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Literature summary extracted from

  • Siguier, B.; Haon, M.; Nahoum, V.; Marcellin, M.; Burlet-Schiltz, O.; Coutinho, P.M.; Henrissat, B.; Mourey, L.; ODonohue, M.J.; Berrin, J.G.; Tranier, S.; Dumon, C.
    First structural insights into alpha-L-arabinofuranosidases from the two GH62 glycoside hydrolase subfamilies (2014), J. Biol. Chem., 289, 5261-5273.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.55 expression of His6-tagged enzyme in Pichia pastoris strain X33 Podospora anserina
3.2.1.55 gene UM04309.1, expression of His6-tagged enzyme in Pichia pastoris strain X33 Ustilago maydis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.55 purified recombinant His-tagged enzyme free or complexed with cellotriose, method screening and optimization, hanging-drop vapor-diffusion method is chosen, mixing of equal volumes of 18 mg/ml protein in 50 mM sodium acetate, pH 5.0, and 50 mM NaCl, with reservoir solution containing 25% w/v PEG 4000, 0.2 M calcium chloride, and 0.1 M Tris, pH 8.5, 1 week, 12°C, crystal soaking in ligand solution, X-ray diffraction structure determination and analysis at 1.44-1.85 A resolution, molecular replacement method Podospora anserina
3.2.1.55 purified recombinant His-tagged enzyme free or complexed with sulfur-SAD or L-arabinose, method screening and optimization, hanging-drop vapor-diffusion method is chosen, mixing of equal volumes of 18 mg/ml protein in 50 mM sodium acetate, pH 5.0, and 50 mM NaCl, with reservoir solution containing 20% w/v PEG 3350 and 0.2 M sodium phosphate, 6 days, 12°C, soaking of crystals in ligand solution, X-ray diffraction structure determination and analysis at 1.0-1.75 A resolution, solved by the sulfur-SAD phasing method Ustilago maydis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.55 cellohexaose
-
 Podospora anserina
3.2.1.55 additional information no inhibition by cellohexaose Ustilago maydis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.55 additional information
-
 additional information Michaelis-Menten kinetics Podospora anserina
3.2.1.55 additional information
-
 additional information Michaelis-Menten kinetics Ustilago maydis
3.2.1.55 6.1
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.0, 37°C Podospora anserina
3.2.1.55 7.5
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.0, 37°C Ustilago maydis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.55 67840
-
 x * 67840, His-tagged enzyme, sequence calculation Ustilago maydis
3.2.1.55 99350
-
 x * 99350, His-tagged enzyme, sequence calculation Podospora anserina

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 Podospora anserina the enzyme efficiently removes the alpha-L-arabinosyl substituents from arabinoxylan ?
-
 ?
3.2.1.55 L-arabinoxylan + H2O Ustilago maydis the enzyme efficiently removes the alpha-L-arabinosyl substituents from arabinoxylan ?
-
 ?
3.2.1.55 L-arabinoxylan + H2O Ustilago maydis BRFM1093 the enzyme efficiently removes the alpha-L-arabinosyl substituents from arabinoxylan ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.55 Podospora anserina E2GHW5
-
-
3.2.1.55 Ustilago maydis A0A0D1BZQ4 gene UM04309.1
-
3.2.1.55 Ustilago maydis BRFM1093 A0A0D1BZQ4 gene UM04309.1
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.55 glycoprotein N-deglycosylation by glycosidase Endo-Hf Podospora anserina

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.55 recombinant His6-tagged enzyme from Pichia pastoris strain X33 Podospora anserina
3.2.1.55 recombinant His6-tagged enzyme from Pichia pastoris strain X33 Ustilago maydis

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
-
 Podospora anserina 4-nitrophenol + L-arabinofuranose
-
 ?
3.2.1.55 4-nitrophenyl alpha-L-arabinofuranoside + H2O
-
 Ustilago maydis 4-nitrophenol + L-arabinofuranose
-
 ?
3.2.1.55 4-nitrophenyl alpha-L-arabinofuranoside + H2O
-
 Ustilago maydis BRFM1093 4-nitrophenol + L-arabinofuranose
-
 ?
3.2.1.55 L-arabinoxylan + H2O the enzyme efficiently removes the alpha-L-arabinosyl substituents from arabinoxylan Podospora anserina ?
-
 ?
3.2.1.55 L-arabinoxylan + H2O the enzyme efficiently removes the alpha-L-arabinosyl substituents from arabinoxylan Ustilago maydis ?
-
 ?
3.2.1.55 L-arabinoxylan + H2O the enzyme efficiently removes the alpha-L-arabinosyl substituents from arabinoxylan Ustilago maydis BRFM1093 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.55 ? x * 67840, His-tagged enzyme, sequence calculation Ustilago maydis
3.2.1.55 ? x * 99350, His-tagged enzyme, sequence calculation Podospora anserina
3.2.1.55 More three-dimensional structure, overview Podospora anserina
3.2.1.55 More three-dimensional structure, overview Ustilago maydis

Synonyms

EC Number Synonyms Comment Organism
3.2.1.55 PaAbf62A
-
 Podospora anserina
3.2.1.55 UmAbf62A
-
 Ustilago maydis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.55 37
-
 assay at Podospora anserina
3.2.1.55 37
-
 assay at Ustilago maydis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.55 0.039
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.0, 37°C Ustilago maydis
3.2.1.55 0.38
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.0, 37°C Podospora anserina

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.55 5
-
 assay at Podospora anserina
3.2.1.55 5
-
 assay at Ustilago maydis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.55 3.4
-
 cellohexaose pH 5.0, 37°C Podospora anserina

General Information

EC Number General Information Comment Organism
3.2.1.55 evolution the enzyme belongs to the family 62 glycoside hydrolase, GH62, phylogenetic analysis. The overall three-dimensional structure of PaAbf62A reveals a five-bladed beta-propeller fold that confirms its predicted classification into clan GH-F together with GH43 alpha-L-arabinofuranosidases, structure-function relationships within the GH62 family, overview Podospora anserina
3.2.1.55 evolution the enzyme belongs to the family 62 glycoside hydrolase, GH62, phylogenetic analysis. The overall three-dimensional structure of PaAbf62A reveals a five-bladed beta-propeller fold that confirms its predicted classification into clan GH-F together with GH43 alpha-L-arabinofuranosidases, structure-function relationships within the GH62 family, overview Ustilago maydis

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 0.005
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.0, 37°C Ustilago maydis
3.2.1.55 0.062
-
 4-nitrophenyl-alpha-L-arabinofuranoside pH 5.0, 37°C Podospora anserina