BRENDA - Enzyme Database show
show all sequences of 4.1.99.5

Structure-oriented substrate specificity engineering of aldehyde-deformylating oxygenase towards aldehydes carbon chain length

Bao, L.; Li, J.J.; Jia, C.; Li, M.; Lu, X.; Biotechnol. Biofuels 9, 185 (2016)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
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
Engineering
Amino acid exchange
Commentary
Organism
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
A121F
site-directed mutagenesis, the mutant shows increased activity with C4,6,7 aldehydes compared to the wild-type enzyme
Synechococcus elongatus PCC 7942
C70F
site-directed mutagenesis, the mutant shows increased activity with n-hexanal compared to the wild-type enzyme
Synechococcus elongatus PCC 7942
F87Y
site-directed mutagenesis, the mutant shows increased activity with n-decanal compared to the wild-type enzyme
Synechococcus elongatus PCC 7942
G31F
site-directed mutagenesis
Synechococcus elongatus PCC 7942
I24Y
site-directed mutagenesis, the mutant shows increased activity with n-heptanal compared to the wild-type enzyme
Synechococcus elongatus PCC 7942
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
L198F
site-directed mutagenesis, the mutant shows increased activity with C7-10 aldehydescompared to the wild-type enzyme
Synechococcus elongatus PCC 7942
M193Y
site-directed mutagenesis, the mutant shows increased activity with C6-10 aldehydes compared to the wild-type enzyme
Synechococcus elongatus PCC 7942
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
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
V28F
site-directed mutagenesis, the mutant shows increased activity with n-dodecanal compared to the wild-type enzyme
Synechococcus elongatus PCC 7942
Y21R
site-directed mutagenesis
Synechococcus elongatus PCC 7942
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.069
-
n-nonanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.14
-
n-nonanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
0.18
-
n-octanal
pH 7.2, 37C, recombinant wild-type enzyme and mutant A121F
Synechococcus elongatus PCC 7942
0.56
-
n-Heptanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
0.59
-
n-Heptanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.93
-
n-hexanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.96
-
n-hexanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
Synechococcus elongatus PCC 7942
-
an alkane + formate + H2O + 2 NADP+
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
Synechococcus elongatus PCC 7942 R2
-
an alkane + formate + H2O + 2 NADP+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Synechococcus elongatus PCC 7942
Q54764
i.e. Synechococcus elongates strain PCC 7942
-
Synechococcus elongatus PCC 7942 R2
Q54764
i.e. Synechococcus elongates strain PCC 7942
-
Purification (Commentary)
Commentary
Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
Synechococcus elongatus PCC 7942
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
747351
Synechococcus elongatus PCC 7942
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
747351
Synechococcus elongatus PCC 7942 R2
an alkane + formate + H2O + 2 NADP+
-
-
-
?
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
747351
Synechococcus elongatus PCC 7942
?
-
-
-
-
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
747351
Synechococcus elongatus PCC 7942 R2
?
-
-
-
-
n-butanal + O2 + 2 NADPH + 2 H+
-
747351
Synechococcus elongatus PCC 7942
n-propane + formate + H2O + 2 NADP+
-
-
-
?
n-butanal + O2 + 2 NADPH + 2 H+
-
747351
Synechococcus elongatus PCC 7942 R2
n-propane + formate + H2O + 2 NADP+
-
-
-
?
n-decanal + O2 + 2 NADPH + 2 H+
-
747351
Synechococcus elongatus PCC 7942
n-nonane + formate + H2O + 2 NADP+
-
-
-
?
n-decanal + O2 + 2 NADPH + 2 H+
-
747351
Synechococcus elongatus PCC 7942 R2
n-nonane + formate + H2O + 2 NADP+
-
-
-
?
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
747351
Synechococcus elongatus PCC 7942
n-undecane + formate + H2O + 2 NADP+
-
-
-
?
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
747351
Synechococcus elongatus PCC 7942 R2
n-undecane + formate + H2O + 2 NADP+
-
-
-
?
n-heptanal + O2 + 2 NADPH + 2 H+
-
747351
Synechococcus elongatus PCC 7942
n-hexane + formate + H2O + 2 NADP+
-
-
-
?
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
747351
Synechococcus elongatus PCC 7942
n-pentane + formate + H2O + 2 NADP+
-
-
-
?
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
747351
Synechococcus elongatus PCC 7942
n-octane + formate + H2O + 2 NADP+
-
-
-
?
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
747351
Synechococcus elongatus PCC 7942
n-heptane + formate + H2O + 2 NADP+
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Synechococcus elongatus PCC 7942
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.01
-
n-nonanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.013
-
n-Heptanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.013
-
n-nonanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
0.016
-
n-octanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
0.023
-
n-octanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.025
-
n-Heptanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
0.03
-
n-hexanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.115
-
n-hexanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Synechococcus elongatus PCC 7942
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
-
Synechococcus elongatus PCC 7942
Cloned(Commentary) (protein specific)
Commentary
Organism
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
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
-
Synechococcus elongatus PCC 7942
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
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
A121F
site-directed mutagenesis, the mutant shows increased activity with C4,6,7 aldehydes compared to the wild-type enzyme
Synechococcus elongatus PCC 7942
C70F
site-directed mutagenesis, the mutant shows increased activity with n-hexanal compared to the wild-type enzyme
Synechococcus elongatus PCC 7942
F87Y
site-directed mutagenesis, the mutant shows increased activity with n-decanal compared to the wild-type enzyme
Synechococcus elongatus PCC 7942
G31F
site-directed mutagenesis
Synechococcus elongatus PCC 7942
I24Y
site-directed mutagenesis, the mutant shows increased activity with n-heptanal compared to the wild-type enzyme
Synechococcus elongatus PCC 7942
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
L198F
site-directed mutagenesis, the mutant shows increased activity with C7-10 aldehydescompared to the wild-type enzyme
Synechococcus elongatus PCC 7942
M193Y
site-directed mutagenesis, the mutant shows increased activity with C6-10 aldehydes compared to the wild-type enzyme
Synechococcus elongatus PCC 7942
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
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
V28F
site-directed mutagenesis, the mutant shows increased activity with n-dodecanal compared to the wild-type enzyme
Synechococcus elongatus PCC 7942
Y21R
site-directed mutagenesis
Synechococcus elongatus PCC 7942
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.069
-
n-nonanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.14
-
n-nonanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
0.18
-
n-octanal
pH 7.2, 37C, recombinant wild-type enzyme and mutant A121F
Synechococcus elongatus PCC 7942
0.56
-
n-Heptanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
0.59
-
n-Heptanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.93
-
n-hexanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.96
-
n-hexanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
Synechococcus elongatus PCC 7942
-
an alkane + formate + H2O + 2 NADP+
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
Synechococcus elongatus PCC 7942 R2
-
an alkane + formate + H2O + 2 NADP+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
Synechococcus elongatus PCC 7942
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
747351
Synechococcus elongatus PCC 7942
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
747351
Synechococcus elongatus PCC 7942 R2
an alkane + formate + H2O + 2 NADP+
-
-
-
?
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
747351
Synechococcus elongatus PCC 7942
?
-
-
-
-
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
747351
Synechococcus elongatus PCC 7942 R2
?
-
-
-
-
n-butanal + O2 + 2 NADPH + 2 H+
-
747351
Synechococcus elongatus PCC 7942
n-propane + formate + H2O + 2 NADP+
-
-
-
?
n-butanal + O2 + 2 NADPH + 2 H+
-
747351
Synechococcus elongatus PCC 7942 R2
n-propane + formate + H2O + 2 NADP+
-
-
-
?
n-decanal + O2 + 2 NADPH + 2 H+
-
747351
Synechococcus elongatus PCC 7942
n-nonane + formate + H2O + 2 NADP+
-
-
-
?
n-decanal + O2 + 2 NADPH + 2 H+
-
747351
Synechococcus elongatus PCC 7942 R2
n-nonane + formate + H2O + 2 NADP+
-
-
-
?
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
747351
Synechococcus elongatus PCC 7942
n-undecane + formate + H2O + 2 NADP+
-
-
-
?
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
747351
Synechococcus elongatus PCC 7942 R2
n-undecane + formate + H2O + 2 NADP+
-
-
-
?
n-heptanal + O2 + 2 NADPH + 2 H+
-
747351
Synechococcus elongatus PCC 7942
n-hexane + formate + H2O + 2 NADP+
-
-
-
?
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
747351
Synechococcus elongatus PCC 7942
n-pentane + formate + H2O + 2 NADP+
-
-
-
?
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
747351
Synechococcus elongatus PCC 7942
n-octane + formate + H2O + 2 NADP+
-
-
-
?
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
747351
Synechococcus elongatus PCC 7942
n-heptane + formate + H2O + 2 NADP+
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Synechococcus elongatus PCC 7942
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.01
-
n-nonanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.013
-
n-Heptanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.013
-
n-nonanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
0.016
-
n-octanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
0.023
-
n-octanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.025
-
n-Heptanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
0.03
-
n-hexanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.115
-
n-hexanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Synechococcus elongatus PCC 7942
General Information
General Information
Commentary
Organism
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
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
General Information (protein specific)
General Information
Commentary
Organism
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
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
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.022
-
n-Heptanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.032
-
n-hexanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.045
-
n-Heptanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
0.09
-
n-nonanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
0.09
-
n-octanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
0.12
-
n-hexanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
0.13
-
n-octanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.15
-
n-nonanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.022
-
n-Heptanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.032
-
n-hexanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.045
-
n-Heptanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
0.09
-
n-nonanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
0.09
-
n-octanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
0.12
-
n-hexanal
pH 7.2, 37C, recombinant mutant A121F
Synechococcus elongatus PCC 7942
0.13
-
n-octanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
0.15
-
n-nonanal
pH 7.2, 37C, recombinant wild-type enzyme
Synechococcus elongatus PCC 7942
Other publictions for EC 4.1.99.5
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
747409
Wang
Identification of residues im ...
Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC 7942 R2, Synechocystis sp. PCC 6803
BMC Biotechnol.
17
31-39
2017
-
-
-
-
21
-
-
8
-
2
-
3
-
9
-
-
-
-
-
-
-
-
11
1
-
-
-
28
-
-
-
1
-
-
-
-
-
-
1
-
21
-
-
-
-
8
-
2
-
3
-
-
-
-
-
-
-
-
11
1
-
-
-
28
-
-
-
-
-
2
2
-
9
9
748564
Patrikainen
Comparison of orthologous cya ...
Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102, Prochlorococcus marinus, Prochlorococcus marinus MIT 9313, Synechococcus sp. RS9917, Synechocystis sp. PCC 6803
Metab. Eng. Commun.
5
9-18
2017
-
-
4
-
5
-
-
-
-
-
-
6
-
13
-
-
-
-
-
-
-
-
30
-
-
-
-
-
-
-
-
4
-
-
-
-
-
4
4
-
5
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
30
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
746976
Park
Crystal structures of aldehyd ...
Limnothrix redekei, Limnothrix redekei KNUA012, Oscillatoria sp. KNUA011
Biochem. Biophys. Res. Commun.
477
395-400
2016
-
2
2
2
-
-
-
-
-
-
-
3
-
5
-
-
-
-
-
-
-
-
6
2
2
-
-
-
2
-
-
2
-
-
-
-
2
2
2
2
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
6
2
2
-
-
-
2
-
-
-
-
4
4
-
-
-
747351
Bao
Structure-oriented substrate ...
Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC 7942 R2
Biotechnol. Biofuels
9
185
2016
-
-
1
-
13
-
-
7
-
-
-
2
-
6
-
-
1
-
-
-
-
-
14
-
1
-
-
8
1
-
-
1
-
-
-
-
-
1
1
-
13
-
-
-
-
7
-
-
-
2
-
-
-
1
-
-
-
-
14
-
1
-
-
8
1
-
-
-
-
2
2
-
8
8
747353
Zhang
Microbial synthesis of propan ...
Prochlorococcus marinus, Prochlorococcus marinus MIT 9313
Biotechnol. Biofuels
9
80
2016
-
-
1
-
3
-
-
-
-
-
-
2
-
7
-
-
-
-
-
-
-
-
4
-
1
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
747081
Warui
Efficient delivery of long-ch ...
Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102
Biochemistry
54
1006-1015
2015
-
-
-
-
-
-
-
-
-
-
-
2
-
9
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
748027
Rajakovich
Rapid reduction of the diferr ...
Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102
J. Am. Chem. Soc.
137
11695-11709
2015
-
-
-
-
-
-
-
-
-
1
-
2
-
8
-
-
-
1
-
-
-
-
10
-
1
-
-
-
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
10
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
748032
Shokri
Conversion of aldehyde to alk ...
Prochlorococcus marinus, Prochlorococcus marinus MIT 9313
J. Am. Chem. Soc.
137
7686-7691
2015
-
1
-
-
-
-
-
-
-
1
-
2
-
6
-
-
-
1
-
-
-
-
8
1
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
8
1
-
-
-
-
-
-
-
-
-
2
2
-
-
-
749051
Hayashi
Role of cysteine residues in ...
Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102
PLoS ONE
10
e0122217
2015
-
-
1
-
8
-
-
1
-
1
-
2
-
7
-
-
1
-
-
-
-
-
10
-
1
-
5
-
-
-
-
1
-
-
-
-
-
1
1
-
8
-
-
-
-
1
-
1
-
2
-
-
-
1
-
-
-
-
10
-
1
-
5
-
-
-
-
-
-
3
3
-
-
-
749212
Jia
Structural insights into the ...
Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC 7942 R2
Protein Cell
6
55-67
2015
-
-
1
1
3
-
-
-
-
1
-
2
-
6
-
-
1
1
-
-
-
-
6
1
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
1
3
-
-
-
-
-
-
1
-
2
-
-
-
1
-
-
-
-
6
1
1
-
-
-
1
-
-
-
-
4
4
-
-
-
726552
Das
Mechanistic insights from reac ...
Nostoc punctiforme
ACS Chem. Biol.
9
570-577
2014
-
-
1
-
-
-
1
-
-
1
-
1
-
2
-
-
1
1
-
-
-
-
6
-
1
-
-
3
1
-
-
2
-
-
-
-
-
1
2
-
-
-
-
1
-
-
-
1
-
1
-
-
-
1
-
-
-
-
6
-
1
-
-
3
1
-
-
-
-
1
1
-
-
-
746597
Buer
Insights into substrate and m ...
Prochlorococcus marinus, Prochlorococcus marinus MIT 9313
ACS Chem. Biol.
9
2584-2593
2014
-
-
-
1
1
-
1
-
-
1
-
2
-
6
-
-
-
1
-
-
-
-
8
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
1
1
1
-
-
1
-
-
-
1
-
2
-
-
-
-
-
-
-
-
8
-
-
-
-
1
-
-
-
-
-
2
2
-
-
-
747074
Waugh
Solvent isotope effects on al ...
Prochlorococcus marinus, Prochlorococcus marinus MIT9313
Biochemistry
53
5537-5543
2014
-
-
1
-
-
-
-
1
-
1
-
2
1
3
-
-
1
1
-
-
-
-
6
-
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
1
-
2
1
-
-
1
-
-
-
-
6
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
726548
Aukema
Cyanobacterial aldehyde deform ...
Prochlorococcus marinus, Prochlorococcus marinus MIT 9313
ACS Catal.
3
2228-2238
2013
-
-
1
-
-
-
-
-
-
-
-
-
-
6
-
-
1
-
-
-
-
-
8
-
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
8
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
727215
Zhang
Conversion of fatty aldehydes ...
Synechococcus elongatus
Biotechnol. Biofuels
6
86
2013
-
-
1
-
-
-
-
1
-
-
1
1
-
3
-
-
1
-
-
-
-
-
5
1
1
-
-
1
1
-
-
3
-
-
-
-
-
1
3
-
-
-
-
-
-
1
-
-
1
1
-
-
-
1
-
-
-
-
5
1
1
-
-
1
1
-
-
-
-
-
-
-
-
-
727312
Khara
Production of propane and othe ...
Prochlorococcus marinus, Prochlorococcus marinus MIT9313
ChemBioChem
14
1204-1208
2013
-
-
1
-
4
-
-
-
-
1
-
2
-
3
-
-
1
1
-
-
-
-
8
-
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
4
-
-
-
-
-
-
1
-
2
-
-
-
1
-
-
-
-
8
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
727690
Pandelia
Substrate-triggered addition o ...
Nostoc punctiforme
J. Am. Chem. Soc.
135
15801-15812
2013
1
-
1
-
-
-
-
1
-
1
-
1
-
2
-
-
1
1
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
1
-
1
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
1
1
-
-
-
727693
Paul
Probing the mechanism of cyano ...
Nostoc punctiforme
J. Am. Chem. Soc.
135
5234-5237
2013
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
727001
Li
Evidence for only oxygenative ...
Prochlorococcus marinus
Biochemistry
51
7908-7916
2012
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
715293
Warui
Detection of formate, rather t ...
Nostoc punctiforme
J. Am. Chem. Soc.
133
3316-3319
2011
-
-
1
-
-
-
-
-
-
1
-
2
-
4
-
-
1
1
-
-
-
-
4
-
1
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1
-
2
-
-
-
1
-
-
-
-
4
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
715300
Li
Conversion of fatty aldehydes ...
Nostoc punctiforme
J. Am. Chem. Soc.
133
6158-6161
2011
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
726957
Eser
Oxygen-independent alkane form ...
Nostoc punctiforme, Prochlorococcus marinus, Prochlorococcus marinus MIT9313, Synechococcus sp., Synechocystis sp.
Biochemistry
50
10743-10750
2011
-
-
4
-
-
-
4
-
-
-
-
-
-
8
-
-
-
4
-
-
-
-
15
-
4
-
-
-
4
-
-
4
-
-
-
-
-
4
4
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
15
-
4
-
-
-
4
-
-
-
-
4
4
-
-
-
713511
Schirmer
Microbial biosynthesis of alka ...
Nostoc punctiforme
Science
329
559-562
2010
-
-
1
-
-
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
648395
Schneider-Belhaddad
Solubilization, partial purifi ...
Pisum sativum
Arch. Biochem. Biophys.
377
341-349
2000
4
-
-
-
-
-
7
-
2
1
1
1
-
4
1
-
1
-
-
1
1
-
2
1
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
7
-
-
2
1
1
1
-
1
-
1
-
1
1
-
2
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
648396
Kobayashi
Cobalt proteins ...
Botryococcus braunii
Eur. J. Biochem.
261
1-9
1999
-
-
-
-
-
-
-
-
-
1
2
1
-
1
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
2
1
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
648394
Dennis
A cobalt-porphyrin enzyme conv ...
Botryococcus braunii, Botryococcus braunii Austin
Proc. Natl. Acad. Sci. USA
89
5306-5310
1992
-
-
-
-
-
-
1
-
1
1
2
2
-
5
-
-
1
-
-
-
1
-
4
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
1
2
2
-
-
-
1
-
-
1
-
4
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
648393
Dennis
Alkane biosynthesis by decarbo ...
Botryococcus braunii, Botryococcus braunii Austin
Arch. Biochem. Biophys.
287
268-275
1991
1
-
-
-
-
-
5
1
2
1
-
2
-
6
1
-
-
-
-
-
-
-
4
-
1
-
1
-
1
1
-
1
-
-
-
1
-
-
1
-
-
-
-
5
-
1
2
1
-
2
-
1
-
-
-
-
-
-
4
-
1
-
1
-
1
1
-
-
-
-
-
-
-
-
648392
Cheesbrough
Microsomal preparation from an ...
Podiceps nigricollis
J. Biol. Chem.
263
2738-2743
1988
2
-
-
-
-
-
9
1
2
1
-
1
-
3
1
-
-
-
-
1
-
-
2
-
1
-
1
-
1
1
-
1
-
-
-
2
-
-
1
-
-
-
-
9
-
1
2
1
-
1
-
1
-
-
-
1
-
-
2
-
1
-
1
-
1
1
-
-
-
-
-
-
-
-
648391
Cheesbrough
Alkane biosynthesis by decarbo ...
Pisum sativum
Proc. Natl. Acad. Sci. USA
81
6613-6617
1984
-
-
-
-
-
2
4
1
1
1
-
1
-
3
-
-
-
-
-
2
-
-
2
-
1
-
1
-
1
1
-
1
-
-
-
-
-
-
1
-
-
2
-
4
-
1
1
1
-
1
-
-
-
-
-
2
-
-
2
-
1
-
1
-
1
1
-
-
-
-
-
-
-
-