Désamination oxydative de l'acide l-homocystéine-sulfinique par la l-glutamodéshydrogénase de foie de bœuf. Inhibition de l'enzyme par l'acide l-homocystéique

@inproceedings{JollsBergeret1967DsaminationOD,
  title={D{\'e}samination oxydative de l'acide l-homocyst{\'e}ine-sulfinique par la l-glutamod{\'e}shydrog{\'e}nase de foie de bœuf. Inhibition de l'enzyme par l'acide l-homocyst{\'e}ique},
  author={Bernadette Joll{\`e}s-Bergeret},
  year={1967}
}
Abstract 1. 1.| l -Homocysteinesulfinic acid is reversibly deaminated by liver l -glutamate dehydrogenase ( l -glutamate: NAD(P) oxidoreductase (deaminating), EC 1.4.1.3) with the formation of ammonia and α-ketosulfinic acid. The rate of deamination at the optimum pH (pH 8.8) is about 65% of that observed for l -glutamic acid. The affinity of the enzyme for homocysteinesulfinic acid is ten times smaller than for glutamic acid. 2. 2.| l -Holocysteic acid is a strong inhibitor of the activity of… CONTINUE READING

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