Purification, regulation, and molecular and biochemical characterization of pyruvate carboxylase from Methanobacterium thermoautotrophicum strain deltaH.

@article{Mukhopadhyay1998PurificationRA,
  title={Purification, regulation, and molecular and biochemical characterization of pyruvate carboxylase from Methanobacterium thermoautotrophicum strain deltaH.},
  author={Biswarup Mukhopadhyay and Shana Stoddard and Ralph S. Wolfe},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 9},
  pages={5155-66}
}
We discovered that Methanobacterium thermoautotrophicum strain DeltaH possessed pyruvate carboxylase (PYC), and this biotin prototroph required exogenously supplied biotin to exhibit detectable amounts of PYC activity. The enzyme was highly labile and was stabilized by 10% inositol in buffers to an extent that allowed purification to homogeneity and characterization. The purified enzyme was absolutely dependent on ATP, Mg2+ (or Mn2+ or Co2+), pyruvate, and bicarbonate for activity… CONTINUE READING
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