4.1.99.5: aldehyde oxygenase (deformylating)
This is an abbreviated version!
For detailed information about aldehyde oxygenase (deformylating), go to the full flat file.
Word Map on EC 4.1.99.5
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4.1.99.5
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biofuels
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decarbonylation
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acyl-acyl
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punctiforme
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elongatus
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octadecanal
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di-iron
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drop-in
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cados
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heptadecane
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ferritin-like
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prochlorococcus
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diferric
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photodecarboxylase
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petroleum-derived
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biofuel production
- 4.1.99.5
-
biofuels
-
decarbonylation
-
acyl-acyl
- punctiforme
- elongatus
- octadecanal
-
di-iron
-
drop-in
-
cados
- heptadecane
-
ferritin-like
- prochlorococcus
-
diferric
-
photodecarboxylase
-
petroleum-derived
- biofuel production
Reaction
+ + 2 NADPH + 2 H+ = + + + 2 NADP+
Synonyms
ADO, aldehyde decarbonylase, aldehyde deformylase, aldehyde deformylating oxygenase, aldehyde-deformylating oxygenase, CAD, cADO, cADO-1593, cyanobacterial ADO, cyanobacterial aldehyde decarbonylase, cyanobacterial aldehyde deformylating oxygenase, cyanobacterial aldehyde-deformylating oxygenase, decarbonylase, erial aldehyde-deformylating oxygenase, LiADO, More, Npun_R1711, OsADO, PMT1231, PMT_1231, RS9917_09941, SeADO, sll0208, Synpcc7942_1593
ECTree
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Reaction
Reaction on EC 4.1.99.5 - aldehyde oxygenase (deformylating)
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octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
reaction mechanism, overview
octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
possible reaction mechanism, overview. Formate is the coproduct of alkane production by the Np AD, (ii) the aldehyde hydrogen of the substrate is retained in the formate, and (iii) the hydrogen added to C2 derives (at least in part) from solvent
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octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
mechanism of the unusual iron-catalysed decarbonylation reaction
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octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
mechanistic proposal for the oxygen-independent formation of alkanes by the enzyme. In this mechanism the external reducing system functions catalytically to generate a reactive ketyl radical anion and facilitate carbon-carbon bond cleavage
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octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
mechanistic proposal for the oxygen-independent formation of alkanes by the enzyme. In this mechanism the external reducing system functions catalytically to generate a reactive ketyl radical anion and facilitate carbon-carbon bond cleavage
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octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
mechanistic proposal for the oxygen-independent formation of alkanes by the enzyme. In this mechanism the external reducing system functions catalytically to generate a reactive ketyl radical anion and facilitate carbon-carbon bond cleavage
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octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
mechanistic proposal for the oxygen-independent formation of alkanes by the enzyme. In this mechanism the external reducing system functions catalytically to generate a reactive ketyl radical anion and facilitate carbon-carbon bond cleavage
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octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
proposed mechanism of cADO involving homolytic cleavage of the C1-C2 bond of aldehyde by di-iron peroxo species, and proposed mechanism for deformylation involving heterolytic cleavage of the C1-C2 bond
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octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
the catalytic mechanism involves attack on the carbonyl of the bound substrate by the reduced O2 moiety to form a Fe2 III/III peroxyhemiacetal complex, which undergoes reductive O-O-bond cleavage, leading to C1-C2 radical fragmentation and formation of the alk(a/e)ne and formate products, detailed overview
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
octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
enzyme structures representing the different states during catalytic reaction
octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
proposed mechanism for deformylation of aldehydes by cADO, overview. The rate of alkane formation is the same in D2O or H2O, implying that proton transfer is not a kinetically significant step. When the ratio of protium to deuterium in the product alkane is measured as a function of the mole fraction of D2O, a D2OSIEobs of 2.19 is observed. The SIE is invariant with the mole fraction of D2O, indicating the involvement of a single protic site in the reaction. An iron-bound water molecule is the proton donor to the alkane in the reaction
octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
the aldehyde proton is retained in formate and one of the oxygen atoms derives from molecular oxygen, whereas the proton in the product alkane derives from the solvent. Initial formation of a diferric intermediate in the cADO catalyzed reaction. Addition of a further electron to this complex is proposed to lead to its breakdown and scission of the C1-C2 bond. A radical mechanism for C1-C2 bond cleavage is supported by the observed ring-opening of cyclopropyl aldehydes and oxiranyl aldehydes designed to act as radical clocks during deformylation by cADO. Structure-function analysis
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 ATCC 29133 / PCC 73102
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octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
the aldehyde proton is retained in formate and one of the oxygen atoms derives from molecular oxygen, whereas the proton in the product alkane derives from the solvent. Initial formation of a diferric intermediate in the cADO catalyzed reaction. Addition of a further electron to this complex is proposed to lead to its breakdown and scission of the C1-C2 bond. A radical mechanism for C1-C2 bond cleavage is supported by the observed ring-opening of cyclopropyl aldehydes and oxiranyl aldehydes designed to act as radical clocks during deformylation by cADO. Structure-function analysis
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octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
reaction mechanism, overview
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octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
mechanistic proposal for the oxygen-independent formation of alkanes by the enzyme. In this mechanism the external reducing system functions catalytically to generate a reactive ketyl radical anion and facilitate carbon-carbon bond cleavage
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octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
mechanism of the unusual iron-catalysed decarbonylation reaction
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octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
proposed mechanism for deformylation of aldehydes by cADO, overview. The rate of alkane formation is the same in D2O or H2O, implying that proton transfer is not a kinetically significant step. When the ratio of protium to deuterium in the product alkane is measured as a function of the mole fraction of D2O, a D2OSIEobs of 2.19 is observed. The SIE is invariant with the mole fraction of D2O, indicating the involvement of a single protic site in the reaction. An iron-bound water molecule is the proton donor to the alkane in the reaction
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octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
enzyme structures representing the different states during catalytic reaction
Synechococcus elongatus PCC 7942 = FACHB-805 R2
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