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 Maximum [Da] | Comment | Organism |
---|---|---|---|
71000 | - |
PAGE | Comamonas testosteroni |
73200 | - |
1 * 71000, SDS-PAGE, 1 * 73200, calculated | Comamonas testosteroni |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Comamonas testosteroni | - |
- |
- |
Purification (Comment) | Organism |
---|---|
from ethanol-grown cells | Comamonas testosteroni |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
20.5 | - |
- |
Comamonas testosteroni |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
n-butanol + ferricyanide | - |
Comamonas testosteroni | butanal + ferrocyanide | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 71000, SDS-PAGE, 1 * 73200, calculated | Comamonas testosteroni |
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 |