1.14.14.28: long-chain alkane monooxygenase
This is an abbreviated version!
For detailed information about long-chain alkane monooxygenase, go to the full flat file.
Reaction
Synonyms
LADA, LadAalphaB23, LadAbetaB23, LadBB23, LC-alkane monooxygenase
ECTree
1.14.14.28 long-chain alkane monooxygenaseAdvanced search results
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results (Engineering
Engineering on EC 1.14.14.28 - long-chain alkane monooxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
K361L
-
substitution in the IS4 region, resulting in improved binding energy. As the carbon chain increases the overall binding energy of alkane molecules from C30-C36 decreases as compared with C16. Mutated residue is not involved in binding sites but improves the accessibility of other residues towards the substrate
R359I
-
substitution in the IS4 region, resulting in improved binding energy. As the carbon chain increases the overall binding energy of alkane molecules from C30-C36 decreases as compared with C16. Mutated residue is not involved in binding sites but improves the accessibility of other residues towards the substrate
T369W
-
substitution in the IS4 region, resulting in improved binding energy. As the carbon chain increases the overall binding energy of alkane molecules from C30-C36 decreases as compared with C16. Mutated residue is not involved in binding sites but improves the accessibility of other residues towards the substrate
K361L
-
substitution in the IS4 region, resulting in improved binding energy. As the carbon chain increases the overall binding energy of alkane molecules from C30-C36 decreases as compared with C16. Mutated residue is not involved in binding sites but improves the accessibility of other residues towards the substrate
-
R359I
-
substitution in the IS4 region, resulting in improved binding energy. As the carbon chain increases the overall binding energy of alkane molecules from C30-C36 decreases as compared with C16. Mutated residue is not involved in binding sites but improves the accessibility of other residues towards the substrate
-
T369W
-
substitution in the IS4 region, resulting in improved binding energy. As the carbon chain increases the overall binding energy of alkane molecules from C30-C36 decreases as compared with C16. Mutated residue is not involved in binding sites but improves the accessibility of other residues towards the substrate
-
A102D
hydroxylation activity of purified LadA mutant on hexadecane is 2.1fold higher than that of the wild-type enzyme. Hexadecane degradation rate is 2.3fold higher than that of the wild-type enzyme. A Pseudomonas fluorescens KOB2DELTA1 strain expressing the LadA mutant grows more rapidly with hexadecane than the strain expressing wild-type LadA, confirming the enhanced activity of LadA mutant in vivo. Mutant enzyme with the same size as the wild-type LadA protein. Compared to the wild-type enzyme, the mutant enzyme utilizes a narrower spectrum of n-alkanes, including C16 to C28
A102D/F146C/L320V/N376I
mutant enzyme completely loses the catalytic activity
A102D/F146C/N376I
mutant enzyme completely loses the catalytic activity
A102D/L320V
mutant enzyme completely loses the catalytic activity
A102E
hydroxylation activity of purified LadA mutant on hexadecane is 2.2fold higher than that of the wild-type enzyme. Hexadecane degradation rate is 2.2fold higher than that of the wild-type enzyme. A Pseudomonas fluorescens KOB2DELTA1 strain expressing the LadA mutant grows more rapidly with hexadecane than the strain expressing wild-type LadA, confirming the enhanced activity of LadA mutant in vivo. Mutant enzyme with the same size as the wild-type LadA protein
C14A
point mutation completely abolishes the catalytic activity
F146C
mutant enzyme completely loses the catalytic activity
F146C/L320V/N376I
mutant enzyme completely loses the catalytic activity
F146C/N376I
hydroxylation activity of purified LadA mutant on hexadecane is 2.9fold higher than that of the wild-type enzyme. Hexadecane degradation rate is 2.9fold higher than that of the wild-type enzyme. A Pseudomonas fluorescens KOB2DELTA1 strain expressing the LadA mutant grows more rapidly with hexadecane than the strain expressing wild-type LadA, confirming the enhanced activity of LadA mutant in vivo. Mutant enzyme with the same size as the wild-type LadA protein
F146E/N376I
hydroxylation activity of purified LadA mutant on hexadecane is 2.0fold higher than that of the wild-type enzyme. Hexadecane degradation rate is 2.7fold higher than that of the wild-type enzyme. A Pseudomonas fluorescens KOB2DELTA1 strain expressing the LadA mutant grows more rapidly with hexadecane than the strain expressing wild-type LadA, confirming the enhanced activity of LadA mutant in vivo. Mutant enzyme with the same size as the wild-type LadA protein. Compared to the wild-type enzyme, the mutant enzyme utilizes a narrower spectrum of n-alkanes, including C15 to C28
F146N/N376I
hydroxylation activity of purified LadA mutant on hexadecane is 3.4fold higher than that of the wild-type enzyme. Hexadecane degradation rate is 3.4fold higher than that of the wild-type enzyme. A Pseudomonas fluorescens KOB2DELTA1 strain expressing the LadA mutant grows more rapidly with hexadecane than the strain expressing wild-type LadA, confirming the enhanced activity of LadA mutant in vivo. The mutant enzyme shows a shift in optimum temperature from 60°C (for the wild-type enzyme) to 75°C. Compared to the wild-type enzyme, the mutant enzyme utilizes a narrower spectrum of n-alkanes, including C15 to C28
F146Q/N376I
hydroxylation activity of purified LadA mutant on hexadecane is 2.3fold higher than that of the wild-type enzyme. Hexadecane degradation rate is 2.3fold higher than that of the wild-type enzyme. A Pseudomonas fluorescens KOB2DELTA1 strain expressing the LadA mutant grows more rapidly with hexadecane than the strain expressing wild-type LadA, confirming the enhanced activity of LadA mutant in vivo. Mutant enzyme with the same size as the wild-type LadA protein. Compared to the wild-type enzyme, the mutant enzyme utilizes a narrower spectrum of n-alkanes, including C14 to C24
F146R/N376I
hydroxylation activity of purified LadA mutant on hexadecane is 2.5fold higher than that of the wild-type enzyme. Hexadecane degradation rate is 2.8fold higher than that of the wild-type enzyme. A Pseudomonas fluorescens KOB2DELTA1 strain expressing the LadA mutant grows more rapidly with hexadecane than the strain expressing wild-type LadA, confirming the enhanced activity of LadA mutant in vivo. Mutant enzyme with the same size as the wild-type LadA protein. The mutant enzyme is more heat resistant than wild-type protein, with more than half of the initial activity being retained after incubation at 60°C for 12 h, compared to a 60°C incubation of 4 h or less resulting in the loss of half of the initial activity in the wild-type and F146N/N376I mutant. The mutant enzyme shows a shift in optimum temperature from 60°C (for the wild-type enzyme) to 65°C. Compared to the wild-type enzyme, the mutant enzyme utilizes a narrower spectrum of n-alkanes, including C15 to C24
H17F
the mutant maintains the same dimeric form as the wild type, point mutation completely abolishes the catalytic activity
H311F
the mutant maintains the same dimeric form as the wild type, point mutation completely abolishes the catalytic activity
L320A
hydroxylation activity of purified LadA mutant on hexadecane is 2.2fold higher than that of the wild-type enzyme. Hexadecane degradation rate is 2.5fold higher than that of the wild-type enzyme. A Pseudomonas fluorescens KOB2DELTA1 strain expressing the LadA mutant grows more rapidly with hexadecane than the strain expressing wild-type LadA, confirming the enhanced activity of LadA mutant in vivo. Mutant enzyme with the same size as the wild-type LadA protein. Compared to the wild-type enzyme, the mutant enzyme utilizes a narrower spectrum of n-alkanes, including C15 to C22
L320V
hydroxylation activity of purified LadA mutant on hexadecane is 2.5fold higher than that of the wild-type enzyme. Hexadecane degradation rate is 2.4fold higher than that of the wild-type enzyme. A Pseudomonas fluorescens KOB2DELTA1 strain expressing the LadA mutant grows more rapidly with hexadecane than the strain expressing wild-type LadA, confirming the enhanced activity of LadA mutant in vivo. Mutant enzyme with the same size as the wild-type LadA protein
N376I
mutant enzyme completely loses the catalytic activity
Q79L
the mutant maintains the same dimeric form as the wild type, point mutation completely abolishes the catalytic activity
T63F
the mutant maintains the same dimeric form as the wild type, point mutation completely abolishes the catalytic activity
A102D
-
hydroxylation activity of purified LadA mutant on hexadecane is 2.1fold higher than that of the wild-type enzyme. Hexadecane degradation rate is 2.3fold higher than that of the wild-type enzyme. A Pseudomonas fluorescens KOB2DELTA1 strain expressing the LadA mutant grows more rapidly with hexadecane than the strain expressing wild-type LadA, confirming the enhanced activity of LadA mutant in vivo. Mutant enzyme with the same size as the wild-type LadA protein. Compared to the wild-type enzyme, the mutant enzyme utilizes a narrower spectrum of n-alkanes, including C16 to C28
-
A102E
-
hydroxylation activity of purified LadA mutant on hexadecane is 2.2fold higher than that of the wild-type enzyme. Hexadecane degradation rate is 2.2fold higher than that of the wild-type enzyme. A Pseudomonas fluorescens KOB2DELTA1 strain expressing the LadA mutant grows more rapidly with hexadecane than the strain expressing wild-type LadA, confirming the enhanced activity of LadA mutant in vivo. Mutant enzyme with the same size as the wild-type LadA protein
-
C14A
-
point mutation completely abolishes the catalytic activity
-
F146C
-
mutant enzyme completely loses the catalytic activity
-
H17F
-
the mutant maintains the same dimeric form as the wild type, point mutation completely abolishes the catalytic activity
-
H311F
-
the mutant maintains the same dimeric form as the wild type, point mutation completely abolishes the catalytic activity
-
L320A
-
hydroxylation activity of purified LadA mutant on hexadecane is 2.2fold higher than that of the wild-type enzyme. Hexadecane degradation rate is 2.5fold higher than that of the wild-type enzyme. A Pseudomonas fluorescens KOB2DELTA1 strain expressing the LadA mutant grows more rapidly with hexadecane than the strain expressing wild-type LadA, confirming the enhanced activity of LadA mutant in vivo. Mutant enzyme with the same size as the wild-type LadA protein. Compared to the wild-type enzyme, the mutant enzyme utilizes a narrower spectrum of n-alkanes, including C15 to C22
-
L320V
-
hydroxylation activity of purified LadA mutant on hexadecane is 2.5fold higher than that of the wild-type enzyme. Hexadecane degradation rate is 2.4fold higher than that of the wild-type enzyme. A Pseudomonas fluorescens KOB2DELTA1 strain expressing the LadA mutant grows more rapidly with hexadecane than the strain expressing wild-type LadA, confirming the enhanced activity of LadA mutant in vivo. Mutant enzyme with the same size as the wild-type LadA protein
-
Q79L
-
the mutant maintains the same dimeric form as the wild type, point mutation completely abolishes the catalytic activity
-
T63F
-
the mutant maintains the same dimeric form as the wild type, point mutation completely abolishes the catalytic activity
-
