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Literature summary for 4.1.2.40 extracted from

  • Liotard, B.; Sygusch, J.
    Purification, crystallization and preliminary X-ray analysis of native and selenomethionine class I tagatose-1,6-bisphosphate aldolase from Streptococcus pyogenes (2004), Acta Crystallogr. Sect. D, D60, 528-530.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
recombinant, orthorhombic crystals suitable for structural analysis are obtained by the hanging-drop vapour-diffusion method for the native enzyme and the selenomethionine derivative. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 63.7, b = 108.1, c = 238.7 A for the native form and a = 64.1, b = 108.3, c = 239.8 A for the selenomethionine derivative. The asymmetric unit contains four protomers Streptococcus pyogenes

General Stability

General Stability Organism
native protein crystals can be stored for several months without degradation, crystals of the selenomethionine enzyme are degraded within a few weeks Streptococcus pyogenes

Organism

Organism UniProt Comment Textmining
Streptococcus pyogenes
-
recombinant
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Streptococcus pyogenes

Synonyms

Synonyms Comment Organism
tagatose-1,6-bisphosphate aldolase
-
Streptococcus pyogenes