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Literature summary extracted from

  • Arab-Jaziri, F.; Bissaro, B.; Barbe, S.; Saurel, O.; Debat, H.; Dumon, C.; Gervais, V.; Milon, A.; Andre, I.; Faure, R.; O'Donohue, M.J.
    Functional roles of H98 and W99 and beta2alpha2 loop dynamics in the alpha-L-arabinofuranosidase from Thermobacillus xylanilyticus (2012), FEBS J., 279, 3598-3611.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.55 H98A site-directed mutagenesis, the mutant shows affected kinetics and reduced activity compared to the wild-type enzyme Thermobacillus xylanilyticus
3.2.1.55 H98A/W99A site-directed mutagenesis, the mutant shows affected kinetics and reduced activity compared to the wild-type enzyme Thermobacillus xylanilyticus
3.2.1.55 H98F site-directed mutagenesis, the mutant shows affected kinetics and reduced activity compared to the wild-type enzyme Thermobacillus xylanilyticus
3.2.1.55 H98F/W99F site-directed mutagenesis, the mutant shows affected kinetics and reduced activity compared to the wild-type enzyme Thermobacillus xylanilyticus
3.2.1.55 W99A site-directed mutagenesis, the mutation causes the loss of a hydrogen bond and leads to an alternative binding mode that is detrimental for catalysis, altered binding of the aglycon motif in the active site, the mutant shows affected kinetics and reduced activity compared to the wild-type enzyme Thermobacillus xylanilyticus
3.2.1.55 W99F site-directed mutagenesis, the mutant shows affected kinetics, reduced activity, and altered binding of the aglycon motif in the active site 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 0.72
-
 4-nitrophenyl-alpha-L-arabinofuranoside wild-type enzyme, pH 5.8, 60°C Thermobacillus xylanilyticus
3.2.1.55 0.87
-
 4-nitrophenyl-alpha-L-arabinofuranoside mutant H98F, pH 5.8, 60°C Thermobacillus xylanilyticus
3.2.1.55 1.5 2 4-nitrophenyl-alpha-L-arabinofuranoside mutant H98A, pH 5.8, 60°C Thermobacillus xylanilyticus
3.2.1.55 3.4
-
 4-nitrophenyl-alpha-L-arabinofuranoside mutant H98F/W99F, pH 5.8, 60°C Thermobacillus xylanilyticus
3.2.1.55 4.2
-
 4-nitrophenyl-alpha-L-arabinofuranoside mutant W99F, pH 5.8, 60°C Thermobacillus xylanilyticus
3.2.1.55 9.1
-
 4-nitrophenyl-alpha-L-arabinofuranoside mutant W99A, pH 5.8, 60°C Thermobacillus xylanilyticus
3.2.1.55 15
-
 4-nitrophenyl-alpha-L-arabinofuranoside mutant H98A/W99A, pH 5.8, 60°C Thermobacillus xylanilyticus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.55 additional information Thermobacillus xylanilyticus alpha-L-arabinofuranosidases are exo-acting glycoside hydrolases that catalyse the hydrolysis of terminal non-reducing alpha-L-arabinofuranosyl moieties in oligosaccharides and polysaccharides through the cleavage of 1->2 and/or 1->3 glycosidic bonds ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.55 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 the substrate binding process is driven by favourable entropy, which is linked to the movement of the beta2alpha2 loop. Loop closure relocates the solvent-exposed W99 into a buried location, allowing its involvement in substrate binding and in the formation of a functional active site. Residue H98 has a role in the dynamic formation as catalytically operational active site, which may be a specific feature of a subset of GH51 arabinofuranosidases Thermobacillus xylanilyticus 4-nitrophenol + L-arabinofuranose
-
 ?
3.2.1.55 additional information alpha-L-arabinofuranosidases are exo-acting glycoside hydrolases that catalyse the hydrolysis of terminal non-reducing alpha-L-arabinofuranosyl moieties in oligosaccharides and polysaccharides through the cleavage of 1->2 and/or 1->3 glycosidic bonds Thermobacillus xylanilyticus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.55 More three-dimensional structure of the enzyme, overview Thermobacillus xylanilyticus

Synonyms

EC Number Synonyms Comment Organism
3.2.1.55 ABF
-
 Thermobacillus xylanilyticus
3.2.1.55 alpha-L-arabinofuranosidase
-
 Thermobacillus xylanilyticus
3.2.1.55 GH51 arabinofuranosidase
-
 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 77
-
 4-nitrophenyl-alpha-L-arabinofuranoside mutant W99F, pH 5.8, 60°C Thermobacillus xylanilyticus
3.2.1.55 97
-
 4-nitrophenyl-alpha-L-arabinofuranoside mutant H98F/W99F, pH 5.8, 60°C Thermobacillus xylanilyticus
3.2.1.55 137
-
 4-nitrophenyl-alpha-L-arabinofuranoside mutant W99A, pH 5.8, 60°C Thermobacillus xylanilyticus
3.2.1.55 154
-
 4-nitrophenyl-alpha-L-arabinofuranoside mutant H98A/W99A, pH 5.8, 60°C Thermobacillus xylanilyticus
3.2.1.55 192
-
 4-nitrophenyl-alpha-L-arabinofuranoside mutant H98A, pH 5.8, 60°C Thermobacillus xylanilyticus
3.2.1.55 199
-
 4-nitrophenyl-alpha-L-arabinofuranoside mutant H98F, pH 5.8, 60°C Thermobacillus xylanilyticus
3.2.1.55 575
-
 4-nitrophenyl-alpha-L-arabinofuranoside wild-type enzyme, pH 5.8, 60°C Thermobacillus xylanilyticus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.55 5.8
-
 assay at Thermobacillus xylanilyticus

General Information

EC Number General Information Comment Organism
3.2.1.55 evolution the enzyme belongs to the family 51 glycoside hydrolase, GH51 Thermobacillus xylanilyticus
3.2.1.55 additional information functional role of the mobile beta2alpha2 loop, especially of loop residues H98 and W99, analysis by site-directed mutagenesis, isothermal titration calorimetry, saturation transfer difference NMR spectroscopy, and molecular dynamics simulation, three-dimensional structure of the enzyme and its active site, overview Thermobacillus xylanilyticus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.1.55 9.8
-
 4-nitrophenyl-alpha-L-arabinofuranoside mutant H98A/W99A, pH 5.8, 60°C Thermobacillus xylanilyticus
3.2.1.55 15.1
-
 4-nitrophenyl-alpha-L-arabinofuranoside mutant W99A, pH 5.8, 60°C Thermobacillus xylanilyticus
3.2.1.55 18
-
 4-nitrophenyl-alpha-L-arabinofuranoside mutant W99F, pH 5.8, 60°C Thermobacillus xylanilyticus
3.2.1.55 28.2
-
 4-nitrophenyl-alpha-L-arabinofuranoside mutant H98F/W99F, pH 5.8, 60°C Thermobacillus xylanilyticus
3.2.1.55 126
-
 4-nitrophenyl-alpha-L-arabinofuranoside mutant H98A, pH 5.8, 60°C Thermobacillus xylanilyticus
3.2.1.55 228
-
 4-nitrophenyl-alpha-L-arabinofuranoside mutant H98F, pH 5.8, 60°C Thermobacillus xylanilyticus
3.2.1.55 795
-
 4-nitrophenyl-alpha-L-arabinofuranoside wild-type enzyme, pH 5.8, 60°C Thermobacillus xylanilyticus