EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.4 | expression in Escherichia coli strain BL21(DE3) | Pyrococcus horikoshii |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.2.1.4 | hanging-drop vapour diffusion method. The crystal of the enzymeligand complex is prepared from the truncated protein lacking five amino acid residues from both the N- and C-terminal ends. Crystal structures of mutants enzymes (E201A, E342A and Y299F) in the complex with either the substrate or product ligands | Pyrococcus horikoshii |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.4 | Q306A | 25% of the activity with avicel as compared to wild-type enzyme | Pyrococcus horikoshii |
3.2.1.4 | W377A | complete loss of activity with avicel | Pyrococcus horikoshii |
3.2.1.4 | W82A | 75% of the activity with avicel as compared to wild-type enzyme | Pyrococcus horikoshii |
3.2.1.4 | Y299F | complete loss of activity with avicel | Pyrococcus horikoshii |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.4 | Pyrococcus horikoshii | O58925 | - |
- |
3.2.1.4 | Pyrococcus horikoshii OT-3 | O58925 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.4 | - |
Pyrococcus horikoshii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.4 | avicel + H2O | - |
Pyrococcus horikoshii | cellobiose + ? | - |
? | |
3.2.1.4 | avicel + H2O | - |
Pyrococcus horikoshii OT-3 | cellobiose + ? | - |
? | |
3.2.1.4 | cellulose + H2O | the substrate position is fixed by the alignment of one cellobiose unit between the two aromatic amino acid residues at subsites +1 and +2. During the enzyme reaction, the glucose structure of cellulose substrates is distorted at subsite -1, and the beta-1,4-glucoside bond between glucose moieties is twisted between subsites -1 and +1. Subsite -2 specifically recognizes the glucose residue, but recognition by subsites +1 and +2 is loose during the enzyme reaction. Analysis of the enzyme-substrate structure suggests that an incoming water molecule, essential for hydrolysis during the retention process, might be introduced to the cleavage position after the cellobiose product at subsites +1 and +2 is released from the active site | Pyrococcus horikoshii | cellobiose + ? | - |
? | |
3.2.1.4 | cellulose + H2O | the substrate position is fixed by the alignment of one cellobiose unit between the two aromatic amino acid residues at subsites +1 and +2. During the enzyme reaction, the glucose structure of cellulose substrates is distorted at subsite -1, and the beta-1,4-glucoside bond between glucose moieties is twisted between subsites -1 and +1. Subsite -2 specifically recognizes the glucose residue, but recognition by subsites +1 and +2 is loose during the enzyme reaction. Analysis of the enzyme-substrate structure suggests that an incoming water molecule, essential for hydrolysis during the retention process, might be introduced to the cleavage position after the cellobiose product at subsites +1 and +2 is released from the active site | Pyrococcus horikoshii OT-3 | cellobiose + ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.4 | PH1171 | - |
Pyrococcus horikoshii |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.4 | 85 | - |
assay at | Pyrococcus horikoshii |
3.2.1.4 | 100 | - |
optimal temperature is above 100°C | Pyrococcus horikoshii |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.4 | 5.5 | - |
assay at | Pyrococcus horikoshii |