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Literature summary for 4.1.99.5 extracted from

  • Shokri, A.; Que, L.
    Conversion of aldehyde to alkane by a peroxoiron(III) complex a functional model for the cyanobacterial aldehyde-deformylating oxygenase (2015), J. Am. Chem. Soc., 137, 7686-7691 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.99.5

Application

Application Comment Organism
biofuel production the conversion of long-chain fatty aldehydes to corresponding alkanes, that is catalyzed by cyanobacterial aldehyde-deformylating oxygenase (cADO), is probably useful for production of biofuel Prochlorococcus marinus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ nonheme di-iron center Prochlorococcus marinus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ Prochlorococcus marinus
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 an alkane + formate + H2O + 2 NADP+
-
 ?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ Prochlorococcus marinus MIT 9313
-
 an alkane + formate + H2O + 2 NADP+
-
 ?

Organism

Organism UniProt Comment Textmining
Prochlorococcus marinus Q7V6D4
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-
Prochlorococcus marinus MIT 9313 Q7V6D4
-
-

Reaction

Reaction Comment Organism Reaction ID
octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+ reaction mechanism, overview Prochlorococcus marinus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
 Prochlorococcus marinus an alkane + formate + H2O + 2 NADP+
-
 ?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ 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 Prochlorococcus marinus an alkane + formate + H2O + 2 NADP+
-
 ?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
 Prochlorococcus marinus MIT 9313 an alkane + formate + H2O + 2 NADP+
-
 ?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ 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 Prochlorococcus marinus MIT 9313 an alkane + formate + H2O + 2 NADP+
-
 ?
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 Prochlorococcus marinus ?
-
 ?
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 Prochlorococcus marinus MIT 9313 ?
-
 ?
n-undecanal + O2 + 2 NADPH + 2 H+
-
 Prochlorococcus marinus n-decane + formate + H2O + 2 NADP+
-
 ?
n-undecanal + O2 + 2 NADPH + 2 H+
-
 Prochlorococcus marinus MIT 9313 n-decane + formate + H2O + 2 NADP+
-
 ?

Subunits

Subunits Comment Organism
More enzyme structure analysis Prochlorococcus marinus

Synonyms

Synonyms Comment Organism
cADO
-
 Prochlorococcus marinus
cyanobacterial aldehyde-deformylating oxygenase
-
 Prochlorococcus marinus
PMT_1231
-
 Prochlorococcus marinus

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Prochlorococcus marinus

General Information

General Information Comment Organism
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 Prochlorococcus marinus
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 Prochlorococcus marinus