4.1.99.5: aldehyde oxygenase (deformylating)
This is an abbreviated version!
For detailed information about aldehyde oxygenase (deformylating), go to the full flat file.
Word Map on EC 4.1.99.5
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4.1.99.5
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biofuels
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decarbonylation
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acyl-acyl
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punctiforme
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elongatus
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octadecanal
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di-iron
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drop-in
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cados
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heptadecane
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ferritin-like
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prochlorococcus
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diferric
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photodecarboxylase
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petroleum-derived
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biofuel production
- 4.1.99.5
-
biofuels
-
decarbonylation
-
acyl-acyl
- punctiforme
- elongatus
- octadecanal
-
di-iron
-
drop-in
-
cados
- heptadecane
-
ferritin-like
- prochlorococcus
-
diferric
-
photodecarboxylase
-
petroleum-derived
- biofuel production
Reaction
+ + 2 NADPH + 2 H+ = + + + 2 NADP+
Synonyms
ADO, aldehyde decarbonylase, aldehyde deformylase, aldehyde deformylating oxygenase, aldehyde-deformylating oxygenase, CAD, cADO, cADO-1593, cyanobacterial ADO, cyanobacterial aldehyde decarbonylase, cyanobacterial aldehyde deformylating oxygenase, cyanobacterial aldehyde-deformylating oxygenase, decarbonylase, erial aldehyde-deformylating oxygenase, LiADO, More, Npun_R1711, OsADO, PMT1231, PMT_1231, RS9917_09941, SeADO, sll0208, Synpcc7942_1593
ECTree
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KM Value
KM Value on EC 4.1.99.5 - aldehyde oxygenase (deformylating)
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0.18
n-octanal
pH 7.2, 37°C, recombinant wild-type enzyme and mutant A121F
0.2
recombinant mutant F150Y, pH and temperature not specified in the publication
0.244
n-Heptanal
pH 7.2, 22°C, recombinant enzyme with Fd/FNR system
0.3
n-Heptanal
recombinant wild-type enzyme, pH and temperature not specified in the publication
0.32
n-Heptanal
recombinant mutant L148R, pH and temperature not specified in the publication
0.33
n-Heptanal
recombinant mutant Q49H/F150Y, pH and temperature not specified in the publication
0.34
n-Heptanal
recombinant mutant L146T, pH and temperature not specified in the publication
0.34
n-Heptanal
recombinant mutant W178R, pH and temperature not specified in the publication
0.35
n-Heptanal
recombinant wild-type enzyme, pH and temperature not specified in the publication
0.35
n-Heptanal
recombinant mutant Q49H/N123H/F150Y, pH and temperature not specified in the publication
0.38
n-Heptanal
recombinant mutant D49H/N123H, pH and temperature not specified in the publication
0.56
n-Heptanal
pH 7.2, 37°C, recombinant mutant A121F
0.59
n-Heptanal
pH 7.2, 37°C, recombinant wild-type enzyme
0.93
pH 7.2, 37°C, recombinant wild-type enzyme
0.96
n-hexanal
pH 7.2, 37°C, recombinant mutant A121F
0.069
pH 7.2, 37°C, recombinant wild-type enzyme
0.14
n-nonanal
pH 7.2, 37°C, recombinant mutant A121F
additional information
Michaelis-Menten kinetics
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additional information
additional information
complex kinetics of formation of the reaction intermediate, overview
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additional information
additional information
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complex kinetics of formation of the reaction intermediate, overview
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additional information
additional information
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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