Information on EC 1.14.14.28 - long-chain alkane monooxygenase

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The expected taxonomic range for this enzyme is: Geobacillus thermodenitrificans

EC NUMBER
COMMENTARY hide
1.14.14.28
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RECOMMENDED NAME
GeneOntology No.
long-chain alkane monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a long-chain alkane + FMNH2 + O2 = a long-chain primary alcohol + FMN + H2O
show the reaction diagram
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
a long-chain alkane + FMNH2 + O2
a long-chain primary alcohol + FMN + H2O
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
a long-chain alkane + FMNH2 + O2
a long-chain primary alcohol + FMN + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C14A
point mutation completely abolishes 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
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
C14A
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point mutation completely abolishes the catalytic activity
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H17F
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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
-
Q79L
-
the mutant maintains the same dimeric form as the wild type, point mutation completely abolishes the catalytic activity
-
T63F
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the mutant maintains the same dimeric form as the wild type, point mutation completely abolishes the catalytic activity
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