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Literature summary for 3.2.1.22 extracted from

  • Fredslund, F.; Hachem, M.A.; Larsen, R.J.; S?rensen, P.G.; Coutinho, P.M.; Lo Leggio, L.; Svensson, B.
    Crystal structure of alpha-galactosidase from Lactobacillus acidophilus NCFM: insight into tetramer formation and substrate binding (2011), J. Mol. Biol., 412, 466-480.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
the crystal structure of alpha-galactosidase from Lactobacillus acidophilus NCFM (LaMel36A) is determined by single-wavelength anomalous dispersion. In addition, a 1.58-A-resolution crystallographic complex with alpha-D-galactose at substrate binding subsite-1 is determined. LaMel36A has a largeN-terminal twisted beta-sandwich domain, connected by a long alpha-helix to the catalytic (beta/alpha)8-barrel domain, and a C-terminal beta-sheet domain Lactobacillus acidophilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
86000
-
SDS-PAGE Lactobacillus acidophilus
260000
-
gel filtration Lactobacillus acidophilus

Organism

Organism UniProt Comment Textmining
Lactobacillus acidophilus Q7WWP9
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl-alpha-D-galactopyranoside + H2O
-
Lactobacillus acidophilus 4-nitrophenol + alpha-D-galactopyranose
-
?

Subunits

Subunits Comment Organism
tetramer crystal structure, four identical monomers form a tightly packed tetramer where three monomers contribute to the structural integrity of the active site in each monomer Lactobacillus acidophilus

Synonyms

Synonyms Comment Organism
alpha-galactosidase
-
Lactobacillus acidophilus
LaMel36A
-
Lactobacillus acidophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Lactobacillus acidophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
assay at Lactobacillus acidophilus