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Literature summary extracted from

  • Mamo, G.; Thunnissen, M.; Hatti-Kaul, R.; Mattiasson, B.
    An alkaline active xylanase: insights into mechanisms of high pH catalytic adaptation (2009), Biochimie, 91, 1187-1196.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.8 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

EC Number Protein Variants Comment Organism
3.2.1.8 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/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.8 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 ?
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 ?
3.2.1.8 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 ?
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 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.8 Halalkalibacterium halodurans Q17TM8
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-
3.2.1.8 Halalkalibacterium halodurans S7 Q17TM8
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.8 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 ?
-
 ?
3.2.1.8 additional information residues Val169, Ile170 and Asp171 are important to hydrolyze xylan at high pH Halalkalibacterium halodurans ?
-
 ?
3.2.1.8 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 ?
-
 ?
3.2.1.8 additional information residues Val169, Ile170 and Asp171 are important to hydrolyze xylan at high pH Halalkalibacterium halodurans S7 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.8 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

EC Number Synonyms Comment Organism
3.2.1.8 alkaline active xylanase
-
 Halalkalibacterium halodurans
3.2.1.8 xylanase
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 Halalkalibacterium halodurans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.8 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