EC Number   |
General Information |
Reference |
|---|
   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 | evolution |
structurally, the cADO enzyme belongs to the family of ferritin-like nonheme diiron-carboxylate enzymes that include methane monooxygenase (MMO), class I ribonucleotide reductase (RNR), and stearoyl-acyl carrier protein ?9-desaturase (DELTA9D), all of which share a common Fe2(His)2(O2CR)4 active site |
-, 748032 |
| 4.1.99.5 | evolution |
the enzyme belongs to the superfamily of ferritin-like di-iron proteins with conserved sequence of two EX28-29EX2H motifs |
-, 749212 |
| 4.1.99.5 | malfunction |
C71A/S mutations reduce the hydrocarbon producing activity of AD and facilitate the formation of a dimer, while mutations at Cys107 and Cys117 do not affect the hydrocarbon producing activity of the enzyme. The Cys-to-Ala/Ser mutations do not affect the iron binding to the enzyme. Structural features of the Cys-deficient mutants, overview |
-, 749051 |
| 4.1.99.5 | malfunction |
the substrate preferences of some enzyme mutants towards different chain-length substrates are enhanced, e.g. I24Y for n-heptanal, I27F for n-decanal and n-dodecanal, V28F for n-dodecanal, F87Y for n-decanal, C70F for n-hexanal, A118F for n-butanal, A121F for C4,6,7 aldehydes, V184F for n-dodecanal and n-decanal, M193Y for C6-10 aldehydes and L198F for C7-10 aldehydes |
-, 747351 |
| 4.1.99.5 | metabolism |
cyanobacterial aldehyde-deformylating oxygenase (cADO), which catalyzes the conversion of Cn fatty aldehyde to its corresponding Cn-1 alk(a/e)ne, is a key enzyme in fatty alk(a/e)ne biosynthesis pathway |
-, 749212 |
| 4.1.99.5 | metabolism |
efficient delivery of long-chain fatty aldehydes from the Nostoc punctiforme acyl-acyl carrier protein reductase to its cognate aldehyde-deformylating oxygenase in a two-step pathway consisting of an acyl-acyl carrier protein (ACP) reductase (AAR) and an aldehyde-deformylating oxygenase (ADO) allowing various cyanobacteria to convert long-chain fatty acids into hydrocarbons. When the aldehyde substrate is supplied to ADO by AAR, efficient in vitro turnover is observed in the absence of solubilizing agents, even with insoluble substrates like octadec(a/e)nal, overview. AAR and ADO form a tight isolable complex with a Kd of 0.003 mM. The interaction between AAR and ADO facilitates either direct transfer of the aldehyde product of AAR to ADO or formation of the aldehyde product in a microenvironment allowing for its efficient uptake by ADO |
-, 747081 |
| 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 |
comparison of the enzyme from Synechococcus elongates strain PCC 7942 and Synechocystis sp. PCC 6803, the first is more active than the latter against n-hexadecanal. Enzyme structure-function relationship analysis and comparisons, overview |
747409 |
| 4.1.99.5 | more |
Cys71, which is located in close proximity to the substrate-binding site, plays a crucial role in maintaining the activity, structure, and stability of the enzyme |
-, 749051 |
