EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.99.5 | recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS | Nostoc punctiforme |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.1.99.5 | C107A | site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme | Nostoc punctiforme |
4.1.99.5 | C107A/C117A | site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme | Nostoc punctiforme |
4.1.99.5 | C117A | site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme | Nostoc punctiforme |
4.1.99.5 | C71A | site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme | Nostoc punctiforme |
4.1.99.5 | C71A/C107A | site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant | Nostoc punctiforme |
4.1.99.5 | C71A/C107A/C117A | site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant | Nostoc punctiforme |
4.1.99.5 | C71A/C117A | site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant | Nostoc punctiforme |
4.1.99.5 | C71S | site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme | Nostoc punctiforme |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.99.5 | additional information | - |
additional information | Michaelis-Menten kinetics | Nostoc punctiforme |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
4.1.99.5 | Fe2+ | di-iron center, the amount of hydrocarbons produced in recombinant Escherichia coli is decreased when the iron concentration in the M9 medium is decreased. The Cys-to-Ala/Ser mutations do not affect the iron binding to the enzyme | Nostoc punctiforme |
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+ | Nostoc punctiforme | - |
an alkane + formate + H2O + 2 NADP+ | - |
? | |
4.1.99.5 | a long-chain aldehyde + O2 + 2 NADPH + 2 H+ | Nostoc punctiforme ATCC 29133 / PCC 73102 | - |
an alkane + formate + H2O + 2 NADP+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.99.5 | Nostoc punctiforme | B2J1M1 | - |
- |
4.1.99.5 | Nostoc punctiforme ATCC 29133 / PCC 73102 | B2J1M1 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.99.5 | recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and dialysis | Nostoc punctiforme |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.99.5 | a long-chain aldehyde + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme | an alkane + formate + H2O + 2 NADP+ | - |
? | |
4.1.99.5 | a long-chain aldehyde + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme ATCC 29133 / PCC 73102 | an alkane + formate + H2O + 2 NADP+ | - |
? | |
4.1.99.5 | additional information | GC-MS measurements and identification of products | Nostoc punctiforme | ? | - |
? | |
4.1.99.5 | additional information | GC-MS measurements and identification of products | Nostoc punctiforme ATCC 29133 / PCC 73102 | ? | - |
? | |
4.1.99.5 | n-hexadecanal + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme | pentadecane + formate + H2O + 2 NADP+ | - |
? | |
4.1.99.5 | n-hexadecanal + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme ATCC 29133 / PCC 73102 | pentadecane + formate + H2O + 2 NADP+ | - |
? | |
4.1.99.5 | n-octadecanal + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme | heptadecane + formate + H2O + 2 NADP+ | - |
? | |
4.1.99.5 | n-octadecanal + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme ATCC 29133 / PCC 73102 | heptadecane + formate + H2O + 2 NADP+ | - |
? | |
4.1.99.5 | n-octadecenal + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme | 1-heptadecene + formate + H2O + 2 NADP+ | - |
? | |
4.1.99.5 | n-octadecenal + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme ATCC 29133 / PCC 73102 | 1-heptadecene + formate + H2O + 2 NADP+ | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.99.5 | aldehyde deformylating oxygenase | - |
Nostoc punctiforme |
4.1.99.5 | Npun_R1711 | - |
Nostoc punctiforme |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.99.5 | 37 | - |
in vivo assay at | Nostoc punctiforme |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.99.5 | 43 | - |
Tm of recombinant mutant C107A/C117A | Nostoc punctiforme |
4.1.99.5 | 46 | - |
Tm of recombinant mutant C71S | Nostoc punctiforme |
4.1.99.5 | 47 | - |
Tm of recombinant mutants C71A, C107A, C117A, and C71A/C117A | Nostoc punctiforme |
4.1.99.5 | 48 | - |
Tm of recombinant mutant C71A/C107A | Nostoc punctiforme |
4.1.99.5 | 53 | - |
Tm of recombinant wild-type | Nostoc punctiforme |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.1.99.5 | NADPH | - |
Nostoc punctiforme |
EC Number | General Information | Comment | Organism |
---|---|---|---|
4.1.99.5 | malfunction | C71A/S mutations reduce the hydrocarbon producing activity of AD and facilitate the formation of a dimer, while mutations at Cys107 and Cys117 do not affect the hydrocarbon producing activity of the enzyme. The Cys-to-Ala/Ser mutations do not affect the iron binding to the enzyme. Structural features of the Cys-deficient mutants, overview | Nostoc punctiforme |
4.1.99.5 | additional information | Cys71, which is located in close proximity to the substrate-binding site, plays a crucial role in maintaining the activity, structure, and stability of the enzyme | Nostoc punctiforme |
4.1.99.5 | physiological function | aldehyde deformylating oxygenase is a key enzyme for alkane biosynthesis in cyanobacteria | Nostoc punctiforme |