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Information on EC 1.14.14.28 - long-chain alkane monooxygenase
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1.14.14.28 long-chain alkane monooxygenaseIUBMB Comments
The enzyme, characterized from the bacterium Geobacillus thermodenitrificans NG80-2, is capable of converting alkanes ranging from C15 to C36 into their corresponding primary alcohols [1,2]. The FMNH2 cofactor is provided by an FMN reductase .
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
long-chain alkane monooxygenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LADA
LadAalphaB23
LadAbetaB23
LadBB23
LC-alkane monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a long-chain alkane + FMNH2 + O2 = a long-chain primary alcohol + FMN + H2O
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
long-chain-alkane,FMNH2:oxygen oxidoreductase
The enzyme, characterized from the bacterium Geobacillus thermodenitrificans NG80-2, is capable of converting alkanes ranging from C15 to C36 into their corresponding primary alcohols [1,2]. The FMNH2 cofactor is provided by an FMN reductase [3].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
octacosan + FMNH2 + O2
1-octacosanol + FMN + H2O
-
-
?
octadecane + FMNH2 + O2
1-octadecanol + FMN + H2O
-
-
?
pentadecane + FMNH2 + O2
1-pentadecanol + FMN + H2O
-
-
?
tetracosan + FMNH2 + O2
1-tetracosanol + FMN + H2O
-
-
?
a long-chain alkane + FMNH2 + O2
a long-chain primary alcohol + FMN + H2O
-
-
-
?
a long-chain alkane + FMNH2 + O2
a long-chain primary alcohol + FMN + H2O
-
-
?
a long-chain alkane + FMNH2 + O2
a long-chain primary alcohol + FMN + H2O
the enzyme is capable of converting alkanes ranging from C15 to C36 into their corresponding primary alcohols
-
?
a long-chain alkane + FMNH2 + O2
a long-chain primary alcohol + FMN + H2O
-
-
-
?
a long-chain alkane + FMNH2 + O2
a long-chain primary alcohol + FMN + H2O
-
-
?
a long-chain alkane + FMNH2 + O2
a long-chain primary alcohol + FMN + H2O
the enzyme is capable of converting alkanes ranging from C15 to C36 into their corresponding primary alcohols
-
?
docosan + FMNH2 + O2
1-docosanol + FMN + H2O
-
-
?
dotriacontan + FMNH2 + O2
1-dotriacontanol + FMN + H2O
-
-
?
dotriacontan + FMNH2 + O2
1-dotriacontanol + FMN + H2O
-
-
?
hexacosan + FMNH2 + O2
1-hexacosanol + FMN + H2O
-
-
?
hexacosan + FMNH2 + O2
1-hexacosanol + FMN + H2O
-
-
?
hexadecane + FMNH2 + O2
1-hexadecanol + FMN + H2O
-
-
?
hexadecane + FMNH2 + O2
1-hexadecanol + FMN + H2O
-
-
?
hexatriacontan + FMNH2 + O2
1-hexatriacontanol + FMN + H2O
-
-
?
hexatriacontan + FMNH2 + O2
1-hexatriacontanol + FMN + H2O
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a long-chain alkane + FMNH2 + O2
a long-chain primary alcohol + FMN + H2O
-
-
-
-
?
a long-chain alkane + FMNH2 + O2
a long-chain primary alcohol + FMN + H2O
-
-
-
?
a long-chain alkane + FMNH2 + O2
a long-chain primary alcohol + FMN + H2O
-
-
-
-
?
a long-chain alkane + FMNH2 + O2
a long-chain primary alcohol + FMN + H2O
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
hexadecane
pH 7.5, 60°C, mutant enzyme F146E/N376I
2.7
hexadecane
pH 7.5, 60°C, mutant enzyme F146Q/N376I
2.8
hexadecane
pH 7.5, 60°C, mutant enzyme F146C/N376I
8.9
hexadecane
pH 7.5, 60°C, mutant enzyme F146N/N376I
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.043
hexadecane
pH 7.5, 60°C, mutant enzyme F146E/N376I
0.05
hexadecane
pH 7.5, 60°C, mutant enzyme F146Q/N376I
0.055
hexadecane
pH 7.5, 60°C, mutant enzyme F146R/N376I
0.063
hexadecane
pH 7.5, 60°C, mutant enzyme F146C/N376I
0.073
hexadecane
pH 7.5, 60°C, mutant enzyme F146N/N376I
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0082
hexadecane
pH 7.5, 60°C, mutant enzyme F146N/N376I
0.0185
hexadecane
pH 7.5, 60°C, mutant enzyme F146Q/N376I
0.022
hexadecane
pH 7.5, 60°C, mutant enzyme F146C/N376I
0.0295
hexadecane
pH 7.5, 60°C, mutant enzyme F146R/N376I
0.031
hexadecane
pH 7.5, 60°C, mutant enzyme F146E/N376I
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.8
both the wild-type and the mutants are active at pH values from 6.0 to 8.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 90
both the wild-type and the mutants are active at temperatures ranging from 40°C to 90°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
the enzyme initiates the terminal oxidation pathway for degradation of long-chain alkanes
metabolism
-
the enzyme initiates the terminal oxidation pathway for degradation of long-chain alkanes
physiological function
-
isoforms LadAalphaB23, LadAbetaB23 and LadBB23 are functional upon expression in a Pseudomonas fluorescens AlkB1 deletion strain and partially restore alkane degradation activity. Enzymes degrade C12-C23 alkanes
physiological function
-
isoforms LadAalphaB23, LadAbetaB23 and LadBB23 are functional upon expression in a Pseudomonas fluorescens AlkB1 deletion strain and partially restore alkane degradation activity. Enzymes degrade C12-C23 alkanes
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A4IU28_GEOTN
Geobacillus thermodenitrificans (strain NG80-2)
440
0
50466
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of the structure based on PDB entry 3B9N and molecular dynamics simulations
-
crystals of LadA and the LadA:FMN complex are grown using the hanging-drop vapor-diffusion method at 18°C, crystal structure of the enzyme in the apoenzyme form and its complex with FMNH2
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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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
incubation of 4 h or less results in the loss of half of the initial activity in the wild-type and F146N/N376I mutant. Mutant enzyme F146R/N376I retains more than half of the initial activity after incubation for 12 h
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
environmental protection
synthesis
environmental protection
the thermophilic soluble monomeric LadA is an ideal candidate for treatment of environmental oil pollutions
environmental protection
-
the thermophilic soluble monomeric LadA is an ideal candidate for treatment of environmental oil pollutions
synthesis
the thermophilic soluble monomeric LadA is an ideal candidate for and biosynthesis of complex molecules
synthesis
-
the thermophilic soluble monomeric LadA is an ideal candidate for and biosynthesis of complex molecules
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, L.; Liu, X.; Yang, W.; Xu, F.; Wang, W.; Feng, L.; Bartlam, M.; Wang, L.; Rao, Z.
Crystal structure of long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN: unveiling the long-chain alkane hydroxylase
J. Mol. Biol.
376
453-465
2008
Geobacillus thermodenitrificans (A4IU28), Geobacillus thermodenitrificans NG80-2 (A4IU28), Geobacillus thermodenitrificans NG80-2
brenda
Dong, Y.; Yan, J.; Du, H.; Chen, M.; Ma, T.; Feng, L.
Engineering of LadA for enhanced hexadecane oxidation using random- and site-directed mutagenesis
Appl. Microbiol. Biotechnol.
94
1019-1029
2012
Geobacillus thermodenitrificans (A4IU28), Geobacillus thermodenitrificans NG80-2 (A4IU28)
brenda
Wang, W.; Shao, Z.
Diversity of flavin-binding monooxygenase genes (almA) in marine bacteria capable of degradation long-chain alkanes
FEMS Microbiol. Ecol.
80
523-533
2012
Geobacillus thermodenitrificans, Geobacillus thermodenitrificans NG80-2
brenda
Feng, L.; Wang, W.; Cheng, J.; Ren, Y.; Zhao, G.; Gao, C.; Tang, Y.; Liu, X.; Han, W.; Peng, X.; Liu, R.; Wang, L.
Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir
Proc. Natl. Acad. Sci. USA
104
5602-5607
2007
Geobacillus thermodenitrificans (A4IU28), Geobacillus thermodenitrificans NG80-2 (A4IU28), Geobacillus thermodenitrificans NG80-2
brenda
Boonmak, C.; Takahashi, Y.; Morikawa, M.
Cloning and expression of three ladA-type alkane monooxygenase genes from an extremely thermophilic alkane-degrading bacterium Geobacillus thermoleovorans B23
Extremophiles
18
515-523
2014
Geobacillus thermoleovorans, Geobacillus thermoleovorans B23
brenda
Jain, C.; Gupta, M.; Prasad, Y.; Wadhwa, G.; Sharma, S.
Homology modeling and protein engineering of alkane monooxygenase in Burkholderia thailandensis MSMB121 In silico insights
J. Mol. Model.
20
2340
2014
Burkholderia thailandensis, Burkholderia thailandensis MSMB121
brenda
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