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Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion.
The structure of ALDH2 is important for the elucidation of its catalytic mechanism, for a clear understanding of the contribution ofALDH2 to the genetic component of alcoholism and for the development of specific AL DH2 inhibitors as potential drugs for use in the treatment of alcoholism. Expand
Molecular Cloning, Characterization, and Potential Roles of Cytosolic and Mitochondrial Aldehyde Dehydrogenases in Ethanol Metabolism in Saccharomyces cerevisiae
- X. Wang, C. J. Mann, Y. Bai, L. Ni, H. Weiner
- Biology, Medicine
- Journal of bacteriology
- 15 February 1998
The full-length DNAs for two Saccharomyces cerevisiae aldehyde dehydrogenase (ALDH) genes were cloned and expressed in Escherichia coli and the role of mitochondrial ALDH5 in acetaldehyde metabolism has not been defined but appears to be unimportant. Expand
Role of Reduced Lipoic Acid in the Redox Regulation of Mitochondrial Aldehyde Dehydrogenase (ALDH-2) Activity
- P. Wenzel, U. Hink, +8 authors A. Daiber
- Chemistry, Medicine
- Journal of Biological Chemistry
- 5 January 2007
The present data demonstrate that the mitochondrial dithiol compound dihydrolipoic acid restores mitochondrial aldehyde dehydrogenase activity via reduction of a disulfide at the active site and thereby improves nitrate tolerance. Expand
Mitochondrial Aldehyde Dehydrogenase Activity Is Required for Male Fertility in Maize
The finding that T cytoplasm plants that are homozygous for the rf2-R213 allele are male sterile but accumulate normal amounts of RF2 protein that lacks normal mitochondrial ALDH activity provides strong evidence that rf1-encoded mtALDH activity is required to restore male fertility to T cy toplasm maize. Expand
Isolation and Characterization of an Aldehyde Dehydrogenase Encoded by the aldB Gene of Escherichia coli
An aldehyde dehydrogenase was detected in crude cell extracts of Escherichia coli DH5alpha and shared kinetic properties with the mammalian enzyme, which was thought to play a role in the removal of aldehydes and alcohols in cells that were under stress. Expand
Involvement of snapdragon benzaldehyde dehydrogenase in benzoic acid biosynthesis.
- M. C. Long, Dinesh A Nagegowda, +7 authors N. Dudareva
- Biology, Medicine
- The Plant journal : for cell and molecular…
- 1 July 2009
Benzoic acid (BA) is an important building block in a wide spectrum of compounds varying from primary metabolites to secondary products. Benzoic acid biosynthesis from L-phenylalanine requires… Expand
Involvement of Glutamate 399 and Lysine 192 in the Mechanism of Human Liver Mitochondrial Aldehyde Dehydrogenase*
The role of these two NAD+-ribose-binding residues was investigated, and a pre-steady state burst of NADH formation was observed for the E399Q/K and K192Q mutants with benzaldehyde, and p-nitrobenzaldehyde was oxidized faster than benzaldehyde so that when aromatic aldehydes were used as substrates, the rate-limiting step remained deacylation for all these mutants. Expand
Differential effects of Mg2+ ions on the individual kinetic steps of human cytosolic and mitochondrial aldehyde dehydrogenases.
The results indicated that, with both isozymes, Mg(2+) ions tightened the binding of NADH, and by binding to the coenzyme, they increased the nucleophilicity of the nucleophile Cys302. Expand
Horse liver aldehyde dehydrogenase. I. Purification and characterization.
Horse liver aldehyde: NAD oxidoreductase (EC 22.214.171.124) has been purified to homogeneity by a procedure consisting of salt fractionation, ion exchange chromatography, and isoelectric focusing, suggesting a tetrameric structure for the native enzyme. Expand