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Literature summary 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)

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

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.176 A201P predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 A329G predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 A383Y predicted from structure fold, calculation of the thermostability of the mutant, stabilizing mutation Rasamsonia emersonii
3.2.1.176 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
3.2.1.176 D300K predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 D354V predicted from structure fold, calculation of the thermostability of the mutant, stabilizing mutation Rasamsonia emersonii
3.2.1.176 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
3.2.1.176 D52T predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 E325P predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 H208Y predicted from structure fold, calculation of the thermostability of the mutant, stabilizing mutation Rasamsonia emersonii
3.2.1.176 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
3.2.1.176 H358K predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 H358R predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 H358V predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 L113M predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 additional information prediction of point mutations to increase the thermostability of the enzyme, overview Rasamsonia emersonii
3.2.1.176 N126G predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 N439G predicted from structure fold, calculation of the thermostability of the mutant, the mutation results in loss of expression Rasamsonia emersonii
3.2.1.176 N93K predicted from structure fold, calculation of the thermostability of the mutant, increased thermotability compared to the wild-type enzyme Rasamsonia emersonii
3.2.1.176 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
3.2.1.176 P399G predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 Q345M predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 S130T predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 S13P predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 S13P/Y60L7S324P/A383Y7Y43 predicted from structure fold, calculation of the thermostability of the mutant, the mutant is the most thermostable variant Rasamsonia emersonii
3.2.1.176 S222K predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 S324P predicted from structure fold, calculation of the thermostability of the mutant, stabilizing mutation Rasamsonia emersonii
3.2.1.176 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
3.2.1.176 S57D predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 S5T predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 T164K predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 T257 V predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 T257I predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 T257K predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 T273K predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 T273P predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 T339P predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 T339Q predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 T392I predicted from structure fold, calculation of the thermostability of the mutant, stabilizing mutation Rasamsonia emersonii
3.2.1.176 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
3.2.1.176 T395P predicted from structure fold, calculation of the thermostability of the mutant, the mutation results in loss of expression Rasamsonia emersonii
3.2.1.176 T408D predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 T41V predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 V110L predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 V217I predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 V227L predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 V331M predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 V404A predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 Y430F predicted from structure fold, calculation of the thermostability of the mutant, increased thermotability compared to the wild-type enzyme Rasamsonia emersonii
3.2.1.176 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
3.2.1.176 Y60I predicted from structure fold, calculation of the thermostability of the mutant Rasamsonia emersonii
3.2.1.176 Y60L predicted from structure fold, calculation of the thermostability of the mutant, increased thermotability compared to the wild-type enzyme Rasamsonia emersonii
3.2.1.176 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

EC Number Organism UniProt Comment Textmining
3.2.1.176 Rasamsonia emersonii
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.176 4-methylumbelliferyl beta-D-lactopyranoside + H2O
-
 Rasamsonia emersonii 4-methylumbelliferone + lactose
-
 ?
3.2.1.176 crystalline cellulose + H2O
-
 Rasamsonia emersonii cellobiose
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.176 CBH I
-
 Rasamsonia emersonii
3.2.1.176 Cel7A
-
 Rasamsonia emersonii
3.2.1.176 cellobiohydrolase I
-
 Rasamsonia emersonii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.176 55
-
-
 Rasamsonia emersonii