EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.99.5 | overexpression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Prochlorococcus marinus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.99.5 | Prochlorococcus marinus | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.99.5 | heptanal + O2 + 2 NAD(P)H + 2 H+ | with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase | Prochlorococcus marinus | hexane + formate + H2O + 2 NAD(P)+ | - |
? | |
4.1.99.5 | additional information | the enzyme catalyzes the conversion of Cn fatty aldehydes to formate and the corresponding Cn-1 alk(a/e)nes. This apparently hydrolytic reaction is actually a cryptically redox oxygenation process, in which one O-atom is incorporated from O2 into formate and a protein-based reducing system (NADPH, ferredoxin, and ferredoxin reductase) provides all four electrons needed for the complete reduction of O2, absolute O2 requirement for formate production | Prochlorococcus marinus | ? | - |
? | |
4.1.99.5 | octadecanal + O2 + 2 NADH + 2 H+ | with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase | Prochlorococcus marinus | heptadecane + formate + H2O + 2 NAD+ | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.99.5 | cyanobacterial aldehyde decarbonylase | - |
Prochlorococcus marinus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.99.5 | 22 | - |
assay at | Prochlorococcus marinus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.1.99.5 | 7.5 | - |
assay at | Prochlorococcus marinus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
4.1.99.5 | additional information | the definitive reaffirmation of the oxygenative nature of the reaction implies that the enzyme, initially designated as aldehyde decarbonylase when the C1-derived coproduct is thought to be carbon monoxide rather than formate, should be redesignated as aldehyde-deformylating oxygenase, ADO | Prochlorococcus marinus |