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2-(2-tetradecylcyclopropyl)acetaldehyde + 2 NADH + O2 + 2 H+
1-methyl-2-tetradecylcyclopropane + formate + H2O + 2 NAD+
-
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
-
?
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+
-
with reducing system NADH/phenazine methosulfate
-
-
?
fatty aldehyde + O2 + NADPH
alkane + formate + H2O + NADP+
-
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)
-
-
?
heptanal + O2 + 2 NAD(P)H + 2 H+
hexane + formate + H2O + 2 NAD(P)+
-
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
-
-
?
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
-
-
?
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
-
?
pentadecanal + O2 + 2 NADH + 2 H+
tetradecane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate
GC-MS poduct analysis
-
?
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+
-
with reducing system NADH/phenazine methosulfate
-
-
?
trans-3-pentadecanyloxirane-2-carbaldehyde + 2 NADH + O2 + 2 H+
2-pentadecanyloxirane + formate + 2 NAD+ + H2O
-
with reducing system NADH/phenazine methosulfate
-
-
?
additional information
?
-
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
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
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
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
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
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
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
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
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
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+
-
with reducing system NADH/phenazine methosulfate
GC-MS poduct analysis
-
?
butanal + O2 + 2 NADH + 2 H+
propane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate
GC-MS poduct analysis
-
?
decanal + O2 + 2 NADH + 2 H+
nonane + formate + H2O + 2 NAD+
with reducing system NADH/phenazine
-
-
?
decanal + O2 + 2 NADH + 2 H+
nonane + formate + H2O + 2 NAD+
with reducing system NADH/phenazine
-
-
?
heptanal + O2 + 2 NADH + 2 H+
hexane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
GC-MS poduct analysis
-
?
heptanal + O2 + 2 NADH + 2 H+
hexane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
GC-MS poduct analysis
-
?
heptanal + O2 + 2 NADH + 2 H+
hexane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
GC-MS poduct analysis
-
?
heptanal + O2 + 2 NADH + 2 H+
hexane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
GC-MS poduct analysis
-
?
heptanal + O2 + 2 NADH + 2 H+
hexane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
GC-MS poduct analysis
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
long-chain aldehyde + O2 + 2 NADPH + 2 H+
alkane + formate + H2O + 2 NADP+
-
-
-
-
?
long-chain aldehyde + O2 + 2 NADPH + 2 H+
alkane + 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-butanal + O2 + 2 NADPH + 2 H+
n-propane + formate + H2O + 2 NADP+
-
-
-
?
n-butanal + O2 + 2 NADPH + 2 H+
n-propane + formate + H2O + 2 NADP+
-
-
-
?
n-butanal + O2 + 2 NADPH + 2 H+
n-propane + formate + H2O + 2 NADP+
-
-
-
?
n-butanal + O2 + 2 NADPH + 2 H+
n-propane + formate + H2O + 2 NADP+
-
-
-
?
n-butanal + O2 + 2 NADPH + 2 H+
n-propane + formate + H2O + 2 NADP+
-
-
-
?
n-butanal + O2 + 2 NADPH + 2 H+
n-propane + 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-decanal + O2 + 2 NADPH + 2 H+
n-nonane + formate + H2O + 2 NADP+
-
-
-
?
n-decanal + O2 + 2 NADPH + 2 H+
n-nonane + 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+
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
n-heptanal + O2 + 2 NADPH + 2 H+
n-hexane + formate + H2O + 2 NADP+
-
-
-
?
n-heptanal + O2 + 2 NADPH + 2 H+
n-hexane + formate + H2O + 2 NADP+
-
-
-
-
?
n-heptanal + O2 + 2 NADPH + 2 H+
n-hexane + formate + H2O + 2 NADP+
-
-
-
?
n-heptanal + O2 + 2 NADPH + 2 H+
n-hexane + formate + H2O + 2 NADP+
-
-
-
?
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-hexadecanal + O2 + 2 NADPH + 2 H+
pentadecane + formate + H2O + 2 NADP+
-
-
-
?
n-hexadecanal + O2 + 2 NADPH + 2 H+
pentadecane + formate + H2O + 2 NADP+
-
-
-
?
n-hexadecanal + O2 + 2 NADPH + 2 H+
pentadecane + 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-hexanal + O2 + 2 NADPH + 2 H+
n-pentane + formate + H2O + 2 NADP+
-
-
-
?
n-hexanal + O2 + 2 NADPH + 2 H+
n-pentane + formate + H2O + 2 NADP+
-
-
-
?
n-hexanal + O2 + 2 NADPH + 2 H+
n-pentane + formate + H2O + 2 NADP+
-
-
-
?
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
-
-
?
n-hexanal + O2 + 2 NADPH + 2 H+
n-pentane + formate + H2O + 2 NADP+
-
-
-
?
n-hexanal + O2 + 2 NADPH + 2 H+
n-pentane + 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-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)+
endogenous reducing system ferredoxin-mediated the cytochrome c reduction with ferredoxin-NADP+ reductase
-
-
?
octadecanal + O2 + 2 NADH + 2 H+
heptadecane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate
-
-
?
octadecanal + O2 + 2 NADH + 2 H+
heptadecane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate
GC-MS poduct analysis
-
?
octadecanal + O2 + 2 NADH + 2 H+
heptadecane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
GC-MS poduct analysis
-
?
octadecanal + O2 + 2 NADH + 2 H+
heptadecane + formate + H2O + 2 NAD+
with reducing system NADH/phenazine
-
-
?
octadecanal + O2 + 2 NADH + 2 H+
heptadecane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate
GC-MS poduct analysis
-
?
octadecanal + O2 + 2 NADH + 2 H+
heptadecane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
-
-
?
octadecanal + O2 + 2 NADH + 2 H+
heptadecane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
GC-MS poduct analysis
-
?
octadecanal + O2 + 2 NADH + 2 H+
heptadecane + formate + H2O + 2 NAD+
with reducing system NADH/phenazine
-
-
?
octadecanal + O2 + 2 NADH + 2 H+
heptadecane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
GC-MS poduct analysis
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?
octadecanal + O2 + 2 NADH + 2 H+
heptadecane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate
GC-MS poduct analysis
-
?
octadecanal + O2 + 2 NADH + 2 H+
heptadecane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
GC-MS poduct analysis
-
?
octadecanal + O2 + 2 NADH + 2 H+
heptadecane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
GC-MS poduct analysis
-
?
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+
-
the in vitro activity of the enzyme depends on the presence of a reducing system, i.e. NADPH, ferredoxin, and ferredoxin reductase
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-
?
pentanal + O2 + 2 NADH + 2 H+
butane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate
GC-MS poduct analysis
-
?
pentanal + O2 + 2 NADH + 2 H+
butane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate
GC-MS poduct analysis
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?
additional information
?
-
-
responsible for a key step in the biosynthesis of hydrocarbon compounds
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?
additional information
?
-
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final step in alkane biosynthesis
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?
additional information
?
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final step in alkane biosynthesis
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?
additional information
?
-
-
final step in alkane biosynthesis
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?
additional information
?
-
-
final step in alkane biosynthesis
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-
?
additional information
?
-
substrate binding site analysis
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?
additional information
?
-
substrate binding site analysis
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-
?
additional information
?
-
-
the aldehyde hydrogen is retained in the HCO2- and the hydrogen in the nascent methyl group of the alkane originates, at least in part, from solvent. The reaction appears to be formally hydrolytic, but the improbability of a hydrolytic mechanism having the primary carbanion as the leaving group, the structural similarity of the aldehyde decarbonylases to other O2-activating non-heme di-iron proteins, and the dependence of in vitro aldehyde decarbonylase activity on the presence of a reducing system implicate some type of redox mechanism. Two possible resolutions to this conundrum, overview
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-
?
additional information
?
-
cyanobacterial aldehyde-deformylating oxygenases catalyze conversion of saturated or monounsaturated Cn fatty aldehydes to formate and the corresponding Cn-1 alkanes or alkenes, respectively
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-
?
additional information
?
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cyanobacterial aldehyde-deformylating oxygenases catalyze conversion of saturated or monounsaturated Cn fatty aldehydes to formate and the corresponding Cn-1 alkanes or alkenes, respectively
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-
?
additional information
?
-
-
the enzyme catalyzes the unusual hydrolysis of aldehydes to produce alkanes and formate. The reaction requires an external reducing system but does not require oxygen. The enzyme catalyzes aldehyde decarbonylation at a much faster rate under anaerobic conditions, and the oxygen in formate derives from water. Eventhough an oxygen-dependent mechanism may operate in cAD, the oxygen-independent decarbonylation of aldehydes is a general feature of these enzymes
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-
?
additional information
?
-
-
the enzyme is more active with either long-chain (C18-C14) or short-chain (C9-C5) aldehydes whereas medium chain aldehydes, including dodecanal, are turned over considerably more slowly
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-
?
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
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-
?
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
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-
?
additional information
?
-
GC-MS analysis of the volatile alkane products
-
-
?
additional information
?
-
GC-MS measurements and identification of products
-
-
?
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
-
-
?
additional information
?
-
GC-MS analysis of the volatile alkane products
-
-
?
additional information
?
-
GC-MS measurements and identification of products
-
-
?
additional information
?
-
substrate binding site analysis
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-
?
additional information
?
-
-
alkane biosynthesis
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-
?
additional information
?
-
-
alkane biosynthesis
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-
?
additional information
?
-
-
final step in alkane biosynthesis
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-
?
additional information
?
-
-
natural specificity of cADO to favour reactivity against short-chain over long-chain aldehydes
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-
?
additional information
?
-
substrate specificity, overview. Marked decrease in relative yields of aldehyde and alcohol products are observed as the alkyl chain length is decreased from C9 to C8. The relative yields of the one-carbon-shorter alcohol and aldehyde products are optimal with nonanal and decanal and decrease with shorter and longer alkyl chains
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-
?
additional information
?
-
-
the enzyme catalyzes the conversion of Cn fatty aldehydes to formate and the corresponding Cn-1 alk(a/e)nes. This apparently hydrolytic reaction is actually a cryptically redox oxygenation process, in which one O-atom is incorporated from O2 into formate and a protein-based reducing system (NADPH, ferredoxin, and ferredoxin reductase) provides all four electrons needed for the complete reduction of O2, absolute O2 requirement for formate production
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-
?
additional information
?
-
-
the enzyme catalyzes the unusual hydrolysis of aldehydes to produce alkanes and formate. The reaction requires an external reducing system but does not require oxygen. The enzyme catalyzes aldehyde decarbonylation at a much faster rate under anaerobic conditions, and the oxygen in formate derives from water. Eventhough an oxygen-dependent mechanism may operate in cAD, the oxygen-independent decarbonylation of aldehydes is a general feature of these enzymes
-
-
?
additional information
?
-
cyanobacterial aldehyde-deformylating oxygenase (cADO) converts long-chain fatty aldehydes to alkanes via a proposed diferric-peroxo intermediate that carries out the oxidative deformylation of the substrate. The synthetic iron(III)-peroxo complex [FeIII(eta2deltaO2)(TMC)]+ (TMC is tetramethylcyclam) causes a similar transformation in the presence of a suitable H atom donor, thus serving as a functional model for cADO, reaction analysis with undecanal as substrate, detailed overview. Mechanistic studies suggest that the H atom donor can intercept the incipient alkyl radical formed in the oxidative deformylation step in competition with the oxygen rebound step typically used by most oxygenases for forming C-O bonds
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-
?
additional information
?
-
enzyme assay in anaerobic conditions, quantification of hydrocarbon products by GC-MS
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-
?
additional information
?
-
GC-MS analysis of the volatile alkane products
-
-
?
additional information
?
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NMR studies of substrate Binding to cADO
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-
?
additional information
?
-
NMR studies of substrate Binding to cADO
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-
?
additional information
?
-
cyanobacterial aldehyde-deformylating oxygenase (cADO) converts long-chain fatty aldehydes to alkanes via a proposed diferric-peroxo intermediate that carries out the oxidative deformylation of the substrate. The synthetic iron(III)-peroxo complex [FeIII(eta2deltaO2)(TMC)]+ (TMC is tetramethylcyclam) causes a similar transformation in the presence of a suitable H atom donor, thus serving as a functional model for cADO, reaction analysis with undecanal as substrate, detailed overview. Mechanistic studies suggest that the H atom donor can intercept the incipient alkyl radical formed in the oxidative deformylation step in competition with the oxygen rebound step typically used by most oxygenases for forming C-O bonds
-
-
?
additional information
?
-
GC-MS analysis of the volatile alkane products
-
-
?
additional information
?
-
substrate specificity, overview. Marked decrease in relative yields of aldehyde and alcohol products are observed as the alkyl chain length is decreased from C9 to C8. The relative yields of the one-carbon-shorter alcohol and aldehyde products are optimal with nonanal and decanal and decrease with shorter and longer alkyl chains
-
-
?
additional information
?
-
-
the enzyme catalyzes the unusual hydrolysis of aldehydes to produce alkanes and formate. The reaction requires an external reducing system but does not require oxygen. The enzyme catalyzes aldehyde decarbonylation at a much faster rate under anaerobic conditions, and the oxygen in formate derives from water. Eventhough an oxygen-dependent mechanism may operate in cAD, the oxygen-independent decarbonylation of aldehydes is a general feature of these enzymes
-
-
?
additional information
?
-
-
natural specificity of cADO to favour reactivity against short-chain over long-chain aldehydes
-
-
?
additional information
?
-
enzyme assay in anaerobic conditions, quantification of hydrocarbon products by GC-MS
-
-
?
additional information
?
-
the endogenous electron transfer system works more effectively than the heterologous and chemical ones, e.g. phenazine methosulfate or 1-methyoxy-5-methylphenazinium methylsulfate and NADH, overview
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-
?
additional information
?
-
the endogenous electron transfer system works more effectively than the heterologous and chemical ones, e.g. phenazine methosulfate or 1-methyoxy-5-methylphenazinium methylsulfate and NADH, overview
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-
?
additional information
?
-
cADO shows extreme low activity with kcat value below 1/min
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-
?
additional information
?
-
-
cADO shows extreme low activity with kcat value below 1/min
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-
?
additional information
?
-
substrate specificity of recombinant wild-type and mutant enzymes, overview. The wild-type prefers long-chain substrates, but some mutants show also higher activity with short-chain substrates. Analysis of preferred substrates in the presence of the competition substrates for wild-type and mutants enzymes
-
-
?
additional information
?
-
the in vitro reaction catalyzed by cADO requires both the dioxygen as co-substrate and the presence of a reducing system, which provides four electrons per turnover and can either be biological (ferredoxin, ferredoxin reductase, and NADPH) or chemical (phenazine methosulfate and NADH)
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-
?
additional information
?
-
substrate specificity of recombinant wild-type and mutant enzymes, overview. The wild-type prefers long-chain substrates, but some mutants show also higher activity with short-chain substrates. Analysis of preferred substrates in the presence of the competition substrates for wild-type and mutants enzymes
-
-
?
additional information
?
-
cADO shows extreme low activity with kcat value below 1/min
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-
?
additional information
?
-
the in vitro reaction catalyzed by cADO requires both the dioxygen as co-substrate and the presence of a reducing system, which provides four electrons per turnover and can either be biological (ferredoxin, ferredoxin reductase, and NADPH) or chemical (phenazine methosulfate and NADH)
-
-
?
additional information
?
-
-
the enzyme catalyzes the unusual hydrolysis of aldehydes to produce alkanes and formate. The reaction requires an external reducing system but does not require oxygen. The enzyme catalyzes aldehyde decarbonylation at a much faster rate under anaerobic conditions, and the oxygen in formate derives from water. Eventhough an oxygen-dependent mechanism may operate in cAD, the oxygen-independent decarbonylation of aldehydes is a general feature of these enzymes
-
-
?
additional information
?
-
GC-MS analysis of the volatile alkane products
-
-
?
additional information
?
-
-
the enzyme catalyzes the unusual hydrolysis of aldehydes to produce alkanes and formate. The reaction requires an external reducing system but does not require oxygen. The enzyme catalyzes aldehyde decarbonylation at a much faster rate under anaerobic conditions, and the oxygen in formate derives from water. Eventhough an oxygen-dependent mechanism may operate in cAD, the oxygen-independent decarbonylation of aldehydes is a general feature of these enzymes
-
-
?
additional information
?
-
GC-MS analysis of the volatile alkane products
-
-
?
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evolution
cyanobacterial aldehyde-deformylating oxygenases belong to the ferritin-like diiron-carboxylate superfamily of dioxygen-activating proteins
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
evolution
the enzyme belongs to the superfamily of ferritin-like di-iron proteins with conserved sequence of two EX28-29EX2H motifs
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
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evolution
-
the enzyme belongs to the superfamily of ferritin-like di-iron proteins with conserved sequence of two EX28-29EX2H motifs
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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
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
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
-
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
-
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
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
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
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
-
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
-
physiological function
-
alkane biosynthesis pathway
physiological function
-
saturated fatty acids are converted to alkanes (and unsaturated fatty acids to alkenes) in cyanobacteria entailing scission of the C1-C2 bond of a fatty aldehyde intermediate by the enzyme aldehyde decarbonylase. The in vitro activity of the enzyme depends on the presence of a reducing system, i.e. NADPH, ferredoxin, and ferredoxin reductase
physiological function
aldehyde deformylating oxygenase is a key enzyme for alkane biosynthesis in cyanobacteria
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
physiological function
aldehyde-deformylating oxygenase (ADO) is an important enzyme involved in the biosynthetic pathway of fatty alk(a/e)nes in cyanobacteria
physiological function
aldehyde-deformylating oxygenase (ADO) is an important enzyme involved in the biosynthetic pathway of fatty alk(a/e)nes in cyanobacteria. ADO transforms the fatty aldehyde to a Cn-1 hydrocarbon and C1-derived formate
physiological function
cyanobacterial aldehyde-deformylating oxygenase (cADO) catalyzes the conversion of Cn fatty aldehyde to its corresponding Cn-1 alk(a/e)ne with low activity due to a highly labile feature of cADO di-iron center
physiological function
enzyme ADO natively catalyzes the conversion of long-chain aldehydes into corresponding alkanes. To convert short-chain isobutyraldehyde into propane efficiently, the substrate specificity of ADO has to be modified for the utilization of the short-chain aldehydes
physiological function
the cyanobacterial aldehyde deformylating oxygenase (cADO) is a key enzyme that catalyzes the unusual deformylation of aliphatic aldehydes for alkane biosynthesis
physiological function
the cyanobacterial aldehyde deformylating oxygenase (cADO) is a key enzyme that catalyzes the unusual deformylation of aliphatic aldehydes for alkane biosynthesis
physiological function
the nonheme diiron enzyme cyanobacterial aldehyde deformylating oxygenase, cADO, catalyzes the deformylation of aliphatic aldehydes to alkanes and formate
physiological function
-
aldehyde-deformylating oxygenase (ADO) is an important enzyme involved in the biosynthetic pathway of fatty alk(a/e)nes in cyanobacteria. ADO transforms the fatty aldehyde to a Cn-1 hydrocarbon and C1-derived formate
-
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
-
physiological function
-
aldehyde deformylating oxygenase is a key enzyme for alkane biosynthesis in cyanobacteria
-
physiological function
-
the nonheme diiron enzyme cyanobacterial aldehyde deformylating oxygenase, cADO, catalyzes the deformylation of aliphatic aldehydes to alkanes and formate
-
physiological function
-
enzyme ADO natively catalyzes the conversion of long-chain aldehydes into corresponding alkanes. To convert short-chain isobutyraldehyde into propane efficiently, the substrate specificity of ADO has to be modified for the utilization of the short-chain aldehydes
-
physiological function
-
the cyanobacterial aldehyde deformylating oxygenase (cADO) is a key enzyme that catalyzes the unusual deformylation of aliphatic aldehydes for alkane biosynthesis
-
physiological function
-
aldehyde-deformylating oxygenase (ADO) is an important enzyme involved in the biosynthetic pathway of fatty alk(a/e)nes in cyanobacteria
-
physiological function
-
cyanobacterial aldehyde-deformylating oxygenase (cADO) catalyzes the conversion of Cn fatty aldehyde to its corresponding Cn-1 alk(a/e)ne with low activity due to a highly labile feature of cADO di-iron center
-
additional information
-
the definitive reaffirmation of the oxygenative nature of the reaction implies that the enzyme, initially designated as aldehyde decarbonylase when the C1-derived coproduct is thought to be carbon monoxide rather than formate, should be redesignated as aldehyde-deformylating oxygenase, ADO
additional information
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the enzyme shows a mainly alpha helical architecture, with a ferritin-like four-helix bundle. The latter contains the di-iron centre, coordinated by two histidine residues and four carboxylates from glutamate side chains. Substrates access the active site through a tunnel-like hydrophobic pocket. Active site structure analysis from crystal structure, PDB ID 20C5
additional information
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the very low activity of the enzyme appears to result from inhibition by the ferredoxin reducing system used in the assay and the low solubility of the substrate
additional information
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the very low activity of the enzyme appears to result from inhibition by the ferredoxin reducing system used in the assay and the low solubility of the substrate
additional information
-
the very low activity of the enzyme appears to result from inhibition by the ferredoxin reducing system used in the assay and the low solubility of the substrate
additional information
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the very low activity of the enzyme appears to result from inhibition by the ferredoxin reducing system used in the assay and the low solubility of the substrate
additional information
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
additional information
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
additional information
Glu144, one of the iron-coordinating residues, plays a vital role in the catalytic reaction of cADO. The helix, in which Glu144 resides, exhibits two distinct conformations that correlate with the different binding states of the di-iron center in cADO structures. Enzyme structure analysis, comparisons of wild-type and mutant structures, overview. A continuous tube-shaped non-protein electron density, resembling a lipid molecule, is observed close to the di-iron center in all structures but the Y122F structure, a hydrophobic substrate channel in SeADO is described
additional information
residue L194, at the center of the hydrophobic cavity, might serve as a gateway for substrate entry, but L194 does not play a kinetically significant role in limiting substrate access to the active site. Structure of metal-free cADO, overview
additional information
residues close to the di-iron center (Tyr39, Gln110, Tyr122), the protein surface (Trp178), and involved in the hydrogen-bonding network (Arg62, Asp143) and the oligopeptide whose conformation changed (Leu/Thr146, Leu148, Asn149 and Tyr/Phe150) in the absence of the diiron center are identified. 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
additional information
-
residues close to the di-iron center (Tyr39, Gln110, Tyr122), the protein surface (Trp178), and involved in the hydrogen-bonding network (Arg62, Asp143) and the oligopeptide whose conformation changed (Leu/Thr146, Leu148, Asn149 and Tyr/Phe150) in the absence of the diiron center are identified. 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
additional information
solvent isotope effects on alkane formation by cyanobacterial aldehyde deformylating oxygenase and their mechanistic implications, overview
additional information
the enzyme structure consists of eight a-helices found in ferritin-like di-iron proteins. Residues Tyr21, Ile27, Val28, Phe67, Phe86, Phe87, Phe117, Ala118, Ala121, Tyr122, Try125, and Tyr184 contributing to substrate binding, and Glu32, Glu60, His63, Glu115, Glu144, and His147 participating in iron coordination. OsADO structure resembles ADO structures with active sites containing both metal co-factor and substrate, OsADO active site is fully occupied, helix 5 of OsADO with an iron bound in the active site is a long helix
additional information
the enzyme structure consists of eight a-helices found in ferritin-like di-iron proteins. Residues Tyr21, Ile27, Val28, Phe67, Phe86, Phe87, Phe117, Ala118, Ala121, Tyr122, Try125, and Tyr184 contributing to substrate binding, and Glu32, Glu60, His63, Glu115, Glu144, and His147 participating in iron coordination. The LiADO structure resembles ADO structures with an empty active site, the LiADO active site is vacant of iron and substrates, helix 5 of LiADO, which lacks iron in the active site, presents two conformations (one long and two short helices), indicating that an equilibrium exists between the two states in solution
additional information
the synthetic iron(III)-peroxo complex [FeIII(eta2deltaO2)(TMC)]+ (TMC is tetramethylcyclam) causes a similar transformation in the presence of a suitable H atom donor, thus serving as a functional model for cADO, reaction analysis with undecanal with [FeIII(TMC)(delta2deltaO2)]+, detailed overview
additional information
-
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
-
additional information
-
residue L194, at the center of the hydrophobic cavity, might serve as a gateway for substrate entry, but L194 does not play a kinetically significant role in limiting substrate access to the active site. Structure of metal-free cADO, overview
-
additional information
-
the synthetic iron(III)-peroxo complex [FeIII(eta2deltaO2)(TMC)]+ (TMC is tetramethylcyclam) causes a similar transformation in the presence of a suitable H atom donor, thus serving as a functional model for cADO, reaction analysis with undecanal with [FeIII(TMC)(delta2deltaO2)]+, detailed overview
-
additional information
-
the very low activity of the enzyme appears to result from inhibition by the ferredoxin reducing system used in the assay and the low solubility of the substrate
-
additional information
-
the enzyme shows a mainly alpha helical architecture, with a ferritin-like four-helix bundle. The latter contains the di-iron centre, coordinated by two histidine residues and four carboxylates from glutamate side chains. Substrates access the active site through a tunnel-like hydrophobic pocket. Active site structure analysis from crystal structure, PDB ID 20C5
-
additional information
-
solvent isotope effects on alkane formation by cyanobacterial aldehyde deformylating oxygenase and their mechanistic implications, overview
-
additional information
-
the enzyme structure consists of eight a-helices found in ferritin-like di-iron proteins. Residues Tyr21, Ile27, Val28, Phe67, Phe86, Phe87, Phe117, Ala118, Ala121, Tyr122, Try125, and Tyr184 contributing to substrate binding, and Glu32, Glu60, His63, Glu115, Glu144, and His147 participating in iron coordination. The LiADO structure resembles ADO structures with an empty active site, the LiADO active site is vacant of iron and substrates, helix 5 of LiADO, which lacks iron in the active site, presents two conformations (one long and two short helices), indicating that an equilibrium exists between the two states in solution
-
additional information
-
residues close to the di-iron center (Tyr39, Gln110, Tyr122), the protein surface (Trp178), and involved in the hydrogen-bonding network (Arg62, Asp143) and the oligopeptide whose conformation changed (Leu/Thr146, Leu148, Asn149 and Tyr/Phe150) in the absence of the diiron center are identified. 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
-
additional information
-
Glu144, one of the iron-coordinating residues, plays a vital role in the catalytic reaction of cADO. The helix, in which Glu144 resides, exhibits two distinct conformations that correlate with the different binding states of the di-iron center in cADO structures. Enzyme structure analysis, comparisons of wild-type and mutant structures, overview. A continuous tube-shaped non-protein electron density, resembling a lipid molecule, is observed close to the di-iron center in all structures but the Y122F structure, a hydrophobic substrate channel in SeADO is described
-
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C107A
site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme
C107A/C117A
site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme
C117A
site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme
C71A
site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme
C71A/C107A
site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant
C71A/C107A/C117A
site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant
C71A/C117A
site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant
C71S
site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme
C107A
-
site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme
-
C107A/C117A
-
site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme
-
C117A
-
site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme
-
C71A
-
site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme
-
C71S
-
site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme
-
I127G
site-directed mutagenesis, increased activity compared to wild-type
I127G/A48G
site-directed mutagenesis, increased activity compared to wild-type
L194A
site-directed mutagenesis, the mutant has kinetic properties very similar to the wild-type enzyme
V41Y
-
site-directed mutagenesis, the mutant has the same global architecture as wild-type enzyme, the mutant shows highly reduced activity with the majority of long-chain aldehyde substrates tested
V41Y/A134F
-
site-directed mutagenesis, the double mutant shows reduced activity with long-chain aldehyde substrates and increased activity with short-chain aldehyde substrates like the single mutants
A134F
-
site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type
-
I127G
-
site-directed mutagenesis, increased activity compared to wild-type
-
I127G/A48G
-
site-directed mutagenesis, increased activity compared to wild-type
-
L194A
-
site-directed mutagenesis, the mutant has kinetic properties very similar to the wild-type enzyme
-
A134F
-
site-directed mutagenesis, the mutant has the same global architecture as wild-type enzyme, the mutant shows highly reduced activity with the majority of long-chain aldehyde substrates tested. the A134F variant displays an approximate fourfold increase in the rate of butanal consumption and approximately sixfold increase in pentanal consumption compared to wild-type enzyme, the mutant generates enhanced levels of propane production in whole-cell biotransformations compared to wild-type cADO
-
V41Y
-
site-directed mutagenesis, the mutant has the same global architecture as wild-type enzyme, the mutant shows highly reduced activity with the majority of long-chain aldehyde substrates tested
-
V41Y/A134F
-
site-directed mutagenesis, the double mutant shows reduced activity with long-chain aldehyde substrates and increased activity with short-chain aldehyde substrates like the single mutants
-
A118F
site-directed mutagenesis, the mutant shows increased activity with n-butanal compared to the wild-type enzyme. A118F does not show any obvious activity against C14,16,18 aldehydes, and only exhibits slight activity towards n-dodecanal and n-decanal for long-chain substrates
A121F
site-directed mutagenesis, the mutant shows increased activity with C4,6,7 aldehydes compared to the wild-type enzyme
C70F
site-directed mutagenesis, the mutant shows increased activity with n-hexanal compared to the wild-type enzyme
D143A
site-directed mutagenesis, altered activity compared to wild-type
D49H
site-directed mutagenesis, altered activity compared to wild-type
F150Y
site-directed mutagenesis, altered activity compared to wild-type
F86Y/F87Y
site-directed mutagenesis, structure comparison with the wild-type enzyme
F87Y
site-directed mutagenesis, the mutant shows increased activity with n-decanal compared to the wild-type enzyme
G31F
site-directed mutagenesis
I24Y
site-directed mutagenesis, the mutant shows increased activity with n-heptanal compared to the wild-type enzyme
I27F
site-directed mutagenesis, the mutant shows increased activity with n-decanal and n-dodecanal compared to the wild-type enzyme
L146T
site-directed mutagenesis, altered activity compared to wild-type
L198F
site-directed mutagenesis, the mutant shows increased activity with C7-10 aldehydescompared to the wild-type enzyme
M193Y
site-directed mutagenesis, the mutant shows increased activity with C6-10 aldehydes compared to the wild-type enzyme
N123H
site-directed mutagenesis, altered activity compared to wild-type
N149A
site-directed mutagenesis, altered activity compared to wild-type
Q110L
site-directed mutagenesis, altered activity compared to wild-type
Q49H/F150Y
site-directed mutagenesis, altered activity compared to wild-type
Q49H/N123H/F150Y
site-directed mutagenesis, altered activity compared to wild-type
R62A
site-directed mutagenesis, altered activity compared to wild-type
V184F
site-directed mutagenesis, the mutant shows increased activity with n-dodecanal and n-decanal compared to the wild-type enzyme
V28F
site-directed mutagenesis, the mutant shows increased activity with n-dodecanal compared to the wild-type enzyme
W178R
site-directed mutagenesis, altered activity compared to wild-type
Y21R
site-directed mutagenesis
Y39F
site-directed mutagenesis, altered activity compared to wild-type
D143A
-
site-directed mutagenesis, altered activity compared to wild-type
-
F86Y/F87Y
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
-
F87Y
-
site-directed mutagenesis, the mutant shows increased activity with n-decanal compared to the wild-type enzyme
-
I24Y
-
site-directed mutagenesis, the mutant shows increased activity with n-heptanal compared to the wild-type enzyme
-
L198F
-
site-directed mutagenesis, the mutant shows increased activity with C7-10 aldehydescompared to the wild-type enzyme
-
R62A
-
site-directed mutagenesis, altered activity compared to wild-type
-
Y21R
-
site-directed mutagenesis
-
Y39F
-
site-directed mutagenesis, altered activity compared to wild-type
-
D49H
site-directed mutagenesis, altered activity compared to wild-type
D49H/N123H
site-directed mutagenesis, altered activity compared to wild-type
L148R
site-directed mutagenesis, altered activity compared to wild-type
N123H
site-directed mutagenesis, altered activity compared to wild-type
T146L
site-directed mutagenesis, altered activity compared to wild-type
Y150F
site-directed mutagenesis, altered activity compared to wild-type
A134F
-
site-directed mutagenesis, the mutant has the same global architecture as wild-type enzyme, the mutant shows highly reduced activity with the majority of long-chain aldehyde substrates tested. the A134F variant displays an approximate fourfold increase in the rate of butanal consumption and approximately sixfold increase in pentanal consumption compared to wild-type enzyme, the mutant generates enhanced levels of propane production in whole-cell biotransformations compared to wild-type cADO
A134F
site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type
Y122F
site-directed mutagenesis, structure comparison with the wild-type enzyme
Y122F
site-directed mutagenesis, altered activity compared to wild-type
Y122F
-
site-directed mutagenesis, altered activity compared to wild-type
-
Y122F
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
-
additional information
installation of a recombinant hydrocarbon production system in Escherichia coli strain BL21(DE3)DELTAyqhDDELTAahr for production of n-alkanes by a combinant ion of four enzymes, i.e. aldehyde deformylating oxygenase (from Nostoc punctiforme ), ferredoxin (from Synechocystis), phosphopantetheinyl transferase (from Bacillus subtilis) and carboxylic acid reductase (from Mycobacterium marinum), method optimization and evaluation, overview. GC-MS analysis of the volatile alkanes produced. Comparison of ADO orthologues from different origins in hydrocarbon biosynthesis in vivo
additional information
-
installation of a recombinant hydrocarbon production system in Escherichia coli strain BL21(DE3)DELTAyqhDDELTAahr for production of n-alkanes by a combinant ion of four enzymes, i.e. aldehyde deformylating oxygenase (from Nostoc punctiforme ), ferredoxin (from Synechocystis), phosphopantetheinyl transferase (from Bacillus subtilis) and carboxylic acid reductase (from Mycobacterium marinum), method optimization and evaluation, overview. GC-MS analysis of the volatile alkanes produced. Comparison of ADO orthologues from different origins in hydrocarbon biosynthesis in vivo
-
additional information
-
alteration of the enzyme's substrate specificity by engineering of active site residues involved in substrate binding, residues V41 and A134, adjacent to the C9 position of the ligand, might influence fatty acid binding, overview
additional information
installation of a recombinant hydrocarbon production system in Escherichia coli strain BL21(DE3)DELTAyqhDDELTAahr for production of n-alkanes by a combinant ion of four enzymes, i.e. aldehyde deformylating oxygenase (from Prochlorococcus marinus, wild-type and mutant A134F), ferredoxin (from Synechocystis), phosphopantetheinyl transferase (from Bacillus subtilis) and carboxylic acid reductase (from Mycobacterium marinum), method optimization and evaluation, overview. GC-MS analysis of the volatile alkanes produced. Comparison of ADO orthologues from different origins in hydrocarbon biosynthesis in vivo
additional information
screening for Prochlorococcus marinus enzyme ADO mutants generated by engineering the active center to accommodate branched-chain isobutyraldehyde, identification of two ADO mutants, I127G and I127G/A48G, which exhibit higher catalytic activity for isobutyraldehyde and 3fold improved propane productivity compared to wild-type, propane biosynthesis generation
additional information
-
screening for Prochlorococcus marinus enzyme ADO mutants generated by engineering the active center to accommodate branched-chain isobutyraldehyde, identification of two ADO mutants, I127G and I127G/A48G, which exhibit higher catalytic activity for isobutyraldehyde and 3fold improved propane productivity compared to wild-type, propane biosynthesis generation
-
additional information
-
installation of a recombinant hydrocarbon production system in Escherichia coli strain BL21(DE3)DELTAyqhDDELTAahr for production of n-alkanes by a combinant ion of four enzymes, i.e. aldehyde deformylating oxygenase (from Prochlorococcus marinus, wild-type and mutant A134F), ferredoxin (from Synechocystis), phosphopantetheinyl transferase (from Bacillus subtilis) and carboxylic acid reductase (from Mycobacterium marinum), method optimization and evaluation, overview. GC-MS analysis of the volatile alkanes produced. Comparison of ADO orthologues from different origins in hydrocarbon biosynthesis in vivo
-
additional information
-
alteration of the enzyme's substrate specificity by engineering of active site residues involved in substrate binding, residues V41 and A134, adjacent to the C9 position of the ligand, might influence fatty acid binding, overview
-
additional information
cADO is engineered to improve specificity for short- to medium-chain aldehydes, site-directed mutagenesis of some residues in analogy to the more active enzyme from Prochlorococcus marinus strain MIT9313
additional information
-
cADO is engineered to improve specificity for short- to medium-chain aldehydes, site-directed mutagenesis of some residues in analogy to the more active enzyme from Prochlorococcus marinus strain MIT9313
additional information
enzyme structure analysis, comparisons of wild-type and mutant structures, overview
additional information
structure-guided protein engineering to alter substrate specificity of aldehyde-deformylating oxygenase towards aldehydes carbon chain length. The impact of the engineered cADO mutants on the change of the hydrocarbon profile is demonstrated by co-expressing acyl-ACP thioesterase BTE, fadD and V184F in Escherichia coli, showing that n-undecane is the main fatty alkane
additional information
-
structure-guided protein engineering to alter substrate specificity of aldehyde-deformylating oxygenase towards aldehydes carbon chain length. The impact of the engineered cADO mutants on the change of the hydrocarbon profile is demonstrated by co-expressing acyl-ACP thioesterase BTE, fadD and V184F in Escherichia coli, showing that n-undecane is the main fatty alkane
-
additional information
-
cADO is engineered to improve specificity for short- to medium-chain aldehydes, site-directed mutagenesis of some residues in analogy to the more active enzyme from Prochlorococcus marinus strain MIT9313
-
additional information
-
enzyme structure analysis, comparisons of wild-type and mutant structures, overview
-
additional information
installation of a recombinant hydrocarbon production system in Escherichia coli strain BL21(DE3)DELTAyqhDDELTAahr for production of n-alkanes by a combinant ion of four enzymes, i.e. aldehyde deformylating oxygenase (from Synechococcus sp. RS9917), ferredoxin (from Synechocystis), phosphopantetheinyl transferase (from Bacillus subtilis) and carboxylic acid reductase (from Mycobacterium marinum), method optimization and evaluation, overview. GC-MS analysis of the volatile alkanes produced. Comparison of ADO orthologues from different origins in hydrocarbon biosynthesis in vivo
additional information
cADO is engineered to improve specificity for short- to medium-chain aldehydes, site-directed mutagenesis of some residues in analogy to the more active enzyme from Prochlorococcus marinus strain MIT9313
additional information
installation of a recombinant hydrocarbon production system in Escherichia coli strain BL21(DE3)DELTAyqhDDELTAahr for production of n-alkanes by a combinant ion of four enzymes, i.e. aldehyde deformylating oxygenase (from Synechocystis sp. PCC 6803), ferredoxin (from Synechocystis), phosphopantetheinyl transferase (from Bacillus subtilis) and carboxylic acid reductase (from Mycobacterium marinum), method optimization and evaluation, overview. GC-MS analysis of the volatile alkanes produced. Comparison of ADO orthologues from different origins in hydrocarbon biosynthesis in vivo
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Cheesbrough, T.M.; Kolattukudy, P.E.
Alkane biosynthesis by decarbonylation of aldehydes catalyzed by a particulate preparation from Pisum sativum
Proc. Natl. Acad. Sci. USA
81
6613-6617
1984
Pisum sativum
brenda
Cheesbrough, T.M.; Kolattukudy, P.E.
Microsomal preparation from an animal tissue catalyzes release of carbon monoxide from a fatty aldehyde to generate an alkane
J. Biol. Chem.
263
2738-2743
1988
Podiceps nigricollis
brenda
Dennis, M.W.; Kolattukubdy, P.E.
Alkane biosynthesis by decarbonylation of aldehyde catalyzed by a microsomal preparation from Botryococcus braunii
Arch. Biochem. Biophys.
287
268-275
1991
Botryococcus braunii, Botryococcus braunii Austin
brenda
Dennis, M.; Kolattukudy, P.E.
A cobalt-porphyrin enzyme converts a fatty aldehyde to a hydrocarbon and CO
Proc. Natl. Acad. Sci. USA
89
5306-5310
1992
Botryococcus braunii, Botryococcus braunii Austin
brenda
Schneider-Belhaddad, F.; Kolattukudy, P.
Solubilization, partial purification, and characterization of a fatty aldehyde decarbonylase from a higher plant, Pisum sativum
Arch. Biochem. Biophys.
377
341-349
2000
Pisum sativum
brenda
Kobayashi, M.; Shimizu, S.
Cobalt proteins
Eur. J. Biochem.
261
1-9
1999
Botryococcus braunii
brenda
Schirmer, A.; Rude, M.A.; Li, X.; Popova, E.; del Cardayre, S.B.
Microbial biosynthesis of alkanes
Science
329
559-562
2010
Nostoc punctiforme
brenda
Warui, D.M.; Li, N.; N?rgaard, H.; Krebs, C.; Bollinger, J.M.; Booker, S.J.
Detection of formate, rather than carbon monoxide, as the stoichiometric coproduct in conversion of fatty aldehydes to alkanes by a cyanobacterial aldehyde decarbonylase
J. Am. Chem. Soc.
133
3316-3319
2011
Nostoc punctiforme
brenda
Li, N.; Nrgaard, H.; Warui, D.M.; Booker, S.J.; Krebs, C.; Bollinger, J.M.
Conversion of fatty aldehydes to alka(e)nes and formate by a cyanobacterial aldehyde decarbonylase: cryptic redox by an unusual dimetal oxygenase
J. Am. Chem. Soc.
133
6158-6161
2011
Nostoc punctiforme
brenda
Aukema, K.G.; Makris, T.M.; Stoian, S.A.; Richman, J.E.; Muenck, E.; Lipscomb, J.D.; Wackett, L.P.
Cyanobacterial aldehyde deformylase oxygenation of aldehydes yields n-1 aldehydes and alcohols in addition to alkanes
ACS Catal.
3
2228-2238
2013
Prochlorococcus marinus (Q7V6D4), Prochlorococcus marinus MIT 9313 (Q7V6D4)
brenda
Das, D.; Ellington, B.; Paul, B.; Marsh, E.N.
Mechanistic insights from reaction of alpha-oxiranyl-aldehydes with cyanobacterial aldehyde deformylating oxygenase
ACS Chem. Biol.
9
570-577
2014
Nostoc punctiforme
brenda
Eser, B.E.; Das, D.; Han, J.; Jones, P.R.; Marsh, E.N.
Oxygen-independent alkane formation by non-heme iron-dependent cyanobacterial aldehyde decarbonylase: investigation of kinetics and requirement for an external electron donor
Biochemistry
50
10743-10750
2011
Synechocystis sp., Nostoc punctiforme, Prochlorococcus marinus, Synechococcus sp., Prochlorococcus marinus MIT9313
brenda
Li, N.; Chang, W.C.; Warui, D.M.; Booker, S.J.; Krebs, C.; Bollinger, J.M.
Evidence for only oxygenative cleavage of aldehydes to alk(a/e)nes and formate by cyanobacterial aldehyde decarbonylases
Biochemistry
51
7908-7916
2012
Prochlorococcus marinus
brenda
Zhang, J.; Lu, X.; Li, J.J.
Conversion of fatty aldehydes into alk (a/e)nes by in vitro reconstituted cyanobacterial aldehyde-deformylating oxygenase with the cognate electron transfer system
Biotechnol. Biofuels
6
86
2013
Synechococcus elongatus (Q54764), Synechococcus elongatus PCC 7942 (Q54764)
brenda
Khara, B.; Menon, N.; Levy, C.; Mansell, D.; Das, D.; Marsh, E.N.; Leys, D.; Scrutton, N.S.
Production of propane and other short-chain alkanes by structure-based engineering of ligand specificity in aldehyde-deformylating oxygenase
ChemBioChem
14
1204-1208
2013
Prochlorococcus marinus, Prochlorococcus marinus MIT9313
brenda
Pandelia, M.E.; Li, N.; Noergaard, H.; Warui, D.M.; Rajakovich, L.J.; Chang, W.C.; Booker, S.J.; Krebs, C.; Bollinger, J.M.
Substrate-triggered addition of dioxygen to the diferrous cofactor of aldehyde-deformylating oxygenase to form a diferric-peroxide intermediate
J. Am. Chem. Soc.
135
15801-15812
2013
Nostoc punctiforme (B2J1M1), Nostoc punctiforme
brenda
Paul, B.; Das, D.; Ellington, B.; Marsh, E.N.
Probing the mechanism of cyanobacterial aldehyde decarbonylase using a cyclopropyl aldehyde
J. Am. Chem. Soc.
135
5234-5237
2013
Nostoc punctiforme
brenda
Buer, B.C.; Paul, B.; Das, D.; Stuckey, J.A.; Marsh, E.N.
Insights into substrate and metal binding from the crystal structure of cyanobacterial aldehyde deformylating oxygenase with substrate bound
ACS Chem. Biol.
9
2584-2593
2014
Prochlorococcus marinus (Q7V6D4), Prochlorococcus marinus MIT 9313 (Q7V6D4)
brenda
Park, A.K.; Kim, I.S.; Jeon, B.W.; Roh, S.J.; Ryu, M.Y.; Baek, H.R.; Jo, S.W.; Kim, Y.S.; Park, H.; Lee, J.H.; Yoon, H.S.; Kim, H.W.
Crystal structures of aldehyde deformylating oxygenase from Limnothrix sp. KNUA012 and Oscillatoria sp. KNUA011
Biochem. Biophys. Res. Commun.
477
395-400
2016
Oscillatoria sp. KNUA011 (A0A191T887), Limnothrix redekei (A0A191T893), Limnothrix redekei KNUA012 (A0A191T893)
brenda
Waugh, M.W.; Marsh, E.N.
Solvent isotope effects on alkane formation by cyanobacterial aldehyde deformylating oxygenase and their mechanistic implications
Biochemistry
53
5537-5543
2014
Prochlorococcus marinus (Q7V6D4), Prochlorococcus marinus MIT9313 (Q7V6D4)
brenda
Warui, D.M.; Pandelia, M.E.; Rajakovich, L.J.; Krebs, C.; Bollinger, J.M.; Booker, S.J.
Efficient delivery of long-chain fatty aldehydes from the Nostoc punctiforme acyl-acyl carrier protein reductase to its cognate aldehyde-deformylating oxygenase
Biochemistry
54
1006-1015
2015
Nostoc punctiforme (B2J1M1), Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102 (B2J1M1)
brenda
Bao, L.; Li, J.J.; Jia, C.; Li, M.; Lu, X.
Structure-oriented substrate specificity engineering of aldehyde-deformylating oxygenase towards aldehydes carbon chain length
Biotechnol. Biofuels
9
185
2016
Synechococcus elongatus PCC 7942 = FACHB-805 (Q54764), Synechococcus elongatus PCC 7942 = FACHB-805 R2 (Q54764)
brenda
Zhang, L.; Liang, Y.; Wu, W.; Tan, X.; Lu, X.
Microbial synthesis of propane by engineering valine pathway and aldehyde-deformylating oxygenase
Biotechnol. Biofuels
9
80
2016
Prochlorococcus marinus (Q7V6D4), Prochlorococcus marinus MIT 9313 (Q7V6D4)
brenda
Wang, Q.; Bao, L.; Jia, C.; Li, M.; Li, J.J.; Lu, X.
Identification of residues important for the activity of aldehyde-deformylating oxygenase through investigation into the structure-activity relationship
BMC Biotechnol.
17
31-39
2017
Synechococcus elongatus PCC 7942 = FACHB-805 (Q54764), Synechococcus elongatus PCC 7942 = FACHB-805, Synechocystis sp. PCC 6803 (Q55688), Synechococcus elongatus PCC 7942 = FACHB-805 R2 (Q54764)
brenda
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
J. Am. Chem. Soc.
137
11695-11709
2015
Nostoc punctiforme (B2J1M1), Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102 (B2J1M1)
brenda
Shokri, A.; Que, L.
Conversion of aldehyde to alkane by a peroxoiron(III) complex a functional model for the cyanobacterial aldehyde-deformylating oxygenase
J. Am. Chem. Soc.
137
7686-7691
2015
Prochlorococcus marinus (Q7V6D4), Prochlorococcus marinus MIT 9313 (Q7V6D4)
brenda
Patrikainen, P.; Carbonell, V.; Thiel, K.; Aro, E.M.; Kallio, P.
Comparison of orthologous cyanobacterial aldehyde deformylating oxygenases in the production of volatile C3-C7 alkanes in engineered E. coli
Metab. Eng. Commun.
5
9-18
2017
Synechococcus sp. RS9917 (A3Z5H6), Nostoc punctiforme (B2J1M1), Synechocystis sp. PCC 6803 (Q55688), Prochlorococcus marinus (Q7V6D4), Nostoc punctiforme ATCC 29133 / PCC 73102 (B2J1M1), Prochlorococcus marinus MIT 9313 (Q7V6D4)
brenda
Hayashi, Y.; Yasugi, F.; Arai, M.
Role of cysteine residues in the structure, stability, and alkane producing activity of cyanobacterial aldehyde deformylating oxygenase
PLoS ONE
10
e0122217
2015
Nostoc punctiforme (B2J1M1), Nostoc punctiforme ATCC 29133 / PCC 73102 (B2J1M1)
brenda
Jia, C.; Li, M.; Li, J.; Zhang, J.; Zhang, H.; Cao, P.; Pan, X.; Lu, X.; Chang, W.
Structural insights into the catalytic mechanism of aldehyde-deformylating oxygenases
Protein Cell
6
55-67
2015
Synechococcus elongatus PCC 7942 = FACHB-805 (Q54764), Synechococcus elongatus PCC 7942 = FACHB-805 R2 (Q54764)
brenda