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Literature summary extracted from

  • Lee, J.H.; Hyun, Y.J.; Kim, D.H.
    Cloning and characterization of alpha-L-arabinofuranosidase and bifunctional alpha-L-arabinopyranosidase/beta-D-galactopyranosidase from Bifidobacterium longum H-1 (2011), J. Appl. Microbiol., 111, 1097-1107.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.55 expressed in Escherichia coli BL21(DE3) cells Bifidobacterium longum

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.55 Ba2+ 68% residual activity at 1 mM Bifidobacterium longum
3.2.1.55 Co2+ 54.4% residual activity at 1 mM Bifidobacterium longum
3.2.1.55 Cu2+ 7% residual activity at 1 mM Bifidobacterium longum
3.2.1.55 Fe2+ 81.3% residual activity at 1 mM Bifidobacterium longum
3.2.1.55 Mg2+ 80.2% residual activity at 1 mM Bifidobacterium longum
3.2.1.55 Ni2+ 85.1% residual activity at 1 mM Bifidobacterium longum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.55 0.21
-
 4-nitrophenyl alpha-L-arabinofuranoside in 50 mM sodium acetate buffer (pH 5.5), at 37°C Bifidobacterium longum
3.2.1.55 1.73
-
 ginsenoside Rc in 50 mM sodium acetate buffer (pH 5.5), at 37°C Bifidobacterium longum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.55 Ca2+ 109.4% relative activity at 1 mM Bifidobacterium longum
3.2.1.55 Na+ the enzyme activity is unaffected by NaCl concentration in the range of 0-1 mM Bifidobacterium longum

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.55 Bifidobacterium longum E7CY70
-
-
3.2.1.55 Bifidobacterium longum H-1 E7CY70
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.55 Ni2+-charged HiTrap IMAC column chromatography Bifidobacterium longum

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 2.64
-
 crude extract, using 4-nitrophenyl alpha-L-arabinofuranoside as substrate, in 50 mM sodium acetate buffer (pH 5.5), at 37°C Bifidobacterium longum
3.2.1.55 71.36
-
 after 26fold purification, using 4-nitrophenyl alpha-L-arabinofuranoside as substrate, in 50 mM sodium acetate buffer (pH 5.5), at 37°C Bifidobacterium longum

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 100% activity Bifidobacterium longum 4-nitrophenol + alpha-L-arabinofuranose
-
 ?
3.2.1.55 4-nitrophenyl alpha-L-arabinofuranoside + H2O 100% activity Bifidobacterium longum H-1 4-nitrophenol + alpha-L-arabinofuranose
-
 ?
3.2.1.55 ginsenoside Rc + H2O 10.5% activity compared to 4-nitrophenyl alpha-L-arabinofuranoside Bifidobacterium longum ginsenoside Rd + L-arabinofuranose
-
 ?
3.2.1.55 ginsenoside Rc + H2O 10.5% activity compared to 4-nitrophenyl alpha-L-arabinofuranoside Bifidobacterium longum H-1 ginsenoside Rd + L-arabinofuranose
-
 ?
3.2.1.55 additional information the enzyme does not hydrolyse 4-nitrophenyl alpha-L-arabinopyranoside, 4-nitrophenyl beta-L-arabinopyranoside, 4-nitrophenyl beta-L-arabinofuranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl beta-D-galactopyranoside, and ginsenoside Rb2 Bifidobacterium longum ?
-
 ?
3.2.1.55 additional information the enzyme does not hydrolyse 4-nitrophenyl alpha-L-arabinopyranoside, 4-nitrophenyl beta-L-arabinopyranoside, 4-nitrophenyl beta-L-arabinofuranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl beta-D-galactopyranoside, and ginsenoside Rb2 Bifidobacterium longum H-1 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.55 AfuB
-
 Bifidobacterium longum
3.2.1.55 alpha-L-arabinofuranosidase
-
 Bifidobacterium longum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.55 57
-
 when incubated for 15 min at pH 7.0 Bifidobacterium longum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.55 4.7
-
 at 37°C Bifidobacterium longum