Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.1.20 extracted from

  • Ernst, H.A.; Willemoes, M.; Lo Leggio, L.; Leonard, G.; Blum, P.; Larsen, S.
    Characterization of different crystal forms of the alpha-glucosidase MalA from Sulfolobus solfataricus (2005), Acta Crystallogr. Sect. F, 61, 1039-1042.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene malA, overexpression of wild-type and selenomethionine-labeled enzyme in Escherichia coli Saccharolobus solfataricus

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant wild-type and selenomethionine-labeled enzyme, hanging drop vapour diffusion method, 2-5 mg/ml protein in 20 mM Tris-HCl, pH 7.5, and 20 mM NaCl, 0.002 ml protein solution is mixed with 0.003 ml reservoir solution and equilibrated against 1 ml reservoir solution, different compositions of the reservoir solution result in different crystal forms, overview, X-ray diffraction structure determination and analysis of the different crystal forms at 2.5-4.2 A resolution Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
gene malA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and selenomethionine-labeled enzyme from Escherichia coli by ammonium sulfate fractionation, ion exchange chromatography, and gel filtration Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
MalA
-
Saccharolobus solfataricus
More the enzyme belongs to the alpha-glucosidase family 31 Saccharolobus solfataricus