PANTHER - Family Information

PANTHER Family Information

Family:

ALCOHOL DEHYDROGENASE RELATED (PTHR11695)

Subfamilies:

PANTHER Links:

Tree MSA

Abstract:

Alcohol dehydrogenase (EC: 1.1.1.1) (ADH) catalyzes the reversible oxidation of ethanol to acetaldehyde with the concomitant reduction of NAD: Ethanol + NAD = Acetaldehyde + 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 [PMID:3622514, PMID:1593644] are dimeric or tetrameric enzymes that bind two atoms of zinc per subunit. One of the zinc atom 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 most species there are more than one isozyme (for example, human 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.

In addition, this family 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 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.

InterPro Accession:

IPR002085

PANTHER Molecular Function:

Oxidoreductase