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Literature summary extracted from

  • Debeche, T.; Bliard, C.; Debeire, P.; O'Donohue, M.J.
    Probing the catalytically essential residues of the alpha-L-arabinofuranosidase from Thermobacillus xylanilyticus (2002), Protein Eng., 15, 21-28.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.55 expression of wild-type and mutant enzymes in Escherichia coli BL21(DE3) Thermobacillus xylanilyticus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.55 D55A site-directed mutagenesis, activity is similar to wild-type enzyme activity Thermobacillus xylanilyticus
3.2.1.55 E112A site-directed mutagenesis, activity is similar to wild-type enzyme activity Thermobacillus xylanilyticus
3.2.1.55 E143A site-directed mutagenesis, activity is similar to wild-type enzyme activity Thermobacillus xylanilyticus
3.2.1.55 E176A site-directed mutagenesis, exchange of the acid-base residue, nearly inactive mutant, 8925fold reduced activity compared to the wild-type enzyme Thermobacillus xylanilyticus
3.2.1.55 E176D site-directed mutagenesis, exchange of the acid-base residue, mutant enzyme shows altered kinetic properties compared to the wild-type enzyme Thermobacillus xylanilyticus
3.2.1.55 E176Q site-directed mutagenesis, exchange of the acid-base residue, mutant enzyme is insensitive to pH Thermobacillus xylanilyticus
3.2.1.55 E28A site-directed mutagenesis, nearly inactive mutant, 5950fold reduced activity compared to the wild-type enzyme Thermobacillus xylanilyticus
3.2.1.55 E28A/E176A site-directed mutagenesis, completely inactive mutant Thermobacillus xylanilyticus
3.2.1.55 E28D site-directed mutagenesis, mutant enzyme shows altered kinetic properties compared to the wild-type enzyme Thermobacillus xylanilyticus
3.2.1.55 E28Q site-directed mutagenesis, mutant enzyme shows altered kinetic properties compared to the wild-type enzyme Thermobacillus xylanilyticus
3.2.1.55 E28Q site-directed mutagenesis, mutant enzyme shows increased sensitivity to pH and a lower pH optimum compared to the wild-type enzyme Thermobacillus xylanilyticus
3.2.1.55 E298A site-directed mutagenesis, nearly inactive mutant, 178500fold reduced activity compared to the wild-type enzyme Thermobacillus xylanilyticus
3.2.1.55 E298D site-directed mutagenesis, mutant enzyme shows altered kinetic properties compared to the wild-type enzyme Thermobacillus xylanilyticus
3.2.1.55 E298Q site-directed mutagenesis, mutant enzyme shows increased sensitivity to pH and a lower pH optimum compared to the wild-type enzyme Thermobacillus xylanilyticus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.55 additional information
-
 additional information kinetics, wild-type and mutant enzymes, influence of sodium formate and sodium azide, overview Thermobacillus xylanilyticus
3.2.1.55 0.3
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.8, 60°C, mutant E176D Thermobacillus xylanilyticus
3.2.1.55 0.41
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.8, 60°C, mutant E176Q Thermobacillus xylanilyticus
3.2.1.55 0.43
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.8, 60°C, mutant E176A Thermobacillus xylanilyticus
3.2.1.55 0.51
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.8, 60°C, mutant E28D Thermobacillus xylanilyticus
3.2.1.55 0.7
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.8, 60°C, wild-type enzyme Thermobacillus xylanilyticus
3.2.1.55 0.91
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.8, 60°C, mutant E298Q Thermobacillus xylanilyticus
3.2.1.55 1.04
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.8, 60°C, mutant E28A Thermobacillus xylanilyticus
3.2.1.55 1.11
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.8, 60°C, mutant E298D Thermobacillus xylanilyticus
3.2.1.55 34
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.8, 60°C, mutant E28Q Thermobacillus xylanilyticus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.55 Sodium azide activates mutant enzymes: E28A 6fold, E176A 7fold, and E298A 67fold, at up to 0.5 M, no activation of the wild-type enzyme Thermobacillus xylanilyticus
3.2.1.55 Sodium formate activates mutant enzymes: E28A 60fold at 4 M, E176A 4fold at 4 M, and E298A 36fold at 0.5-1.0 M, no activation of the wild-type enzyme Thermobacillus xylanilyticus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.55 56102
-
 x * 56102, sequence calculation Thermobacillus xylanilyticus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.55 Thermobacillus xylanilyticus O69262
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.55 recombinant wild-type and mutant enzymes from Escherichia coli Thermobacillus xylanilyticus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.55 1,5-alpha-L-arabinofuranohexaose + 5 H2O = 6 alpha-L-arabinofuranose reaction mechanism, active site structure, Glu28, the catalytic nucleophil, Glu176, the acid-base residue, and Glu298, responsible for modulation of the ionization state of the acid-base and for substrate fixation, are important for catalytic activity Thermobacillus xylanilyticus
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.55 347
-
 purified recombinant mutant D55A Thermobacillus xylanilyticus
3.2.1.55 356
-
 purified recombinant mutant E112A Thermobacillus xylanilyticus
3.2.1.55 357
-
 purified recombinant wild-type enzyme Thermobacillus xylanilyticus
3.2.1.55 361
-
 purified recombinant mutant E176A Thermobacillus xylanilyticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.55 4-nitrophenyl alpha-L-arabinofuranoside + H2O hydrolysis of the substrate with retention of the anomeric configuration Thermobacillus xylanilyticus 4-nitrophenol + alpha-L-arabinofuranose
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.55 ? x * 56102, sequence calculation Thermobacillus xylanilyticus

Synonyms

EC Number Synonyms Comment Organism
3.2.1.55 alpha-L-arabinofuranosidase D3
-
 Thermobacillus xylanilyticus
3.2.1.55 More enzyme belongs to family 51 of the glycosyl hydrolase classification as part of the 4/7 glycosyl hydrolase superfamily Thermobacillus xylanilyticus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.55 60
-
 assay at Thermobacillus xylanilyticus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.55 0.39
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.8, 60°C, mutant E176A Thermobacillus xylanilyticus
3.2.1.55 0.53
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.8, 60°C, mutant E298D Thermobacillus xylanilyticus
3.2.1.55 0.63
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.8, 60°C, mutant E28A Thermobacillus xylanilyticus
3.2.1.55 0.65
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.8, 60°C, mutant E176D Thermobacillus xylanilyticus
3.2.1.55 1.04
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.8, 60°C, mutant E298Q Thermobacillus xylanilyticus
3.2.1.55 1.08
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.8, 60°C, mutant E28D Thermobacillus xylanilyticus
3.2.1.55 5.95
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.8, 60°C, mutant E28Q Thermobacillus xylanilyticus
3.2.1.55 36.7
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.8, 60°C, mutant E176Q Thermobacillus xylanilyticus
3.2.1.55 4100
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.8, 60°C, wild-type enzyme Thermobacillus xylanilyticus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.55 5.6 6.2
-
 Thermobacillus xylanilyticus