EC Number   |
Natural Substrates |
|---|
   4.1.99.5 | a long-chain aldehyde + O2 + 2 NADPH + 2 H+ |
- |
| 4.1.99.5 | long-chain aldehyde + O2 + 2 NADPH + 2 H+ |
- |
| 4.1.99.5 | more |
responsible for a key step in the biosynthesis of hydrocarbon compounds |
| 4.1.99.5 | more |
alkane biosynthesis |
| 4.1.99.5 | more |
final step in alkane biosynthesis |
| 4.1.99.5 | more |
the aldehyde hydrogen is retained in the HCO2- and the hydrogen in the nascent methyl group of the alkane originates, at least in part, from solvent. The reaction appears to be formally hydrolytic, but the improbability of a hydrolytic mechanism having the primary carbanion as the leaving group, the structural similarity of the aldehyde decarbonylases to other O2-activating non-heme di-iron proteins, and the dependence of in vitro aldehyde decarbonylase activity on the presence of a reducing system implicate some type of redox mechanism. Two possible resolutions to this conundrum, overview |
| 4.1.99.5 | more |
cyanobacterial aldehyde-deformylating oxygenases catalyze conversion of saturated or monounsaturated Cn fatty aldehydes to formate and the corresponding Cn-1 alkanes or alkenes, respectively |
| 4.1.99.5 | more |
natural specificity of cADO to favour reactivity against short-chain over long-chain aldehydes |
| 4.1.99.5 | octadecanal + O2 + 2 NADPH + 2 H+ |
- |
