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Literature summary for 4.1.2.40 extracted from

  • Lowkam, C.; Liotard, B.; Sygusch, J.
    Structure of a class I tagatose-1,6-biphosphate aldolase: Study into an apparent loss of stereospecificity (2010), J. Biol. Chem., 5, 21143-21152.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
plasmid pKK-223-3 with T7 IPTG-inducible promoter and coding for the lacD2 gene product tagatose-1-6-biphosphate aldolase 2 transformed and overexpressed using the Escherichia coli JM109 strain Streptococcus pyogenes

Crystallization (Commentary)

Crystallization (Comment) Organism
native enzyme and native enzyme in complex with dihydroxyacetone-P, by the hanging drop method. Native free TBP aldolase crystallized in the P212121 space group with four protomers in the asymmetric unit and diffracted to 1.87 A resolution. Folding of the polypeptide chain of TBP aldolase corresponds to a (alpha/beta)8 or TIM barrel fold. The liganded crystal structure is isomorphous with the crystal structure of the native aldolase and diffracted to 1.92 A resolution Streptococcus pyogenes

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
gel filtration Streptococcus pyogenes

Organism

Organism UniProt Comment Textmining
Streptococcus pyogenes
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by anion-exchange chromatography and gel filtration, to homogeneity Streptococcus pyogenes

Subunits

Subunits Comment Organism
dimer gel filtration Streptococcus pyogenes

Synonyms

Synonyms Comment Organism
tagatose-1,6-biphosphate aldolase 2
-
Streptococcus pyogenes
TBP aldolase
-
Streptococcus pyogenes