EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.1 | O2 | inhibits biotransformation of 2,4,6,8,10,12-hexanitro-2,4,6,8,10,12-hexaazaisowurzitane | Pseudomonas sp. |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.13.1 | Pseudomonas sp. | - |
ATCC 29352 | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.14.13.1 | 0.000256 | - |
biotransformation of 2,4,6,8,10,12-hexanitro-2,4,6,8,10,12-hexaazaisowurzitane | Pseudomonas sp. |
1.14.13.1 | 0.58 | - |
reaction with salicylate | Pseudomonas sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.13.1 | 2,4,6,8,10,12-hexanitro-2,4,6,8,10,12-hexaazaisowurzitane + NADH | the enzyme catalyzes two oxygen-sensitive single-electron transfer steps necessary to release two nitrite ions from 2,4,6,8,10,12-hexanitro-2,4,6,8,10,12-hexaazaisowurzitane and this is followed by the secondary decomposition of this energetic chemical | Pseudomonas sp. | NO2- + N2O + formate + NH4+ | N2O is abiotically produced from NO2-NH2 | ? | |
1.14.13.1 | salicylate + NADH + H+ + O2 | - |
Pseudomonas sp. | catechol + NAD+ + H2O + CO2 | - |
? |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.1 | FAD | the FAD-site of the enzyme is involved in the biotransformation of 2,4,6,8,10,12-hexanitro-2,4,6,8,10,12-hexaazaisowurzitane | Pseudomonas sp. | |
1.14.13.1 | NADH | - |
Pseudomonas sp. |