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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Metals Ions
Metals Ions on EC 4.1.99.5 - aldehyde oxygenase (deformylating)
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Co2+
Fe2+
additional information
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noncorrin-cobalt-containing enzyme, 1 Co-porphyrin per alphabeta pair of subunits
Fe2+
di-iron enzyme, Moessbauer spectrum of the cofactor during the reaction steps, coordinations of the different cofactor states, e.g. the peroxo-Fe2 III/III intermediate, Fe2 III/III peroxyhemiacetal complex, or a micro-oxo-Fe2 III/III cluster, detailed overview
Fe2+
di-iron center, the amount of hydrocarbons produced in recombinant Escherichia coli is decreased when the iron concentration in the M9 medium is decreased. The Cys-to-Ala/Ser mutations do not affect the iron binding to the enzyme
Fe2+
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di-iron centre, coordinated by two histidine residues and four carboxylates from glutamate side chains
Fe2+
di-iron center, Glu144 is one of the iron-coordinating residues and 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. The highly labile feature of cADO di-iron center seems to be responsible for the low enzymatic activity. Six conservative amino acids, loctaed in two EX28-29EX2H motifs, from four helices (Glu32 from helix H1, Glu115 from helix H4, Glu60 and His63 from helix H2, and Glu144 and His147 from helix H5) act as metal ligands. The WT0 structure is characterized by losing the di-iron cluster and by exhibiting a distorted conformation of helix H5. This structure is likely to represent the inactive state of SeADO, as it has lost its cofactor iron