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Literature summary 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.
    View publication on PubMed

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.9.1 71000
-
 PAGE Comamonas testosteroni
1.1.9.1 73200
-
 1 * 71000, SDS-PAGE, 1 * 73200, calculated Comamonas testosteroni

Organism

EC Number Organism UniProt Comment Textmining
1.1.9.1 Comamonas testosteroni
-
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.9.1 20.5
-
-
 Comamonas testosteroni

Substrates and Products (Substrate)

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

Subunits

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.9.1 heme holoenzyme contains equimolar amounts of pyrroloquinoline quinone, Ca2+ and covalently bound heme. Low-spin heme protein Comamonas testosteroni
1.1.9.1 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