Mitochondrial aldehyde dehydrogenase Homology of putative targeting sequence to that of carbamyl phosphate synthetase I revealed by correlation of cDNA and protein data

@article{Hempel1987MitochondrialAD,
  title={Mitochondrial aldehyde dehydrogenase Homology of putative targeting sequence to that of carbamyl phosphate synthetase I revealed by correlation of cDNA and protein data},
  author={John Hempel and Jan Olov H{\"o}{\"o}g and Hans J{\"o}rnvall},
  journal={FEBS Letters},
  year={1987},
  volume={222}
}
9 Citations

Primary structures of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences.

Comparisons with the amino acid sequences of other aldehyde dehydrogenases support the suggestion that the NAD-binding domain may be located in the middle portion of the mature enzyme.

Human aldehyde dehydrogenase. cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde.

Human liver aldehyde dehydrogenase (E3 isozyme), with wide substrate specificity and low Km for 4-aminobutyraldehyde, was only recently characterized [Kurys, G., Ambroziak, W. & Pietruszko, R. (1989)

Mitochondrial aldehyde dehydrogenase from horse liver. Correlations of the same species variants for both the cytosolic and the mitochondrial forms of an enzyme.

Unexpectedly, positions with residues unique to one of the four enzymes are about twice as common in both of the horse proteins than in either of the human proteins, showing that not only functional properties of the protein, but also other factors, such as generation time, are important for enzyme divergence.

Sequence of the signal peptide for rat liver mitochondrial aldehyde dehydrogenase.

Biotransformation of Xenobiotics

The metabolic fate of a xenobiotic can have an important bearing on its toxic potential, the disposition of the compound in the body and the excretion of the compounds.

Evolution and Structural Theory: The Frontier Between Chemistry and Biology

Models that interrelate the primary structures of enzymes and their behaviors, primary structure and natural selection, and finally natural selection and enzymic behavior are reviewed.

Pharmacogenetics of aldehyde dehydrogenase (ALDH).

Molecular Biological Approaches to Studies of Alcohol-Metabolizing Enzymes

Many questions about the mechanisms by which alcohol affects organisms and about inherited differences in alcohol metabolism can be answered using molecular biological/molecular genetic approaches.

Genetic polymorphisms and related risk factors of ischemic stroke in a Mongolian population in China

Ишемический инсульт, вызванный прерыванием потока крови в мозг, представляет серьезную медицинскую проблему, являясь фактором риска смерти и потери трудоспособности. Недавние исследования геномных

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The 500-residue amino acid sequence of the subunit of mitochondrial human liver aldehyde dehydrogenase is reported. It is the first structure determined for this enzyme type from any species, and is

Aldehyde dehydrogenase from human liver. Primary structure of the cytoplasmic isoenzyme.

Analysis of CNBr fragments and other peptides from human liver cytoplasmic aldehyde dehydrogenase enabled determination of the complete primary structure of this protein, supporting the concept that the enzyme is a homotetramer.

The cytoplasmic isoenzyme of horse liver aldehyde dehydrogenase. Relationship to the corresponding human isoenzyme.

The structural divergence between the cytoplasmic isoenzymes of aldehyde dehydrogenase from different species was investigated by analysis of peptides from the horse protein, and correlation of the

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The amino acid sequence of GTP:AMP phosphotransferase (AK3) from beef-heart mitochondria has been determined, except for one segment of about 33 residues in the middle of the polypeptide chain, demonstrating that earlier views on substrate binding have to be modified.

Molecular abnormality of an inactive aldehyde dehydrogenase variant commonly found in Orientals.

It is concluded that a point mutation in the human ALDH2 locus produced the glutamine leads to lysine substitution and enzyme inactivation in atypical livers.