Cloned (Comment) | Organism |
---|---|
gene PMT_1231, recombinant expression in Escherichia coli | Prochlorococcus marinus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
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 | Prochlorococcus marinus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | essential, di-iron center | Prochlorococcus marinus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | 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+ | Prochlorococcus marinus MIT9313 | - |
an alkane + formate + H2O + 2 NADP+ | - |
? |
Organic Solvent | Comment | Organism |
---|---|---|
additional information | solvent isotope effects on alkane formation by the enzyme have mechanistic implications | Prochlorococcus marinus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Prochlorococcus marinus | Q7V6D4 | - |
- |
Prochlorococcus marinus MIT9313 | Q7V6D4 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli | Prochlorococcus marinus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+ | proposed mechanism for deformylation of aldehydes by cADO, overview. 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 | Prochlorococcus marinus |
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+ | - |
Prochlorococcus marinus MIT9313 | an alkane + formate + H2O + 2 NADP+ | - |
? | |
additional information | enzyme assay in anaerobic conditions, quantification of hydrocarbon products by GC-MS | Prochlorococcus marinus | ? | - |
? | |
additional information | enzyme assay in anaerobic conditions, quantification of hydrocarbon products by GC-MS | Prochlorococcus marinus MIT9313 | ? | - |
? | |
n-octadecanal + O2 + 2 NADPH + 2 H+ | - |
Prochlorococcus marinus | heptadecane + formate + H2O + 2 NADP+ | - |
? | |
n-octadecanal + O2 + 2 NADPH + 2 H+ | - |
Prochlorococcus marinus MIT9313 | heptadecane + formate + H2O + 2 NADP+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
cyanobacterial aldehyde deformylating oxygenase | - |
Prochlorococcus marinus |
PMT_1231 | - |
Prochlorococcus marinus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Prochlorococcus marinus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.8 | - |
- |
Prochlorococcus marinus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | - |
Prochlorococcus marinus |
General Information | Comment | Organism |
---|---|---|
additional information | solvent isotope effects on alkane formation by cyanobacterial aldehyde deformylating oxygenase and their mechanistic implications, overview | Prochlorococcus marinus |