Involvement of glutamate 268 in the active site of human liver mitochondrial (class 2) aldehyde dehydrogenase as probed by site-directed mutagenesis.

@article{Wang1995InvolvementOG,
  title={Involvement of glutamate 268 in the active site of human liver mitochondrial (class 2) aldehyde dehydrogenase as probed by site-directed mutagenesis.},
  author={Xuefeng Wang and Henry Weiner},
  journal={Biochemistry},
  year={1995},
  volume={34 1},
  pages={237-43}
}
On the basis of chemical modification studies, it was postulated that glutamate 268 was a component of the active site of liver aldehyde dehydrogenase [Abriola, D. P., Fields, R., MacKerell, A. D., Jr., & Pietruszko, R. (1987) Biochemistry 26, 5679-5684]. To study its role, the residue in human liver mitochondrial (class 2) aldehyde dehydrogenase was mutated to an aspartate, a glutamine, or a lysine, and the enzyme was expressed in Escherichia coli. The mutations did not affect the Km values… CONTINUE READING

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