Crystallization (Comment) | Organism |
---|---|
purified recombinant enzyme, by hanging drop vapour diffusion method, room temperature, 0.001 ml of protein solution containing 5 mg/ml protein is mixed with 0.001 ml of reservoir solution containing 30% v/v 2-methyl-2,4-pentanediol, 20 mM CaCl2, and 100 mM sodium acetate, pH 4.6, and equilibrated against 1 ml of reservoir solution, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement method | Halalkalibacterium halodurans |
Protein Variants | Comment | Organism |
---|---|---|
V169A/I170F/D171N | site-directed mutagenesis, the mutant shows a pH optimum of pH 7.0, incontrast to the wild-type enzyme which has an optimum at pH 9.0-9.5 | Halalkalibacterium halodurans |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Halalkalibacterium halodurans | the alkaliphilic bacterium produces an alkaline active xylanase, the alkaline active xylanases have highly acidic surfaces and fewer solvent exposed alkali labile residues, mechanisms of high pH stability and catalysis, overview | ? | - |
? | |
additional information | Halalkalibacterium halodurans S7 | the alkaliphilic bacterium produces an alkaline active xylanase, the alkaline active xylanases have highly acidic surfaces and fewer solvent exposed alkali labile residues, mechanisms of high pH stability and catalysis, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Halalkalibacterium halodurans | Q17TM8 | - |
- |
Halalkalibacterium halodurans S7 | Q17TM8 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the alkaliphilic bacterium produces an alkaline active xylanase, the alkaline active xylanases have highly acidic surfaces and fewer solvent exposed alkali labile residues, mechanisms of high pH stability and catalysis, overview | Halalkalibacterium halodurans | ? | - |
? | |
additional information | residues Val169, Ile170 and Asp171 are important to hydrolyze xylan at high pH | Halalkalibacterium halodurans | ? | - |
? | |
additional information | the alkaliphilic bacterium produces an alkaline active xylanase, the alkaline active xylanases have highly acidic surfaces and fewer solvent exposed alkali labile residues, mechanisms of high pH stability and catalysis, overview | Halalkalibacterium halodurans S7 | ? | - |
? | |
additional information | residues Val169, Ile170 and Asp171 are important to hydrolyze xylan at high pH | Halalkalibacterium halodurans S7 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme has the common eightfold TIM-barrel structure of family 10 xylanases, however, unlike non-alkaline active xylanases, it has a highly negatively charged surface and a deeper active site cleft, structure comparisons, overview | Halalkalibacterium halodurans |
Synonyms | Comment | Organism |
---|---|---|
alkaline active xylanase | - |
Halalkalibacterium halodurans |
xylanase | - |
Halalkalibacterium halodurans |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9 | 9.5 | residues Val169, Ile170 and Asp171 are important to hydrolyze xylan at high pH, mechanisms of high pH stability and catalysis, overview | Halalkalibacterium halodurans |