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Literature summary extracted from

  • Maehara, T.; Fujimoto, Z.; Ichinose, H.; Michikawa, M.; Harazono, K.; Kaneko, S.
    Crystal structure and characterization of the glycoside hydrolase family 62 alpha-L-arabinofuranosidase from Streptomyces coelicolor (2014), J. Biol. Chem., 289, 7962-7972.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.55 recombinant expression of wild-type and mutant enzymes in Streptomyces lividans strain 1326 and secretion to the culture medium Streptomyces coelicolor

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.55 purified recomnbinant enzyme free or complexed with mercury derivative, L-arabinose, or xylooligosaccharides, sitting drop vapour diffusion method, mixing of 0.0012 ml of 8.3 mg/ml protein in 2 mM Tris-HCl buffer, pH 7.0, and 20 mM NaCl, with 0.001 ml of reservoir solution containing 20% w/v PEG 3350 and 0.2 M tripotassium citrate, pH 8.3, 20°C, X-ray diffraction structure determination and analysis at 1.4-2.1 A resolution, model building and molecular refinement Streptomyces coelicolor

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.55 D165E site-directed mutagenesis Streptomyces coelicolor
3.2.1.55 D165N site-directed mutagenesis Streptomyces coelicolor
3.2.1.55 D202N site-directed mutagenesis, inactive mutant Streptomyces coelicolor
3.2.1.55 E324Q site-directed mutagenesis Streptomyces coelicolor
3.2.1.55 E361Q site-directed mutagenesis, inactive mutant Streptomyces coelicolor
3.2.1.55 N425Q site-directed mutagenesis Streptomyces coelicolor
3.2.1.55 N462Q site-directed mutagenesis, the mutant shows 30% reduced activity compared to the wild-type enzyme Streptomyces coelicolor
3.2.1.55 W233A site-directed mutagenesis Streptomyces coelicolor
3.2.1.55 W233F site-directed mutagenesis Streptomyces coelicolor
3.2.1.55 W233Y site-directed mutagenesis Streptomyces coelicolor
3.2.1.55 W270A site-directed mutagenesis, the mutant shows 70% reduced activity compared to the wild-type enzyme Streptomyces coelicolor
3.2.1.55 W270F site-directed mutagenesis, the mutant shows 70% reduced activity compared to the wild-type enzyme Streptomyces coelicolor
3.2.1.55 W270Y site-directed mutagenesis, the mutant shows 50% reduced activity compared to the wild-type enzyme Streptomyces coelicolor
3.2.1.55 Y424A site-directed mutagenesis Streptomyces coelicolor
3.2.1.55 Y424F site-directed mutagenesis Streptomyces coelicolor
3.2.1.55 Y424W site-directed mutagenesis Streptomyces coelicolor
3.2.1.55 Y461A site-directed mutagenesis, the mutant shows 20% reduced activity compared to the wild-type enzyme Streptomyces coelicolor
3.2.1.55 Y461F site-directed mutagenesis, the mutant shows 80% reduced activity compared to the wild-type enzyme Streptomyces coelicolor
3.2.1.55 Y461W site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Streptomyces coelicolor

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 of mutant enzymes, overview Streptomyces coelicolor
3.2.1.55 1.9
-
 4-nitrophenyl-alpha-L-arabinofuranoside ph 5.5, 37°C, recombinant wild-type enzyme Streptomyces coelicolor
3.2.1.55 7.3
-
 wheat L-arabinoxylan ph 5.5, 37°C, recombinant wild-type enzyme Streptomyces coelicolor

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.55 extracellular
-
 Streptomyces coelicolor
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.55 L-arabinoxylan + H2O Streptomyces coelicolor the enzyme efficiently removes the alpha-L-arabinosyl substituents from arabinoxylan ?
-
 ?
3.2.1.55 L-arabinoxylan + H2O Streptomyces coelicolor A3(2) the enzyme efficiently removes the alpha-L-arabinosyl substituents from arabinoxylan ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.55 Streptomyces coelicolor O54161
-
-
3.2.1.55 Streptomyces coelicolor A3(2) O54161
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.55 recombinant wild-type and mutant enzymes from Streptomyces lividans strain 1326 culture medium by affinity chromatography using lactosyl-Sepharose, dialysis and ultrafiltration Streptomyces coelicolor

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
-
 Streptomyces coelicolor 4-nitrophenol + L-arabinofuranose
-
 ?
3.2.1.55 4-nitrophenyl alpha-L-arabinofuranoside + H2O
-
 Streptomyces coelicolor A3(2) 4-nitrophenol + L-arabinofuranose
-
 ?
3.2.1.55 L-arabinoxylan + H2O the enzyme efficiently removes the alpha-L-arabinosyl substituents from arabinoxylan Streptomyces coelicolor ?
-
 ?
3.2.1.55 L-arabinoxylan + H2O the enzyme efficiently removes the alpha-L-arabinosyl substituents from arabinoxylan Streptomyces coelicolor A3(2) ?
-
 ?
3.2.1.55 additional information substrate specificity and substrate-binding mechanism, overview Streptomyces coelicolor ?
-
 ?
3.2.1.55 additional information substrate specificity and substrate-binding mechanism, overview Streptomyces coelicolor A3(2) ?
-
 ?
3.2.1.55 wheat L-arabinoxylan + H2O the enzyme efficiently removes the alpha-L-arabinosyl substituents from arabinoxylan Streptomyces coelicolor ?
-
 ?
3.2.1.55 wheat L-arabinoxylan + H2O the enzyme efficiently removes the alpha-L-arabinosyl substituents from arabinoxylan Streptomyces coelicolor A3(2) ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.55 exo-alpha-L-arabinofuranosidase UniProt Streptomyces coelicolor
3.2.1.55 ScAraf62A
-
 Streptomyces coelicolor

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.55 30 45 assay at Streptomyces coelicolor

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.55 0.02
-
 4-nitrophenyl-alpha-L-arabinofuranoside ph 5.5, 37°C, recombinant wild-type enzyme Streptomyces coelicolor
3.2.1.55 0.3
-
 wheat L-arabinoxylan ph 5.5, 37°C, recombinant wild-type enzyme Streptomyces coelicolor

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.55 5.5 6 assay at Streptomyces coelicolor

General Information

EC Number General Information Comment Organism
3.2.1.55 evolution the enzyme belongs to the family 62 glycoside hydrolase, GH62. The crystal structure comprises a carbohydrate-binding module family 13 domain at its N-terminus and a catalytic domain at its C-terminus Streptomyces coelicolor
3.2.1.55 additional information the catalytic domain is a five-bladed beta-propeller consisting of five radially oriented anti-parallel beta-sheets, substrate binding at five subsites in the catalytic cleft and an L-arabinose-binding pocket at the bottom of the cleft. Asp202 and Glu361 are catalytic residues, and Trp270, Tyr461, and Asn462 are involved in the substrate-binding site for discriminating the substrate structures Streptomyces coelicolor

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 0.011
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.5, 37°C, recombinant wild-type enzyme Streptomyces coelicolor
3.2.1.55 0.042
-
 wheat L-arabinoxylan pH 5.5, 37°C, recombinant wild-type enzyme Streptomyces coelicolor