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Literature summary for 3.2.1.4 extracted from

  • Kim, H.; Ishikawa, K.
    Functional analysis of hyperthermophilic endocellulase from Pyrococcus horikoshii by crystallographic snapshots (2011), Biochem. J., 437, 223-230 .
    View publication on PubMed
Search for more literature for 3.2.1.4

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli strain BL21(DE3) Pyrococcus horikoshii

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapour diffusion method. The crystal of the enzyme–ligand 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

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

Organism UniProt Comment Textmining
Pyrococcus horikoshii O58925
-
-
Pyrococcus horikoshii OT-3 O58925
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus horikoshii

Substrates and Products (Substrate)

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

Synonyms Comment Organism
PH1171
-
 Pyrococcus horikoshii

Temperature Optimum [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
 assay at Pyrococcus horikoshii