Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli strain BL21(DE3) | Pyrococcus horikoshii |
Crystallization (Comment) | Organism |
---|---|
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 |
Protein Variants | Comment | Organism |
---|---|---|
Q306A | 25% of the activity with avicel as compared to wild-type enzyme | Pyrococcus horikoshii |
W377A | complete loss of activity with avicel | Pyrococcus horikoshii |
W82A | 75% of the activity with avicel as compared to wild-type enzyme | Pyrococcus horikoshii |
Y299F | complete loss of activity with avicel | Pyrococcus horikoshii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus horikoshii | O58925 | - |
- |
Pyrococcus horikoshii OT-3 | O58925 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Pyrococcus horikoshii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
avicel + H2O | - |
Pyrococcus horikoshii | cellobiose + ? | - |
? | |
avicel + H2O | - |
Pyrococcus horikoshii OT-3 | cellobiose + ? | - |
? | |
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 + ? | - |
? | |
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 + ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PH1171 | - |
Pyrococcus horikoshii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
85 | - |
assay at | Pyrococcus horikoshii |
100 | - |
optimal temperature is above 100°C | Pyrococcus horikoshii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | - |
assay at | Pyrococcus horikoshii |