The nature of the coenzyme of aspartic acid, serine, and threonine deaminases.

@article{Lichstein1949TheNO,
  title={The nature of the coenzyme of aspartic acid, serine, and threonine deaminases.},
  author={H. Lichstein and J. Christman},
  journal={Journal of bacteriology},
  year={1949},
  volume={58 5},
  pages={
          565-72
        }
}
We have reported previously that biotin, as well as muscle adenylic acid, is somehow concerned in the reversible deamination of aspartic acid, and in the deamination of serine and threonine (Lichstein and Umbreit, 1947a; Lichstein and Christman, 1948). This has been demonstrated by employing an aging technique consisting of the exposure of living bacterial cell suspensions to molar phosphate at pH 4 for a short time (Lichstein and Umbreit, 1947a,b; Lichstein and Christman, 1948). The intimate… Expand
12 Citations
The preparation of the coenzyme of aspartic acid deaminase.
Further studies on the biotin coenzyme.
Functions of biotin in enzyme systems.
The effect of carbohydrates on the tryptophanase activity of bacteria.
The degradation of amino-acids
The biotin-dependent enzymes.
  • J. Moss, M. Lane
  • Chemistry, Medicine
  • Advances in enzymology and related areas of molecular biology
  • 1971
CHAPTER VIII – BIOTIN
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