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Literature summary extracted from

  • Bao, L.; Li, J.J.; Jia, C.; Li, M.; Lu, X.
    Structure-oriented substrate specificity engineering of aldehyde-deformylating oxygenase towards aldehydes carbon chain length (2016), Biotechnol. Biofuels, 9, 185 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.99.5 gene Synpcc7942_1593, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha Synechococcus elongatus PCC 7942 = FACHB-805

Protein Variants

EC Number Protein Variants Comment Organism
4.1.99.5 A118F site-directed mutagenesis, the mutant shows increased activity with n-butanal compared to the wild-type enzyme. A118F does not show any obvious activity against C14,16,18 aldehydes, and only exhibits slight activity towards n-dodecanal and n-decanal for long-chain substrates Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 A121F site-directed mutagenesis, the mutant shows increased activity with C4,6,7 aldehydes compared to the wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 C70F site-directed mutagenesis, the mutant shows increased activity with n-hexanal compared to the wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 F87Y site-directed mutagenesis, the mutant shows increased activity with n-decanal compared to the wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 G31F site-directed mutagenesis Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 I24Y site-directed mutagenesis, the mutant shows increased activity with n-heptanal compared to the wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 I27F site-directed mutagenesis, the mutant shows increased activity with n-decanal and n-dodecanal compared to the wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 L198F site-directed mutagenesis, the mutant shows increased activity with C7-10 aldehydescompared to the wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 M193Y site-directed mutagenesis, the mutant shows increased activity with C6-10 aldehydes compared to the wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 additional information structure-guided protein engineering to alter substrate specificity of aldehyde-deformylating oxygenase towards aldehydes carbon chain length. The impact of the engineered cADO mutants on the change of the hydrocarbon profile is demonstrated by co-expressing acyl-ACP thioesterase BTE, fadD and V184F in Escherichia coli, showing that n-undecane is the main fatty alkane Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 V184F site-directed mutagenesis, the mutant shows increased activity with n-dodecanal and n-decanal compared to the wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 V28F site-directed mutagenesis, the mutant shows increased activity with n-dodecanal compared to the wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 Y21R site-directed mutagenesis Synechococcus elongatus PCC 7942 = FACHB-805

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.99.5 0.069
-
 n-nonanal pH 7.2, 37°C, recombinant wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.14
-
 n-nonanal pH 7.2, 37°C, recombinant mutant A121F Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.18
-
 n-octanal pH 7.2, 37°C, recombinant wild-type enzyme and mutant A121F Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.56
-
 n-Heptanal pH 7.2, 37°C, recombinant mutant A121F Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.59
-
 n-Heptanal pH 7.2, 37°C, recombinant wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.93
-
 n-hexanal pH 7.2, 37°C, recombinant wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.96
-
 n-hexanal pH 7.2, 37°C, recombinant mutant A121F Synechococcus elongatus PCC 7942 = FACHB-805

Natural Substrates/ Products (Substrates)

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+ Synechococcus elongatus PCC 7942 = FACHB-805
-
 an alkane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 a long-chain aldehyde + O2 + 2 NADPH + 2 H+ Synechococcus elongatus PCC 7942 = FACHB-805 R2
-
 an alkane + formate + H2O + 2 NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.5 Synechococcus elongatus PCC 7942 = FACHB-805 Q54764 i.e. Synechococcus elongates strain PCC 7942
-
4.1.99.5 Synechococcus elongatus PCC 7942 = FACHB-805 R2 Q54764 i.e. Synechococcus elongates strain PCC 7942
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.99.5 recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3) Synechococcus elongatus PCC 7942 = FACHB-805

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.5 a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
 Synechococcus elongatus PCC 7942 = FACHB-805 an alkane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
 Synechococcus elongatus PCC 7942 = FACHB-805 R2 an alkane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 additional information substrate specificity of recombinant wild-type and mutant enzymes, overview. The wild-type prefers long-chain substrates, but some mutants show also higher activity with short-chain substrates. Analysis of preferred substrates in the presence of the competition substrates for wild-type and mutants enzymes Synechococcus elongatus PCC 7942 = FACHB-805 ?
-
 ?
4.1.99.5 additional information substrate specificity of recombinant wild-type and mutant enzymes, overview. The wild-type prefers long-chain substrates, but some mutants show also higher activity with short-chain substrates. Analysis of preferred substrates in the presence of the competition substrates for wild-type and mutants enzymes Synechococcus elongatus PCC 7942 = FACHB-805 R2 ?
-
 ?
4.1.99.5 n-butanal + O2 + 2 NADPH + 2 H+
-
 Synechococcus elongatus PCC 7942 = FACHB-805 n-propane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 n-butanal + O2 + 2 NADPH + 2 H+
-
 Synechococcus elongatus PCC 7942 = FACHB-805 R2 n-propane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 n-decanal + O2 + 2 NADPH + 2 H+
-
 Synechococcus elongatus PCC 7942 = FACHB-805 n-nonane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 n-decanal + O2 + 2 NADPH + 2 H+
-
 Synechococcus elongatus PCC 7942 = FACHB-805 R2 n-nonane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 n-dodecanal + O2 + 2 NADPH + 2 H+ mutants show increased activity with n-dodecanal compared to wild-type: V184F 4.4fold, F87Y 2.5fold, I27F 2.1fold and V28Y 2.0fold. Yields of n-undecane of wild-type and some cADO mutants against n-dodecanal in the presence of the competition substrates, overview Synechococcus elongatus PCC 7942 = FACHB-805 undecane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 n-dodecanal + O2 + 2 NADPH + 2 H+ mutants show increased activity with n-dodecanal compared to wild-type: V184F 4.4fold, F87Y 2.5fold, I27F 2.1fold and V28Y 2.0fold. Yields of n-undecane of wild-type and some cADO mutants against n-dodecanal in the presence of the competition substrates, overview Synechococcus elongatus PCC 7942 = FACHB-805 R2 undecane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 n-heptanal + O2 + 2 NADPH + 2 H+
-
 Synechococcus elongatus PCC 7942 = FACHB-805 n-hexane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 n-hexanal + O2 + 2 NADPH + 2 H+ mutants A121F, C70F, M193Y, and L198F show 2.7, 2.5, 1.7 and 1.4fold increase in kcatapp against n-hexanal, respectively, compared to wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805 n-pentane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 n-nonanal + O2 + 2 NADPH + 2 H+ mutant M193Y and L198F exhibit a 1.7 and 2.0fold increase in kcat, respectively, compared to wild-type, while kcat value of I24Y is much lower than that of the wild-type, and those of C70F and A121F are about half of that of wild-type Synechococcus elongatus PCC 7942 = FACHB-805 n-octane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 n-octanal + O2 + 2 NADPH + 2 H+ mutant M193Y show 3.2fold improved activity, and mutants A121F and L198F exhibit comparable activity to wild-type, while mutants I24Y and C70F display much lower activity compared to wild-type Synechococcus elongatus PCC 7942 = FACHB-805 n-heptane + formate + H2O + 2 NADP+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.99.5 ADO
-
 Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 aldehyde-deformylating oxygenase
-
 Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 cADO
-
 Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 cADO-1593
-
 Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 cyanobacterial ADO
-
 Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 Synpcc7942_1593
-
 Synechococcus elongatus PCC 7942 = FACHB-805

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.99.5 37
-
 assay at Synechococcus elongatus PCC 7942 = FACHB-805

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.99.5 0.01
-
 n-nonanal pH 7.2, 37°C, recombinant wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.013
-
 n-nonanal pH 7.2, 37°C, recombinant mutant A121F Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.013
-
 n-Heptanal pH 7.2, 37°C, recombinant wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.016
-
 n-octanal pH 7.2, 37°C, recombinant mutant A121F Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.023
-
 n-octanal pH 7.2, 37°C, recombinant wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.025
-
 n-Heptanal pH 7.2, 37°C, recombinant mutant A121F Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.03
-
 n-hexanal pH 7.2, 37°C, recombinant wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.115
-
 n-hexanal pH 7.2, 37°C, recombinant mutant A121F Synechococcus elongatus PCC 7942 = FACHB-805

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.99.5 7.2
-
 assay at Synechococcus elongatus PCC 7942 = FACHB-805

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.5 NADPH
-
 Synechococcus elongatus PCC 7942 = FACHB-805

General Information

EC Number General Information Comment Organism
4.1.99.5 malfunction the substrate preferences of some enzyme mutants towards different chain-length substrates are enhanced, e.g. I24Y for n-heptanal, I27F for n-decanal and n-dodecanal, V28F for n-dodecanal, F87Y for n-decanal, C70F for n-hexanal, A118F for n-butanal, A121F for C4,6,7 aldehydes, V184F for n-dodecanal and n-decanal, M193Y for C6-10 aldehydes and L198F for C7-10 aldehydes Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 physiological function aldehyde-deformylating oxygenase (ADO) is an important enzyme involved in the biosynthetic pathway of fatty alk(a/e)nes in cyanobacteria Synechococcus elongatus PCC 7942 = FACHB-805

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.1.99.5 0.022
-
 n-Heptanal pH 7.2, 37°C, recombinant wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.032
-
 n-hexanal pH 7.2, 37°C, recombinant wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.045
-
 n-Heptanal pH 7.2, 37°C, recombinant mutant A121F Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.09
-
 n-octanal pH 7.2, 37°C, recombinant mutant A121F Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.09
-
 n-nonanal pH 7.2, 37°C, recombinant mutant A121F Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.12
-
 n-hexanal pH 7.2, 37°C, recombinant mutant A121F Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.13
-
 n-octanal pH 7.2, 37°C, recombinant wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.5 0.15
-
 n-nonanal pH 7.2, 37°C, recombinant wild-type enzyme Synechococcus elongatus PCC 7942 = FACHB-805