcus horikoshii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus horikoshii | O58925 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
crystalline cellulose + H2O | - |
Pyrococcus horikoshii | ? | - |
? | |
p-nitrophenyl cellobiose + H2O | - |
Pyrococcus horikoshii | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
EGPh | - |
Pyrococcus horikoshii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
90 | - |
mutant enzyme C106A/C159A/C372A/C412A | Pyrococcus horikoshii |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
95 | 96 | Tm-value for mutant enzymes C106A/C159A/C372A/C412A, C106A/C159A and C372A/C412A | Pyrococcus horikoshii |
100 | - |
Tm-value for wild-type enzyme | Pyrococcus horikoshii |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.24 | - |
p-nitrophenyl cellobiose | 50°C, mutant enzyme C106A/C159A | Pyrococcus horikoshii | |
0.41 | - |
p-nitrophenyl cellobiose | 50°C, wild-type enzyme | Pyrococcus horikoshii | |
0.43 | - |
p-nitrophenyl cellobiose | 50°C, mutant enzyme C372A/C412A | Pyrococcus horikoshii | |
0.47 | - |
p-nitrophenyl cellobiose | 50°C, mutant enzyme C106A/C159A/C372A/C412A | Pyrococcus horikoshii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5 | 7 | wild-type and mutant enzymes C106A/C159A/C372A/C412A, C106A/C159A and C372A/C412A | Pyrococcus horikoshii |