Literature summary for 1.1.9.1 extracted from

De Jong, G.A.H.; Geerlof, A.; Stoorvogel, J.; Jongejan, J.A.; de Vries, S.; Duine, J.a.
Quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni. Purification, characterization, and reconstitution of the apoenzyme with pyrolloquinoline quinone analogues (1995), Eur. J. Biochem., 230, 899-905.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	holoenzyme contains equimolar amounts of pyrroloquinoline quinone, Ca2+ and covalently bound heme	Comamonas testosteroni

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
71000	-	PAGE	Comamonas testosteroni
73200	-	1 * 71000, SDS-PAGE, 1 * 73200, calculated	Comamonas testosteroni

Organism

Organism	UniProt	Comment	Textmining
Comamonas testosteroni	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
from ethanol-grown cells	Comamonas testosteroni

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
20.5	-	-	Comamonas testosteroni

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
n-butanol + ferricyanide	-	Comamonas testosteroni	butanal + ferrocyanide	-	?

Subunits

Subunits	Comment	Organism
monomer	1 * 71000, SDS-PAGE, 1 * 73200, calculated	Comamonas testosteroni

Cofactor

Cofactor	Comment	Organism	Structure
heme	holoenzyme contains equimolar amounts of pyrroloquinoline quinone, Ca2+ and covalently bound heme. Low-spin heme protein	Comamonas testosteroni
pyrroloquinoline quinone	holoenzyme contains equimolar amounts of pyrroloquinoline quinone, Ca2+ and covalently bound heme. Reconstitution of apoenzyme with pyrroloquinoline quinone analogues results in a decreased activity and enantioselectivity for the oxidation of chiral alcohols. Possession of the o-quinone or o-quinol moiety is not essential for binding but it is for activity	Comamonas testosteroni

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Release 2023.1 (January 2023)