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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Cofactor
Cofactor on EC 4.1.99.5 - aldehyde oxygenase (deformylating)
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Ferredoxin
identification of Synechocystis sp. PC 6803 ssl0020 ferredoxin, PetF, UniProt ID P27320, as an efficient ADO reductant, overview
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additional information
ferredoxin-mediated the cytochrome c reduction with ferredoxin-NADP+ reductase: ADO is selective against ferredoxin and the interaction between ferredoxin and ferredoxin-NADP+ reductase is very important for efficient electron transfer and ADO activity
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