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Threonine-phosphate decarboxylase

Part of the Springer Handbook of Enzymes book series (HDBKENZYMES, volume S7)

Keywords

Escherichia Coli Molecular Weight Biosynthetic Pathway Living Organism Structural Study 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. [1]
    Cheong, C.G.; Bauer, C.B.; Brushaber, K.R.; Escalante-Semerena, J.C.; Rayment, I.: Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica. Biochemistry, 41, 4798–4808 (2002)CrossRefPubMedGoogle Scholar
  2. [2]
    Brushaber, K.R.; O’Toole, G.A.; Escalante-Semerena, J.C.: CobD, a novel enzyme with L-threonine-O-3-phosphate decarboxylase activity, is responsible for the synthesis of (R)-1-amino-2-propanol O-2-phosphate, a proposed new intermediate in cobalamin biosynthesis in Salmonella typhimurium LT2. J. Biol. Chem., 273, 2684–2691 (1998)CrossRefPubMedGoogle Scholar
  3. [3]
    Cheong, C.G.; Escalante-Semerena, J.C.; Rayment, I.: Structural studies of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica: The apo, substrate, and product-aldimine complexes. Biochemistry, 41, 9079–9089 (2002)CrossRefPubMedGoogle Scholar

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© Springer-Verlag Berlin Heidelberg 2010

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