EC Number | Application | Comment | Organism |
---|---|---|---|
4.1.99.5 | 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 |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
4.1.99.5 | Fe2+ | nonheme di-iron center | Prochlorococcus marinus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.99.5 | a long-chain aldehyde + O2 + 2 NADPH + 2 H+ | Prochlorococcus marinus | - |
an alkane + formate + H2O + 2 NADP+ | - |
? | |
4.1.99.5 | a long-chain aldehyde + O2 + 2 NADPH + 2 H+ | Prochlorococcus marinus MIT 9313 | - |
an alkane + formate + H2O + 2 NADP+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.99.5 | Prochlorococcus marinus | Q7V6D4 | - |
- |
4.1.99.5 | Prochlorococcus marinus MIT 9313 | Q7V6D4 | - |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
4.1.99.5 | octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+ | reaction mechanism, overview | Prochlorococcus marinus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.99.5 | a long-chain aldehyde + O2 + 2 NADPH + 2 H+ | - |
Prochlorococcus marinus | an alkane + formate + H2O + 2 NADP+ | - |
? | |
4.1.99.5 | 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+ | - |
? | |
4.1.99.5 | a long-chain aldehyde + O2 + 2 NADPH + 2 H+ | - |
Prochlorococcus marinus MIT 9313 | an alkane + formate + H2O + 2 NADP+ | - |
? | |
4.1.99.5 | 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+ | - |
? | |
4.1.99.5 | 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 | ? | - |
? | |
4.1.99.5 | 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 | ? | - |
? | |
4.1.99.5 | n-undecanal + O2 + 2 NADPH + 2 H+ | - |
Prochlorococcus marinus | n-decane + formate + H2O + 2 NADP+ | - |
? | |
4.1.99.5 | n-undecanal + O2 + 2 NADPH + 2 H+ | - |
Prochlorococcus marinus MIT 9313 | n-decane + formate + H2O + 2 NADP+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.1.99.5 | More | enzyme structure analysis | Prochlorococcus marinus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.99.5 | cADO | - |
Prochlorococcus marinus |
4.1.99.5 | cyanobacterial aldehyde-deformylating oxygenase | - |
Prochlorococcus marinus |
4.1.99.5 | PMT_1231 | - |
Prochlorococcus marinus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.1.99.5 | NADPH | - |
Prochlorococcus marinus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
4.1.99.5 | 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 |
4.1.99.5 | 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 |