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Literature summary for 3.2.1.4 extracted from

  • Kang, H.J.; Uegaki, K.; Fukada, H.; Ishikawa, K.
    Improvement of the enzymatic activity of the hyperthermophilic cellulase from Pyrococcus horikoshii (2007), Extremophiles, 11, 251-256.
    View publication on PubMed

Protein Variants

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 [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

Organism UniProt Comment Textmining
Pyrococcus horikoshii O58925
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
crystalline cellulose + H2O
-
Pyrococcus horikoshii ?
-
?
p-nitrophenyl cellobiose + H2O
-
Pyrococcus horikoshii ?
-
?

Synonyms

Synonyms Comment Organism
EGPh
-
Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
90
-
mutant enzyme C106A/C159A/C372A/C412A Pyrococcus horikoshii

Temperature Stability [°C]

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 [1/s]

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

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