Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | nonheme-diiron enzyme | Nostoc punctiforme |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ | Nostoc punctiforme | - |
an alkane + formate + H2O + 2 NADP+ | - |
? | |
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ | Nostoc punctiforme ATCC 29133 / PCC 73102 | - |
an alkane + formate + H2O + 2 NADP+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Nostoc punctiforme | B2J1M1 | - |
- |
Nostoc punctiforme ATCC 29133 / PCC 73102 | B2J1M1 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+ | aldehyde-deformylating oxygenase (ADO) catalyzes conversion of a fatty aldehyde to the corresponding alk(a/e)ne and formate, consuming four electrons and one molecule of O2 per turnover and incorporating one atom from O2 into the formate coproduct. A cyanobacterial [2Fe-2S] ferredoxin (PetF), reduced by ferredoxin-NADP+ reductase (FNR) using NADPH, is implicated. Rapid reduction of the diferric-peroxyhemiacetal intermediate in ADO by a cyanobacterial ferredoxin. The enzyme follows a free-radical mechanism via radical and Fe2 III/III?PHA intermediate, reaction overview | Nostoc punctiforme |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme | an alkane + formate + H2O + 2 NADP+ | - |
? | |
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ | ADO activity is dependent upon a continuous supply of electrons, both for reduction of the Fe2 III/III form of the cofactor back to the O2-reactive Fe2 II/II state and during conversion of the Fe2 III/III-PHA intermediate state to the product complex | Nostoc punctiforme | an alkane + formate + H2O + 2 NADP+ | - |
? | |
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme ATCC 29133 / PCC 73102 | an alkane + formate + H2O + 2 NADP+ | - |
? | |
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ | ADO activity is dependent upon a continuous supply of electrons, both for reduction of the Fe2 III/III form of the cofactor back to the O2-reactive Fe2 II/II state and during conversion of the Fe2 III/III-PHA intermediate state to the product complex | Nostoc punctiforme ATCC 29133 / PCC 73102 | an alkane + formate + H2O + 2 NADP+ | - |
? | |
additional information | aldehyde-deformylating oxygenase (ADO) catalyzes conversion of a fatty aldehyde to the corresponding alk(a/e)ne and formate, consuming four electrons and one molecule of O2 per turnover and incorporating one atom from O2 into the formate coproduct. A cyanobacterial [2Fe-2S] ferredoxin (PetF), reduced by ferredoxin-NADP+ reductase (FNR) using NADPH, is implicated. Rapid reduction of the diferric-peroxyhemiacetal intermediate in ADO by a cyanobacterial ferredoxin. The enzyme follows a free-radical mechanism. Both the diferric form of Nostoc punctiforme ADO and its (putative) diferric-peroxyhemiacetal intermediate are reduced much more rapidly by Synechocystis sp. PCC6803 PetF than by the previously employed chemical reductant, 1-methoxy-5-methylphenazinium methyl sulfate. The yield of formate and alkane per reduced PetF approaches its theoretical upper limit when reduction of the intermediate is carried out in the presence of FNR. Reduction of the intermediate by either system leads to accumulation of a substrate-derived peroxyl radical as a result of off-pathway trapping of the C2-alkyl radical intermediate by excess O2, which consequently diminishes the yield of the hydrocarbon product. A sulfinyl radical located on residue Cys71 also accumulates with short-chain aldehydes | Nostoc punctiforme | ? | - |
? | |
additional information | aldehyde-deformylating oxygenase (ADO) catalyzes conversion of a fatty aldehyde to the corresponding alk(a/e)ne and formate, consuming four electrons and one molecule of O2 per turnover and incorporating one atom from O2 into the formate coproduct. A cyanobacterial [2Fe-2S] ferredoxin (PetF), reduced by ferredoxin-NADP+ reductase (FNR) using NADPH, is implicated. Rapid reduction of the diferric-peroxyhemiacetal intermediate in ADO by a cyanobacterial ferredoxin. The enzyme follows a free-radical mechanism. Both the diferric form of Nostoc punctiforme ADO and its (putative) diferric-peroxyhemiacetal intermediate are reduced much more rapidly by Synechocystis sp. PCC6803 PetF than by the previously employed chemical reductant, 1-methoxy-5-methylphenazinium methyl sulfate. The yield of formate and alkane per reduced PetF approaches its theoretical upper limit when reduction of the intermediate is carried out in the presence of FNR. Reduction of the intermediate by either system leads to accumulation of a substrate-derived peroxyl radical as a result of off-pathway trapping of the C2-alkyl radical intermediate by excess O2, which consequently diminishes the yield of the hydrocarbon product. A sulfinyl radical located on residue Cys71 also accumulates with short-chain aldehydes | Nostoc punctiforme ATCC 29133 / PCC 73102 | ? | - |
? | |
n-decanal + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme | n-nonane + formate + H2O + 2 NADP+ | - |
? | |
n-decanal + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme ATCC 29133 / PCC 73102 | n-nonane + formate + H2O + 2 NADP+ | - |
? | |
n-octanal + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme | n-heptane + formate + H2O + 2 NADP+ | - |
? | |
n-octanal + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme ATCC 29133 / PCC 73102 | n-heptane + formate + H2O + 2 NADP+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ADO | - |
Nostoc punctiforme |
aldehyde-deformylating oxygenase | - |
Nostoc punctiforme |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
5 | - |
assay at | Nostoc punctiforme |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Nostoc punctiforme |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
Ferredoxin | identification of Synechocystis sp. PC 6803 ssl0020 ferredoxin, PetF, UniProt ID P27320, as an efficient ADO reductant, overview | Nostoc punctiforme | |
NADPH | - |
Nostoc punctiforme |
General Information | Comment | Organism |
---|---|---|
physiological function | aldehyde-deformylating oxygenase (ADO) is a ferritin-like nonheme-diiron enzyme that catalyzes the last step in a pathway through which fatty acids are converted into hydrocarbons in cyanobacteria | Nostoc punctiforme |