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Literature summary for 3.2.1.176 extracted from

  • Komor, R.S.; Romero, P.A.; Xie, C.B.; Arnold, F.H.
    Highly thermostable fungal cellobiohydrolase I (Cel7A) engineered using predictive methods (2012), Protein Eng. Des. Sel., 25, 827-833.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in yeast strain YDR483W BY4742 Rasamsonia emersonii

Protein Variants

Protein Variants Comment Organism
A201P predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
A329G predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
A383Y predicted from structure fold, calculation of the thermostability of the mutant, stabilizing mutation Rasamsonia emersonii
A383Y the mutation increases stability and results in a 10°C increase in the optimal temperature for activity, to 65°C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type Rasamsonia emersonii
D300K predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
D354V predicted from structure fold, calculation of the thermostability of the mutant, stabilizing mutation Rasamsonia emersonii
D354V the mutation increases stability and results in a 10°C increase in the optimal temperature for activity, to 65°C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type Rasamsonia emersonii
D52T predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
E325P predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
H208Y predicted from structure fold, calculation of the thermostability of the mutant, stabilizing mutation Rasamsonia emersonii
H208Y the mutation increases stability and results in a 10°C increase in the optimal temperature for activity, to 65°C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type Rasamsonia emersonii
H358K predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
H358R predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
H358V predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
L113M predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
additional information prediction of point mutations to increase the thermostability of the enzyme, overview Rasamsonia emersonii
N126G predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
N439G predicted from structure fold, calculation of the thermostability of the mutant, the mutation results in loss of expression Rasamsonia emersonii
N93K predicted from structure fold, calculation of the thermostability of the mutant, increased thermotability compared to the wild-type enzyme Rasamsonia emersonii
N93K the mutation increases stability and results in a 10°C increase in the optimal temperature for activity, to 65°C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type Rasamsonia emersonii
P399G predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
Q345M predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
S130T predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
S13P predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
S13P/Y60L7S324P/A383Y7Y43 predicted from structure fold, calculation of the thermostability of the mutant, the mutant is the most thermostable variant Rasamsonia emersonii
S222K predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
S324P predicted from structure fold, calculation of the thermostability of the mutant, stabilizing mutation Rasamsonia emersonii
S324P the mutation increases stability and results in a 10°C increase in the optimal temperature for activity, to 65°C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type Rasamsonia emersonii
S57D predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
S5T predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
T164K predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
T257 V predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
T257I predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
T257K predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
T273K predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
T273P predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
T339P predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
T339Q predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
T392I predicted from structure fold, calculation of the thermostability of the mutant, stabilizing mutation Rasamsonia emersonii
T392I the mutation increases stability and results in a 10°C increase in the optimal temperature for activity, to 65°C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type Rasamsonia emersonii
T395P predicted from structure fold, calculation of the thermostability of the mutant, the mutation results in loss of expression Rasamsonia emersonii
T408D predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
T41V predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
V110L predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
V217I predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
V227L predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
V331M predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
V404A predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
Y430F predicted from structure fold, calculation of the thermostability of the mutant, increased thermotability compared to the wild-type enzyme Rasamsonia emersonii
Y430F the mutation increases stability and results in a 10°C increase in the optimal temperature for activity, to 65°C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type Rasamsonia emersonii
Y60I predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
Y60L predicted from structure fold, calculation of the thermostability of the mutant, increased thermotability compared to the wild-type enzyme Rasamsonia emersonii
Y60L the mutation increases stability and results in a 10°C increase in the optimal temperature for activity, to 65°C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type Rasamsonia emersonii

Organism

Organism UniProt Comment Textmining
Rasamsonia emersonii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Rasamsonia emersonii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-methylumbelliferyl beta-D-lactopyranoside + H2O
-
Rasamsonia emersonii 4-methylumbelliferone + lactose
-
?
crystalline cellulose + H2O
-
Rasamsonia emersonii cellobiose
-
?

Synonyms

Synonyms Comment Organism
CBH I
-
Rasamsonia emersonii
Cel7A
-
Rasamsonia emersonii
cellobiohydrolase I
-
Rasamsonia emersonii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
-
Rasamsonia emersonii