• Corpus ID: 40001259

1 STRUCTURE OF A CLASS I TAGATOSE-1 , 6-BIPHOSPHATE ALDOLASE : STUDY INTO AN APPARENT LOSS OF STEREOSPECIFICITY

@inproceedings{LowKam20101SO,
  title={1 STRUCTURE OF A CLASS I TAGATOSE-1 , 6-BIPHOSPHATE ALDOLASE : STUDY INTO AN APPARENT LOSS OF STEREOSPECIFICITY},
  author={Clotilde LowKam and Brigitte Liotard and Jurgen Sygusch},
  year={2010}
}
Tagatose-1,6-biphosphate (TBP) aldolase from Streptococcus pyogenes is a class I aldolase that exhibits a remarkable lack of chiral discrimination with respect to the configuration of hydroxyl groups at both C3 and C4 positions. The enzyme catalyzes the reversible cleavage of four diastereoisomers: fructose-1,6-bisphosphate (FBP), psicose-1,6-bis-phosphate, sorbose-1,6bisphosphate and tagatose-1,6-bisphosphate to dihydroxyacetone-P and D-glyceraldehyde 3-P with high catalytic efficiency. To… 

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