Model for the structure of formaldehyde dehydrogenase based on alcohol dehydrogenase.
The three-dimensional structure of rat liver formaldehyde dehydrogenase (FALDH), previously known as class III alcohol dehydrogenase, was constructed using computer graphics and computer programs developed for model building. The construction is based on horse liver alcohol dehydrogenase (EE-ADH), whose structure has been elucidated by X-ray crystallography. The high sequence homology between the two enzymes makes knowledge-based modelling feasible in this case. The model shows a remarkable similarity to horse liver alcohol dehydrogenase especially in the NAD-binding domain. Certain mutations, and the one insertion in FALDH compared to EE-ADH in particular, have cause important changes in the substrate binding site, and thus aliphatic alcohols have been replaced by hemi-thioacetals as favourable substrates.
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Department of Crystallography, Birkbeck College, London, UK.
D000426:Alcohol Dehydrogenase / Q000737:chemistry; D000445:Aldehyde Oxidoreductases / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D008099:Liver / Q000201:enzymology; D008958:Models, Molecular; D015394:Molecular Structure; D051381:Rats; D012689:Sequence Homology, Nucleic Acid
D000426:Alcohol Dehydrogenase; C020145:formaldehyde dehydrogenase (glutathione); D000445:Aldehyde Oxidoreductases