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Literature summary for 4.1.99.5 extracted from

  • Rajakovich, L.J.; N?rgaard, H.; Warui, D.M.; Chang, W.C.; Li, N.; Booker, S.J.; Krebs, C.; Bollinger, J.M.; Pandelia, M.E.
    Rapid reduction of the diferric-peroxyhemiacetal intermediate in aldehyde-deformylating oxygenase by a cyanobacterial ferredoxin evidence for a free-radical mechanism (2015), J. Am. Chem. Soc., 137, 11695-11709 .
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ nonheme-diiron enzyme Nostoc punctiforme

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ Nostoc punctiforme
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an alkane + formate + H2O + 2 NADP+
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ Nostoc punctiforme ATCC 29133 / PCC 73102
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an alkane + formate + H2O + 2 NADP+
-
?

Organism

Organism UniProt Comment Textmining
Nostoc punctiforme B2J1M1
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-
Nostoc punctiforme ATCC 29133 / PCC 73102 B2J1M1
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-

Reaction

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 and Products (Substrate)

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+
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Nostoc punctiforme n-nonane + formate + H2O + 2 NADP+
-
?
n-decanal + O2 + 2 NADPH + 2 H+
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Nostoc punctiforme ATCC 29133 / PCC 73102 n-nonane + formate + H2O + 2 NADP+
-
?
n-octanal + O2 + 2 NADPH + 2 H+
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Nostoc punctiforme n-heptane + formate + H2O + 2 NADP+
-
?
n-octanal + O2 + 2 NADPH + 2 H+
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Nostoc punctiforme ATCC 29133 / PCC 73102 n-heptane + formate + H2O + 2 NADP+
-
?

Synonyms

Synonyms Comment Organism
ADO
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Nostoc punctiforme
aldehyde-deformylating oxygenase
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Nostoc punctiforme

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5
-
assay at Nostoc punctiforme

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Nostoc punctiforme

Cofactor

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

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