Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | Fe2+-form of enzyme, less than 1 mol per mol of protein | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q9BV57 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(1Z)-1,2-dihydroxyhex-1-en-3-one + O2 | i.e. desthio-acireductone | Homo sapiens | 2-oxovalerate + formic acid | - |
? | |
additional information | human ARD is capable of metal-dependent dual chemistry. The Fe2+-bound ARD shows the highest activity and catalyzes on-pathway chemistry, i.e. reaction of EC 1.13.11.54, whereas Ni2+, Co2+ or Mn2+ forms catalyze off-pathway chemistry, i.e. reasctions of EC 1.13.11.53. The enzymatic activity is metal ion cofactor dependent and the activity trend in decreasing order is Fe2+ > Ni2+ = Co2+ > Mn2+ | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ADI1 | - |
Homo sapiens |
ARD | - |
Homo sapiens |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
Ni2+-bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable | Homo sapiens |