PROSITE documentation PDOC00059

Alcohol dehydrogenase (EC 1.1.1.1) (ADH) catalyzes the reversible oxidation of ethanol to acetaldehyde with the concomitant reduction of NAD [1]. 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.

Iron-containing ADH's have been found in yeast (gene ADH4) [2], as well as in Zymomonas mobilis (gene adhB) [3]. These two iron-containing ADH's are closely related to the following enzymes:

Escherichia coli propanediol oxidoreductase (EC 1.1.1.77) (gene fucO) [4], an enzyme involved in the metabolism of fucose and which also seems to contain ferrous ion(s).
Clostridium acetobutylicum NADPH- and NADH-dependent butanol dehydrogenases (EC 1.1.1.-) (genes adh1, bdhA and bdhB) [5], an enzyme which has activity using butanol and ethanol as substrates.
Escherichia coli adhE [6], an iron-dependent enzyme which harbor three different activities: alcohol dehydrogenase, acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) and pyruvate-formate-lyase deactivase.
Bacterial glycerol dehydrogenase (EC 1.1.1.6) (gene gldA or dhaD) [7].
Clostridium kluyveri NAD-dependent 4-hydroxybutyrate dehydrogenase (4hbd) (EC 1.1.1.61).
Citrobacter freundii and Klebsiella pneumoniae 1,3-propanediol dehydrogenase (EC 1.1.1.202) (gene dhaT).
Bacillus methanolicus NAD-dependent methanol dehydrogenase (EC 1.1.1.244) [8].
Escherichia coli and Salmonella typhimurium ethanolamine utilization protein eutG.
Escherichia coli hypothetical protein yiaY.
Escherichia coli hypothetical protein ybdH.
Escherichia coli hypothetical protein yqhD.
Methanococcus jannaschii hypothetical protein MJ0712.

The patterns that we developed to detect this class of enzymes are based on two conserved regions.

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1	Authors	Branden C.-I., Joernvall H., Eklund H., Furugren B.
1	Source	(In) The Enzymes (3rd edition) 11:104-190(1975).

2	Authors	Conway T., Sewell G.W., Osman Y.A., Ingram L.O.
	Title	Cloning and sequencing of the alcohol dehydrogenase II gene from Zymomonas mobilis.
	Source	J. Bacteriol. 169:2591-2597(1987).
	PubMed ID	3584063

3	Authors	Williamson V.M., Paquin C.E.
	Title	Homology of Saccharomyces cerevisiae ADH4 to an iron-activated alcohol dehydrogenase from Zymomonas mobilis.
	Source	Mol. Gen. Genet. 209:374-381(1987).
	PubMed ID	2823079

4	Authors	Conway T., Ingram L.O.
	Title	Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae.
	Source	J. Bacteriol. 171:3754-3759(1989).
	PubMed ID	2661535

5	Authors	Walter K.A., Bennett G.N., Papoutsakis E.T.
	Title	Molecular characterization of two Clostridium acetobutylicum ATCC 824 butanol dehydrogenase isozyme genes.
	Source	J. Bacteriol. 174:7149-7158(1992).
	PubMed ID	1385386

Iron-containing alcohol dehydrogenases signatures

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6	Authors	Kessler D., Leibrecht I., Knappe J.
	Title	Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE.
	Source	FEBS Lett. 281:59-63(1991).
	PubMed ID	2015910

7	Authors	Truniger V., Boos W.
	Title	Mapping and cloning of gldA, the structural gene of the Escherichia coli glycerol dehydrogenase.
	Source	J. Bacteriol. 176:1796-1800(1994).
	PubMed ID	8132480

8	Authors	de Vries G.E., Arfman N., Terpstra P., Dijkhuizen L.
8	Source	J. Bacteriol. 174:5346-5353(1992).