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octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+
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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
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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
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2-(2-tetradecylcyclopropyl)acetaldehyde + 2 NADH + O2 + 2 H+
1-methyl-2-tetradecylcyclopropane + formate + H2O + 2 NAD+
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formation of 1-octadecene at low level appears to be described by first-order kinetics, 1-octadecene might be involved in enzyme inhibition
GC-MS poduct analysis
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a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
butanal + O2 + 2 NADH + 2 H+
propane + formate + H2O + 2 NAD+
decanal + O2 + 2 NADH + 2 H+
nonane + formate + H2O + 2 NAD+
dodecanal + O2 + 2 NADH + 2 H+
undecane + formate + H2O + 2 NAD+
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with reducing system NADH/phenazine methosulfate
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fatty aldehyde + O2 + NADPH
alkane + formate + H2O + NADP+
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reaction requires dioxygen and results in incorporation of 18O from 18O2 into formate, activity depends on the presence of a reducing system (NADPH, ferredoxin and ferredoxin reductase)
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heptanal + O2 + 2 NAD(P)H + 2 H+
hexane + formate + H2O + 2 NAD(P)+
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with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
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?
heptanal + O2 + 2 NADH + 2 H+
hexane + formate + H2O + 2 NAD+
hexadecanal + O2 + 2 NAD(P)H + 2 H+
pentadecane + formate + H2O + 2 NAD(P)+
isobutyraldehyde + O2 + 2 NADPH + 2 H+
propane + formate + H2O + 2 NADP+
long-chain aldehyde + O2 + 2 NADPH + 2 H+
alkane + formate + H2O + 2 NADP+
n-butanal + O2 + 2 NADPH + 2 H+
n-propane + formate + H2O + 2 NADP+
n-decanal + O2 + 2 NADPH + 2 H+
n-nonane + formate + H2O + 2 NADP+
n-dodecanal + O2 + 2 NADPH + 2 H+
undecane + formate + H2O + 2 NADP+
n-heptanal + O2 + 2 NAD(P)H + 2 H+
n-hexane + formate + H2O + 2 NAD(P)+
n-heptanal + O2 + 2 NADPH + 2 H+
n-hexane + formate + H2O + 2 NADP+
n-hexadecanal + O2 + 2 NADPH + 2 H+
pentadecane + formate + H2O + 2 NADP+
n-hexanal + O2 + 2 NADPH + 2 H+
n-pentane + formate + H2O + 2 NADP+
n-nonanal + O2 + 2 NADPH + 2 H+
n-octane + formate + H2O + 2 NADP+
mutant M193Y and L198F exhibit a 1.7 and 2.0fold increase in kcat, respectively, compared to wild-type, while kcat value of I24Y is much lower than that of the wild-type, and those of C70F and A121F are about half of that of wild-type
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n-octadecanal + O2 + 2 NADPH + 2 H+
heptadecane + formate + H2O + 2 NADP+
n-octadecenal + O2 + 2 NADPH + 2 H+
1-heptadecene + formate + H2O + 2 NADP+
n-octanal + O2 + 2 NADPH + 2 H+
n-heptane + formate + H2O + 2 NADP+
n-undecanal + O2 + 2 NADPH + 2 H+
n-decane + formate + H2O + 2 NADP+
nonanal + O2 + 2 NADH + 2 H+
octane + formate + H2O + 2 NAD+
octadecanal
heptadecane + CO
octadecanal + NADPH + O2
heptadecane + formate + H2O + NADP+
octadecanal + O2 + 2 NAD(P)H + 2 H+
heptadecane + formate + H2O + 2 NAD(P)+
octadecanal + O2 + 2 NADH + 2 H+
heptadecane + formate + H2O + 2 NAD+
octadecanal + O2 + 2 NADPH + 2 H+
heptadecane + formate + H2O + 2 NADP+
octanal + O2 + 2 NADH + 2 H+
heptane + formate + H2O + 2 NAD+
with reducing system NADH/phenazine methosulfate, reaction under anaerobic conditions to protect the cofactor, but the enzyme shows no differences between aerobic and anaerobic condition, meaning that the substrate does not bind tightly to the Fe2 III/III form of the enzyme or that the aldehyde binds in a manner that does not detectably alter its Moessbauer properties
GC-MS poduct analysis
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?
pentadecanal + O2 + 2 NADH + 2 H+
tetradecane + formate + H2O + 2 NAD+
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with reducing system NADH/phenazine methosulfate
GC-MS poduct analysis
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?
pentanal + O2 + 2 NADH + 2 H+
butane + formate + H2O + 2 NAD+
trans-3-nonyloxirane-2-carbaldehyde + 2 NADH + 2 H+
2-nonyloxirane + formate + H2O + 2 NAD+
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with reducing system NADH/phenazine methosulfate
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?
trans-3-pentadecanyloxirane-2-carbaldehyde + 2 NADH + O2 + 2 H+
2-pentadecanyloxirane + formate + 2 NAD+ + H2O
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with reducing system NADH/phenazine methosulfate
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?
additional information
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a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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
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a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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
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?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
C-H-bond-formation by enzyme cADO. The enzyme requires O2 to carry out the oxidative deformylation of substrate to form alkane and formate. The formate product derives an O atom from O2 and retains the aldehyde C-H bond, and the terminal methyl group of the alkane product incorporates an H atom from solvent
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a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
C-H-bond-formation by enzyme cADO. The enzyme requires O2 to carry out the oxidative deformylation of substrate to form alkane and formate. The formate product derives an O atom from O2 and retains the aldehyde C-H bond, and the terminal methyl group of the alkane product incorporates an H atom from solvent
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a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
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butanal + O2 + 2 NADH + 2 H+
propane + formate + H2O + 2 NAD+
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with reducing system NADH/phenazine methosulfate
GC-MS poduct analysis
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butanal + O2 + 2 NADH + 2 H+
propane + formate + H2O + 2 NAD+
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with reducing system NADH/phenazine methosulfate
GC-MS poduct analysis
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?
decanal + O2 + 2 NADH + 2 H+
nonane + formate + H2O + 2 NAD+
with reducing system NADH/phenazine
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decanal + O2 + 2 NADH + 2 H+
nonane + formate + H2O + 2 NAD+
with reducing system NADH/phenazine
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?
heptanal + O2 + 2 NADH + 2 H+
hexane + formate + H2O + 2 NAD+
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with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
GC-MS poduct analysis
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?
heptanal + O2 + 2 NADH + 2 H+
hexane + formate + H2O + 2 NAD+
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with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
GC-MS poduct analysis
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?
heptanal + O2 + 2 NADH + 2 H+
hexane + formate + H2O + 2 NAD+
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with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
GC-MS poduct analysis
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?
heptanal + O2 + 2 NADH + 2 H+
hexane + formate + H2O + 2 NAD+
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with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
GC-MS poduct analysis
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?
heptanal + O2 + 2 NADH + 2 H+
hexane + formate + H2O + 2 NAD+
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with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
GC-MS poduct analysis
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?
hexadecanal + O2 + 2 NAD(P)H + 2 H+
pentadecane + formate + H2O + 2 NAD(P)+
endogenous reducing system ferredoxin-mediated the cytochrome c reduction with ferredoxin-NADP+ reductase
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hexadecanal + O2 + 2 NAD(P)H + 2 H+
pentadecane + formate + H2O + 2 NAD(P)+
endogenous reducing system ferredoxin-mediated the cytochrome c reduction with ferredoxin-NADP+ reductase
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?
isobutyraldehyde + O2 + 2 NADPH + 2 H+
propane + formate + H2O + 2 NADP+
low activity with the wild-type enzyme, but increased activity with enzyme mutants I127G and I127G/A48G
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isobutyraldehyde + O2 + 2 NADPH + 2 H+
propane + formate + H2O + 2 NADP+
low activity with the wild-type enzyme, but increased activity with enzyme mutants I127G and I127G/A48G
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long-chain aldehyde + O2 + 2 NADPH + 2 H+
alkane + formate + H2O + 2 NADP+
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long-chain aldehyde + O2 + 2 NADPH + 2 H+
alkane + formate + H2O + 2 NADP+
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long-chain aldehyde + O2 + 2 NADPH + 2 H+
alkane + formate + H2O + 2 NADP+
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n-butanal + O2 + 2 NADPH + 2 H+
n-propane + formate + H2O + 2 NADP+
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?
n-butanal + O2 + 2 NADPH + 2 H+
n-propane + formate + H2O + 2 NADP+
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?
n-butanal + O2 + 2 NADPH + 2 H+
n-propane + formate + H2O + 2 NADP+
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?
n-butanal + O2 + 2 NADPH + 2 H+
n-propane + formate + H2O + 2 NADP+
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?
n-butanal + O2 + 2 NADPH + 2 H+
n-propane + formate + H2O + 2 NADP+
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?
n-butanal + O2 + 2 NADPH + 2 H+
n-propane + formate + H2O + 2 NADP+
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?
n-butanal + O2 + 2 NADPH + 2 H+
n-propane + formate + H2O + 2 NADP+
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?
n-butanal + O2 + 2 NADPH + 2 H+
n-propane + formate + H2O + 2 NADP+
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?
n-decanal + O2 + 2 NADPH + 2 H+
n-nonane + formate + H2O + 2 NADP+
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?
n-decanal + O2 + 2 NADPH + 2 H+
n-nonane + formate + H2O + 2 NADP+
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?
n-decanal + O2 + 2 NADPH + 2 H+
n-nonane + formate + H2O + 2 NADP+
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n-decanal + O2 + 2 NADPH + 2 H+
n-nonane + formate + H2O + 2 NADP+
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n-dodecanal + O2 + 2 NADPH + 2 H+
undecane + formate + H2O + 2 NADP+
mutants show increased activity with n-dodecanal compared to wild-type: V184F 4.4fold, F87Y 2.5fold, I27F 2.1fold and V28Y 2.0fold. Yields of n-undecane of wild-type and some cADO mutants against n-dodecanal in the presence of the competition substrates, overview
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n-dodecanal + O2 + 2 NADPH + 2 H+
undecane + formate + H2O + 2 NADP+
mutants show increased activity with n-dodecanal compared to wild-type: V184F 4.4fold, F87Y 2.5fold, I27F 2.1fold and V28Y 2.0fold. Yields of n-undecane of wild-type and some cADO mutants against n-dodecanal in the presence of the competition substrates, overview
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n-heptanal + O2 + 2 NAD(P)H + 2 H+
n-hexane + formate + H2O + 2 NAD(P)+
endogenous reducing system ferredoxin-mediated the cytochrome c reduction with ferredoxin-NADP+ reductase
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n-heptanal + O2 + 2 NAD(P)H + 2 H+
n-hexane + formate + H2O + 2 NAD(P)+
endogenous reducing system ferredoxin-mediated the cytochrome c reduction with ferredoxin-NADP+ reductase
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n-heptanal + O2 + 2 NADPH + 2 H+
n-hexane + formate + H2O + 2 NADP+
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n-heptanal + O2 + 2 NADPH + 2 H+
n-hexane + formate + H2O + 2 NADP+
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n-heptanal + O2 + 2 NADPH + 2 H+
n-hexane + formate + H2O + 2 NADP+
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n-heptanal + O2 + 2 NADPH + 2 H+
n-hexane + formate + H2O + 2 NADP+
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n-heptanal + O2 + 2 NADPH + 2 H+
n-hexane + formate + H2O + 2 NADP+
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n-hexadecanal + O2 + 2 NADPH + 2 H+
pentadecane + formate + H2O + 2 NADP+
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n-hexadecanal + O2 + 2 NADPH + 2 H+
pentadecane + formate + H2O + 2 NADP+
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n-hexadecanal + O2 + 2 NADPH + 2 H+
pentadecane + formate + H2O + 2 NADP+
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n-hexadecanal + O2 + 2 NADPH + 2 H+
pentadecane + formate + H2O + 2 NADP+
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n-hexadecanal + O2 + 2 NADPH + 2 H+
pentadecane + formate + H2O + 2 NADP+
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n-hexanal + O2 + 2 NADPH + 2 H+
n-pentane + formate + H2O + 2 NADP+
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n-hexanal + O2 + 2 NADPH + 2 H+
n-pentane + formate + H2O + 2 NADP+
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n-hexanal + O2 + 2 NADPH + 2 H+
n-pentane + formate + H2O + 2 NADP+
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n-hexanal + O2 + 2 NADPH + 2 H+
n-pentane + formate + H2O + 2 NADP+
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n-hexanal + O2 + 2 NADPH + 2 H+
n-pentane + formate + H2O + 2 NADP+
mutants A121F, C70F, M193Y, and L198F show 2.7, 2.5, 1.7 and 1.4fold increase in kcatapp against n-hexanal, respectively, compared to wild-type enzyme
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n-hexanal + O2 + 2 NADPH + 2 H+
n-pentane + formate + H2O + 2 NADP+
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n-hexanal + O2 + 2 NADPH + 2 H+
n-pentane + formate + H2O + 2 NADP+
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-
?
n-octadecanal + O2 + 2 NADPH + 2 H+
heptadecane + formate + H2O + 2 NADP+
-
-
-
?
n-octadecanal + O2 + 2 NADPH + 2 H+
heptadecane + formate + H2O + 2 NADP+
-
-
-
?
n-octadecanal + O2 + 2 NADPH + 2 H+
heptadecane + formate + H2O + 2 NADP+
-
-
-
?
n-octadecanal + O2 + 2 NADPH + 2 H+
heptadecane + formate + H2O + 2 NADP+
-
-
-
?
n-octadecanal + O2 + 2 NADPH + 2 H+
heptadecane + formate + H2O + 2 NADP+
-
-
-
?
n-octadecenal + O2 + 2 NADPH + 2 H+
1-heptadecene + formate + H2O + 2 NADP+
-
-
-
?
n-octadecenal + O2 + 2 NADPH + 2 H+
1-heptadecene + formate + H2O + 2 NADP+
-
-
-
?
n-octanal + O2 + 2 NADPH + 2 H+
n-heptane + formate + H2O + 2 NADP+
-
-
-
?
n-octanal + O2 + 2 NADPH + 2 H+
n-heptane + formate + H2O + 2 NADP+
-
-
-
?
n-octanal + O2 + 2 NADPH + 2 H+
n-heptane + formate + H2O + 2 NADP+
-
-
-
?
n-octanal + O2 + 2 NADPH + 2 H+
n-heptane + formate + H2O + 2 NADP+
binding of 1-[13C]-octanal to enzyme cADO is monitored by 13C NMR
-
-
?
n-octanal + O2 + 2 NADPH + 2 H+
n-heptane + formate + H2O + 2 NADP+
binding of 1-[13C]-octanal to enzyme cADO is monitored by 13C NMR
-
-
?
n-octanal + O2 + 2 NADPH + 2 H+
n-heptane + formate + H2O + 2 NADP+
-
-
-
?
n-octanal + O2 + 2 NADPH + 2 H+
n-heptane + formate + H2O + 2 NADP+
mutant M193Y show 3.2fold improved activity, and mutants A121F and L198F exhibit comparable activity to wild-type, while mutants I24Y and C70F display much lower activity compared to wild-type
-
-
?
n-octanal + O2 + 2 NADPH + 2 H+
n-heptane + formate + H2O + 2 NADP+
-
-
-
?
n-octanal + O2 + 2 NADPH + 2 H+
n-heptane + formate + H2O + 2 NADP+
-
-
-
?
n-undecanal + O2 + 2 NADPH + 2 H+
n-decane + formate + H2O + 2 NADP+
-
-
-
?
n-undecanal + O2 + 2 NADPH + 2 H+
n-decane + formate + H2O + 2 NADP+
-
-
-
?
nonanal + O2 + 2 NADH + 2 H+
octane + formate + H2O + 2 NAD+
with reducing system NADH/phenazine
-
-
?
nonanal + O2 + 2 NADH + 2 H+
octane + formate + H2O + 2 NAD+
with reducing system NADH/phenazine
-
-
?
octadecanal
heptadecane + CO
-
-
-
?
octadecanal
heptadecane + CO
-
-
-
?
octadecanal
heptadecane + CO
-
-
-
?
octadecanal
heptadecane + CO
-
-
-
?
octadecanal
heptadecane + CO
-
-
-
?
octadecanal
heptadecane + CO
-
-
-
?
octadecanal
heptadecane + CO
-
-
-
?
octadecanal
heptadecane + CO
-
-
-
r
octadecanal + NADPH + O2
heptadecane + formate + H2O + NADP+
-
activity depends on the presence of a reducing system (NADPH, ferredoxin and ferredoxin reductase)
-
-
?
octadecanal + NADPH + O2
heptadecane + formate + H2O + NADP+
-
only observed in the presence of ferredoxin, ferredoxin reductase and NADPH
-
-
?
octadecanal + O2 + 2 NAD(P)H + 2 H+
heptadecane + formate + H2O + 2 NAD(P)+
endogenous reducing system ferredoxin-mediated the cytochrome c reduction with ferredoxin-NADP+ reductase
-
-
?
octadecanal + O2 + 2 NAD(P)H + 2 H+
heptadecane + formate + H2O + 2 NAD(P)+
4.1.99.5 aldehyde oxygenase (deformylating)
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