EC Number   |
General Information |
Reference  |
|---|
   4.1.99.5 | physiological function |
alkane biosynthesis pathway |
713511 |
| 4.1.99.5 | physiological function |
saturated fatty acids are converted to alkanes (and unsaturated fatty acids to alkenes) in cyanobacteria entailing scission of the C1-C2 bond of a fatty aldehyde intermediate by the enzyme aldehyde decarbonylase. The in vitro activity of the enzyme depends on the presence of a reducing system, i.e. NADPH, ferredoxin, and ferredoxin reductase |
715293 |
| 4.1.99.5 | metabolism |
in cyanobacteria, aldehyde deformylating oxygenase catalyzes the decarbonylation of fatty aldehydes to the corresponding alkanes or alkenes, last step in the biosynthesis of long-chain aliphatic hydrocarbons, which are derived from fatty acids |
726552 |
| 4.1.99.5 | more |
the very low activity of the enzyme appears to result from inhibition by the ferredoxin reducing system used in the assay and the low solubility of the substrate |
-, 726957 |
| 4.1.99.5 | more |
the definitive reaffirmation of the oxygenative nature of the reaction implies that the enzyme, initially designated as aldehyde decarbonylase when the C1-derived coproduct is thought to be carbon monoxide rather than formate, should be redesignated as aldehyde-deformylating oxygenase, ADO |
727001 |
| 4.1.99.5 | more |
the enzyme shows a mainly alpha helical architecture, with a ferritin-like four-helix bundle. The latter contains the di-iron centre, coordinated by two histidine residues and four carboxylates from glutamate side chains. Substrates access the active site through a tunnel-like hydrophobic pocket. Active site structure analysis from crystal structure, PDB ID 20C5 |
-, 727312 |
| 4.1.99.5 | evolution |
cyanobacterial aldehyde-deformylating oxygenases belong to the ferritin-like diiron-carboxylate superfamily of dioxygen-activating proteins |
727690 |
| 4.1.99.5 | more |
residue L194, at the center of the hydrophobic cavity, might serve as a gateway for substrate entry, but L194 does not play a kinetically significant role in limiting substrate access to the active site. Structure of metal-free cADO, overview |
-, 746597 |
| 4.1.99.5 | physiological function |
the nonheme diiron enzyme cyanobacterial aldehyde deformylating oxygenase, cADO, catalyzes the deformylation of aliphatic aldehydes to alkanes and formate |
-, 746597 |
| 4.1.99.5 | more |
the enzyme structure consists of eight a-helices found in ferritin-like di-iron proteins. Residues Tyr21, Ile27, Val28, Phe67, Phe86, Phe87, Phe117, Ala118, Ala121, Tyr122, Try125, and Tyr184 contributing to substrate binding, and Glu32, Glu60, His63, Glu115, Glu144, and His147 participating in iron coordination. OsADO structure resembles ADO structures with active sites containing both metal co-factor and substrate, OsADO active site is fully occupied, helix 5 of OsADO with an iron bound in the active site is a long helix |
746976 |
