Molecular Biology

Research area: Neuroscience Yeast alcohol dehydrogenase 1 (ADH1) belongs to the family of zinc-containing alcohol dehydrogenases. It is a homotetramer with each subunit containing one catalytic domain and coenzyme-binding domain.

Research area: Neuroscience Yeast alcohol dehydrogenase 1 (ADH1) belongs to the family of zinc-containing alcohol dehydrogenases. It is a homotetramer with each subunit containing one catalytic domain and coenzyme-binding domain.

Research area: Neuroscience Yeast alcohol dehydrogenase 1 (ADH1) belongs to the family of zinc-containing alcohol dehydrogenases. It is a homotetramer with each subunit containing one catalytic domain and coenzyme-binding domain.

Research area: Neuroscience Yeast alcohol dehydrogenase 1 (ADH1) belongs to the family of zinc-containing alcohol dehydrogenases. It is a homotetramer with each subunit containing one catalytic domain and coenzyme-binding domain.

Research area: Neuroscience Yeast alcohol dehydrogenase 1 (ADH1) belongs to the family of zinc-containing alcohol dehydrogenases. It is a homotetramer with each subunit containing one catalytic domain and coenzyme-binding domain.

Research area: Neuroscience Yeast alcohol dehydrogenase 1 (ADH1) belongs to the family of zinc-containing alcohol dehydrogenases. It is a homotetramer with each subunit containing one catalytic domain and coenzyme-binding domain.

Research area: Neuroscience Yeast alcohol dehydrogenase 1 (ADH1) belongs to the family of zinc-containing alcohol dehydrogenases. It is a homotetramer with each subunit containing one catalytic domain and coenzyme-binding domain.

Research area: Neuroscience Yeast alcohol dehydrogenase 1 (ADH1) belongs to the family of zinc-containing alcohol dehydrogenases. It is a homotetramer with each subunit containing one catalytic domain and coenzyme-binding domain.

Application Alcohol Dehydrogenase from Saccharomyces cerevisiae has been used as a gel filtration molecular weight marker/ It has also been used as a component of nine protein mixture for mass spectroscopy analysis. Biochem/physiol Actions ADH

Alcohol dehydrogenases are a group of dehydrogenase enzymes that occur in many organisms. It is a metalloenzyme containing four tightly bound zinc atoms per molecule.

Biochem/physiol Actions Alcohol dehydrogenase catalyzes the oxidative conversion of alcohol into aldehyde . It has a homodimeric structure with a co-enzyme binding domain at the C-terminal and an N-terminal catalytic domain.

Biochem/physiol Actions Alcohol dehydrogenase catalyzes the oxidative conversion of alcohol into aldehyde . It has a homodimeric structure with a co-enzyme binding domain at the C-terminal and an N-terminal catalytic domain.