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Literature summary for 4.1.99.5 extracted from

  • Hayashi, Y.; Yasugi, F.; Arai, M.
    Role of cysteine residues in the structure, stability, and alkane producing activity of cyanobacterial aldehyde deformylating oxygenase (2015), PLoS ONE, 10, e0122217 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS Nostoc punctiforme

Protein Variants

Protein Variants Comment Organism
C107A site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme Nostoc punctiforme
C107A/C117A site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme Nostoc punctiforme
C117A site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme Nostoc punctiforme
C71A site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme Nostoc punctiforme
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
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
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
C71S site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme Nostoc punctiforme

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics Nostoc punctiforme

Metals/Ions

Metals/Ions Comment Organism Structure
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

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+ Nostoc punctiforme
-
an alkane + formate + H2O + 2 NADP+
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ Nostoc punctiforme ATCC 29133 / PCC 73102
-
an alkane + formate + H2O + 2 NADP+
-
?

Organism

Organism UniProt Comment Textmining
Nostoc punctiforme B2J1M1
-
-
Nostoc punctiforme ATCC 29133 / PCC 73102 B2J1M1
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and dialysis Nostoc punctiforme

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
Nostoc punctiforme an alkane + formate + H2O + 2 NADP+
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
Nostoc punctiforme ATCC 29133 / PCC 73102 an alkane + formate + H2O + 2 NADP+
-
?
additional information GC-MS measurements and identification of products Nostoc punctiforme ?
-
?
additional information GC-MS measurements and identification of products Nostoc punctiforme ATCC 29133 / PCC 73102 ?
-
?
n-hexadecanal + O2 + 2 NADPH + 2 H+
-
Nostoc punctiforme pentadecane + formate + H2O + 2 NADP+
-
?
n-hexadecanal + O2 + 2 NADPH + 2 H+
-
Nostoc punctiforme ATCC 29133 / PCC 73102 pentadecane + formate + H2O + 2 NADP+
-
?
n-octadecanal + O2 + 2 NADPH + 2 H+
-
Nostoc punctiforme heptadecane + formate + H2O + 2 NADP+
-
?
n-octadecanal + O2 + 2 NADPH + 2 H+
-
Nostoc punctiforme ATCC 29133 / PCC 73102 heptadecane + formate + H2O + 2 NADP+
-
?
n-octadecenal + O2 + 2 NADPH + 2 H+
-
Nostoc punctiforme 1-heptadecene + formate + H2O + 2 NADP+
-
?
n-octadecenal + O2 + 2 NADPH + 2 H+
-
Nostoc punctiforme ATCC 29133 / PCC 73102 1-heptadecene + formate + H2O + 2 NADP+
-
?

Synonyms

Synonyms Comment Organism
aldehyde deformylating oxygenase
-
Nostoc punctiforme
Npun_R1711
-
Nostoc punctiforme

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
in vivo assay at Nostoc punctiforme

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
43
-
Tm of recombinant mutant C107A/C117A Nostoc punctiforme
46
-
Tm of recombinant mutant C71S Nostoc punctiforme
47
-
Tm of recombinant mutants C71A, C107A, C117A, and C71A/C117A Nostoc punctiforme
48
-
Tm of recombinant mutant C71A/C107A Nostoc punctiforme
53
-
Tm of recombinant wild-type Nostoc punctiforme

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Nostoc punctiforme

General Information

General Information Comment Organism
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
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
physiological function aldehyde deformylating oxygenase is a key enzyme for alkane biosynthesis in cyanobacteria Nostoc punctiforme