EC Number   |
Natural Substrates |
|---|
   1.4.9.1 | 2-phenylethylamine + 2 H2O + 2 acceptor |
primary amine |
| 1.4.9.1 | methylamine + amicyanin + H2O |
amicyanin is the in vivo electron acceptor |
| 1.4.9.1 | methylamine + H2O + 2 amicyanin |
- |
| 1.4.9.1 | methylamine + H2O + amicyanin |
- |
| 1.4.9.1 | more |
an essential enzyme for the aerobic degradation of many primary amines even though they have quite different chemical structures (aromatic or aliphatic) |
| 1.4.9.1 | more |
when different QHNDH mutants (peaA, peaC and peaD) are transformed with a genetic construction containing the peaABCD cluster, all the recombinant strains efficiently catabolized 2-phenylethylamine as well as other primary amines like propyl-, butyl- and pentylamine. |
| 1.4.9.1 | more |
amicyanin ami catalyzes the electron transfer from MADH to the terminal oxidase, without the need for any c-type cytochrome. In the absence of either MADH or cytochrome aa3, amicanin is not capable of oxygen reduction on the same time scale. The oxygen consumption depends nearly linearly on the amicyanin concentration up to at least 100 microM. Experiments demonstrate a remarkable number of possibilities for the electron transfer. The interactions appear to be governed exclusively by the electrostatic nature of each of the proteins. Paracoccus denitrificans provides a pool of cytochromes for efficient electron transfer via weak, ill-defined interactions |
