Alcohol dehydrogenase-like, C-terminal
IPR013149
Definition
This entry represents the cofactor-binding domain in alcohol dehydrogenases, which is normally found towards the C-terminal. Structural studies indicate that it forms a classical Rossman fold that reversibly binds NAD(H) [[cite:PMID:12962626], [cite:PMID:12627956], [cite:PMID:7602590]]. This entry also includes NADP-dependent quinone oxidoreductase ([ec:1.6.5.5]), an enzyme found in bacteria (gene qor), in yeast and in mammals, where, in some species such as rodents, it has been recruited as an eye lens protein and is known as zeta-crystallin PMID:8486156. The sequence of quinone oxidoreductase is distantly related to that of other zinc-containing alcohol dehydrogenases, and it lacks the zinc-ligand residues. The torpedo fish and mammalian synaptic vesicle membrane protein vat-1 is related to qor. Other related NADP-dependent oxidoreductases are represented by this entry, such as Enoyl-[acyl-carrier-protein], probable D-xylulose and Prostaglandin reductases. Alcohol dehydrogenase ([ec:1.1.1.1]) (ADH) catalyses the reversible oxidation of alcohols to their corresponding acetaldehyde or ketone with the concomitant reduction of NAD: alcohol + NAD = aldehyde or ketone + NADH Currently three structurally and catalytically different types of alcohol dehydrogenases are known: Zinc-containing 'long-chain' alcohol dehydrogenases. Insect-type, or 'short-chain' alcohol dehydrogenases. Iron-containing alcohol dehydrogenases. Zinc-containing ADH's [[cite:PMID:3622514], [cite:PMID:1593644]] are dimeric or tetrameric enzymes that bind two atoms of zinc per subunit. One of the zinc atoms is essential for catalytic activity while the other is not. Both zinc atoms are coordinated by either cysteine or histidine residues; the catalytic zinc is coordinated by two cysteines and one histidine. Zinc-containing ADH's are found in bacteria, mammals, plants, and in fungi. In many species there is more than one isozyme (for example, humans have at least six isozymes, yeast have three, etc.). A number of other zinc-dependent dehydrogenases are closely related to zinc ADH PMID:8504864 and are included in this family: Sorbitol dehydrogenase ([ec:1.1.1.14]) L-threonine 3-dehydrogenase ([ec:1.1.1.103]) Glutathione-dependent formaldehyde dehydrogenase ([ec:1.1.1.284]) Mannitol dehydrogenase ([ec:1.1.1.255])
15 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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