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Literature summary extracted from

  • Alhassid, A.; Ben-David, A.; Tabachnikov, O.; Libster, D.; Naveh, E.; Zolotnitsky, G.; Shoham, Y.; Shoham, G.
    Crystal structure of an inverting GH 43 1,5-alpha-L-arabinanase from Geobacillus stearothermophilus complexed with its substrate (2009), Biochem. J., 422, 73-82.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.99 gene abnB, expression of wild-type and mutant enzymes Geobacillus stearothermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.99 purified recombinant wild-type enzyme, and mutant enzyme E201A in complex with arabinotriose, hanging drop vapour diffusion, 0.0025-0.003 ml of protein solution with 6.5-13 mg/ml protein is mixed with an equal volume of precipitant solution containing 1.7 M lithium sulfate, 0.1 M Tris buffer, pH 7.5, and 15% v/v glycerol for the wild-type enzyme, and 1.9 M lithium sulfate, 0.1 M Tris buffer, pH 8.5, and 4% w/v PEG 400 for the mutant enzyme, X-ray diffraction structure determination and analysis, molecular replacement Geobacillus stearothermophilus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.99 D147A site-directed mutagenesis, structure comparison with the wild-type enzyme Geobacillus stearothermophilus
3.2.1.99 E201A site-directed mutagenesis, structure comparison with the wild-type enzyme Geobacillus stearothermophilus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.99 Geobacillus stearothermophilus B3EYM8 gene abnB
-
3.2.1.99 Geobacillus stearothermophilus T-6 B3EYM8 gene abnB
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.99 recombinant wild-type and mutant enzymes Geobacillus stearothermophilus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.99 alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O = alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose three catalytic carboxylates: Asp27, the general base, Glu201, the general acid, and Asp147, the pKa modulator, substrate binding structure and catalytic mechanism, overview Geobacillus stearothermophilus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.99 linear arabinan + H2O
-
 Geobacillus stearothermophilus ?
-
 ?
3.2.1.99 linear arabinan + H2O
-
 Geobacillus stearothermophilus T-6 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.99 More the enzyme belongs to the glycoside hydrolase family 43, GH43 Geobacillus stearothermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.99 40
-
 assay at Geobacillus stearothermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.99 7
-
 assay at Geobacillus stearothermophilus