Purification and characterization of eucaryotic alanine racemase acting as key enzyme in cyclosporin biosynthesis.

@article{Hoffmann1994PurificationAC,
  title={Purification and characterization of eucaryotic alanine racemase acting as key enzyme in cyclosporin biosynthesis.},
  author={K. Hoffmann and E. Schneider-Scherzer and H. Kleinkauf and R. Zocher},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 17},
  pages={
          12710-4
        }
}
A specific alanine racemase, which is a key enzyme in the biosynthesis of the undecapeptide cyclosporin A, was purified to electrophoretic homogeneity from the fungus Tolypocladium niveum. This is the first enzyme of this kind isolated from a eucaryotic organism. The enzyme catalyzes the reversible racemization of alanine and requires pyridoxal phosphate as the exclusive cofactor. Km values for L- and D-alanine were found to be 38 and 2 mM, respectively. Maximal reaction velocity was observed… Expand
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