Activating Compound | Comment | Organism | Structure |
---|---|---|---|
benzylamine | activates sQH-AmDH | Paracoccus denitrificans | |
Dithionite | rapidly activates sQH-AmDH, activation process involves a reduction process | Paracoccus denitrificans | |
dithiothreitol | rapidly activates sQH-AmDH, activation process involves a reduction process | Paracoccus denitrificans | |
n-butylamine | activates sQH-AmDH | Paracoccus denitrificans |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
36500 | - |
SDS-PAGE, heme 2 shows two bands | Paracoccus denitrificans |
59500 | - |
SDS-PAGE, heme 2 shows two bands | Paracoccus denitrificans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Paracoccus denitrificans | - |
- |
- |
Purification (Comment) | Organism |
---|---|
ion-exchange chromatography with DEAE-Toyopearl resin | Paracoccus denitrificans |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
heme 2 does not show any enzymatic activity for amine oxidation. Heme 2 is slowly activated in 10-30 h during incubation with n-butylamine. Enzyme is faster activated with benzylamine | Paracoccus denitrificans |
additional information | - |
sQH-AmDH is not electrochemically activated by direct electrolytic reduction with a column electrode at -0.5 V, but it is electrochemically activated by mediated electrolytic reduction with a column electrode | Paracoccus denitrificans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
benzylamine + H2O + ferricyanide | - |
Paracoccus denitrificans | benzaldehyde + NH3 + reduced ferricyanide | - |
? | |
n-butylamine + H2O + ferricyanide | - |
Paracoccus denitrificans | butanal + NH3 + reduced ferricyanide | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterotrimer | gel filtration, mass spectroscopy and UV-VIS spectroscopy: the gamma subunit of sQH-AmDH shows a sharp peak at 390 nm in UV-VIS spectrum clearly distinguishable from that of QH-AmDH. Electrospray ionization mass spectrometric analysis shows that the molecular mass of the gamma subunit of sQH-AmDH is larger than that of QH-AmDH by 15.6. The data suggest that the cysteine tryptophylquinone-like moiety (catalytic center) of the gamma subunit of sQH-AmDH is an oxime | Paracoccus denitrificans |
Synonyms | Comment | Organism |
---|---|---|
Heme 2 | inactive form of QH-AmDH | Paracoccus denitrificans |
quinohemoprotein amine dehydrogenase | - |
Paracoccus denitrificans |
sQH-AmDH | silent form of QH-AmDH | Paracoccus denitrificans |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Paracoccus denitrificans |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Paracoccus denitrificans |