Journal of Drug Metabolism & Toxicology
Open Access

Jennifer Gueldner

Publications

• Review Article
  Emerging Associations of the ALDH2*2 Polymorphism with Disease Susceptibility
  Author(s): Jennifer Gueldner, Christie Sayes, Erika Abel and Erica BruceJennifer Gueldner, Christie Sayes, Erika Abel and Erica Bruce
  
  Ethanol is metabolized by Alcohol Dehydrogenase (ADH) to acetaldehyde and then irreversibly oxidized by Aldehyde Dehydrogenase (ALDH) to nontoxic acetate. In individuals expressing the ALDH2*2 variant enzyme, the rate of conversion from acetaldehyde to acetate is reduced and leads to flushing, nausea, and tachycardia due to increased blood levels of acetaldehyde. The ALDH2*2 variant has a lowered NAD+ coenzyme binding affinity, which results in a lowered clearance capacity toward acetaldehyde. This polymorphism is caused by the substitution of glutamate for lysine at position 487 within the catalytic active site of ALDH2, resulting in effects on subunit and quaternary complex activity. ALDH2*2 alleles are dominant over ALDH2*1 and therefore are expected to contribute to the formation of inactive heterotetramers decreased enzymatic activity in both homozygous and heterozygous individuals... View More»
  DOI: 10.4172/2157-7609.1000202

  Abstract PDF

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