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Information on EC 1.14.15.3 - alkane 1-monooxygenase
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EC Tree
1.14.15.3 alkane 1-monooxygenaseIUBMB Comments
Some enzymes in this group are heme-thiolate proteins (P-450). Also hydroxylates fatty acids in the omega-position.
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Word Map
- 1.14.15.3
-
arachidonic
- peroxisome
- 20-hete
-
20-hydroxyeicosatetraenoic
- methanotrophs
- n-alkanes
-
omega-hydroxylation
- clofibrate
- hydroxylases
- methylosinus
- trichosporium
-
epoxyeicosatrienoic
-
eicosanoids
- pparalpha
- epoxygenase
-
25-hydroxyvitamin
- methylococcus
-
petroleum
- cyp4f2
- proliferators
- cyp3a11
- laurate
-
methane-oxidizing
-
androstane
-
24-hydroxylase
-
17-octadecynoic
-
omega-oxidation
- cyp2c8
-
cyp2b10
-
hydrocarbon-degrading
-
oleovorans
- ch4
-
diferrous
- methylomonas
- n-hexadecane
- rubredoxins
-
cometabolic
- 1-aminobenzotriazole
-
biosurfactant
-
oil-contaminated
- gordonia
- omega-1
- methylocystis
- chlorzoxazone
- suberin
-
dihydroxyeicosatrienoic
-
alkanols
-
di-iron
-
antiferromagnetically
-
high-valent
- drug development
- degradation
- analysis
- synthesis
- environmental protection
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
reduced rubredoxin
+
+
2
=
+
oxidized rubredoxin
+
Synonyms
cyp4a, cyp4a11, methane monooxygenase, alkane hydroxylase, 1-hydroxylase, omega-hydroxylase, cyp4a10, cyp4a14, cyp153, alkane monooxygenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alkane hydroxylase
alkane mono-oxygenase
alkane monooxygenase
alkane-1-monooxygenase 1
alkane-1-monooxygenase 2
AlkB
AlkB1
AlkB2
AlkW1
AlmA
AlmA-like alkane hydroxylase
BMO
CYP153 homologue
CYP153A
CYP4 P450
CYP4A
cytochrome P-450 omega-hydroxylase
cytochrome P450 alkane hydroxylase
cytochrome P450 omega hydroxylase
diiron omega-hydroxylase
Fatty acid omega-hydroxylase
Gpo1
hexane hydroxylase
medium-chain alkane hydroxylase
methane monooxygenase
omega hydroxylase
Prm1ABCD
-
additional information
additional information
-
part of the alkane hydroxylase system containing of the membrane bound alkane 1-monooxygenase, and the soluble rubredoxin and rubredoxin reductase
additional information
-
part of the alkane hydroxylase system containing of the membrane bound alkane 1-monooxygenase, and the soluble rubredoxin and rubredoxin reductase
additional information
-
two genetic homologs, alkB1 and alkB2, genes are expressed at different growth phases, alkB2 expressed in early exponential phase, alkB1 expressed in late exponential phase
additional information
-
part of the alkane hydroxylase system containing of the membrane bound alkane 1-monooxygenase, and the soluble rubredoxin and rubredoxin reductase
additional information
Pseudomonas putida GPo1 / ATCC29347
-
part of the alkane hydroxylase system containing of the membrane bound alkane 1-monooxygenase, and the soluble rubredoxin and rubredoxin reductase
additional information
three component alkane hydroxylase complex consisting of a particulate nonheme integral membrane alkane monooxygenase (AlkB), soluble rubredoxin (AlkG), and soluble rubredoxin reductase (AlkT), at least four alkane monooxygenase gene homologs alkB1-alkB4
additional information
three component alkane hydroxylase complex consisting of a particulate nonheme integral membrane alkane monooxygenase (AlkB), soluble rubredoxin (AlkG), and soluble rubredoxin reductase (AlkT), at least four alkane monooxygenase gene homologs alkB1-alkB4
additional information
three component alkane hydroxylase complex consisting of a particulate nonheme integral membrane alkane monooxygenase (AlkB), soluble rubredoxin (AlkG), and soluble rubredoxin reductase (AlkT), at least four alkane monooxygenase gene homologs alkB1-alkB4
additional information
three component alkane hydroxylase complex consisting of a particulate nonheme integral membrane alkane monooxygenase (AlkB), soluble rubredoxin (AlkG), and soluble rubredoxin reductase (AlkT), at least four alkane monooxygenase gene homologs alkB1-alkB4
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
octane + 2 reduced rubredoxin + O2 + 2 H+ = 1-octanol + 2 oxidized rubredoxin + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
alkane,reduced-rubredoxin:oxygen 1-oxidoreductase
Some enzymes in this group are heme-thiolate proteins (P-450). Also hydroxylates fatty acids in the omega-position.
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CAS REGISTRY NUMBER
COMMENTARY
9059-16-9
-
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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
1,7-octadiene + NADH + H+ + O2
1,2-epoxy-7-octene + NAD+ + H2O
-
epoxidation of simple, aliphatic terminal olefins
-
?
1-hexadecene + reduced rubredoxin + O2
? + oxidized rubredoxin + H2O
-
-
-
?
1-octadecene + reduced rubredoxin + O2
? + oxidized rubredoxin + H2O
-
-
-
?
2 1-octyne + 2 NADH + 2 H+ + 2 O2
1-octanoic acid + 7-octynoic acid + 2 NAD+ + 2 H2O
-
-
-
?
arachidonic acid + NAD(P)H + H+ + O2
(5Z,8Z,11Z,14Z)-20-hydroxyeicosa-5,8,11,14-tetraenoic acid + NAD(P)+ + H2O
arachidonic acid + NAD(P)H + H+ + O2
20-hydroxyicosa-5,8,11,14-tetraenoic acid + NAD(P)+ + H2O
bicyclohexane + reduced rubredoxin + O2
? + oxidized rubredoxin + H2O
-
i.e. bicyclo[3.1.0]hexane, no distinction between the 2- and 3-positions, reaction via formation of a substrate radical that persists in the active site
-
?
cyclohexane + NADH + H+ + O2
cyclohexanol + NAD+ + H2O
-
-
-
?
cyclopentane + NAD(P)H + H+ + O2
cyclopentanol + NAD(P)+ + H2O
-
very poor substrate
-
?
decane + reduced rubredoxin + O2
1-decanol + oxidized rubredoxin + H2O
-
-
-
?
decane + reduced rubredoxin + O2 + H+
1-decanol + oxidized rubredoxin + H2O
-
-
-
r
dicyclopropylketone + NAD(P)H + H+ + O2
? + NAD(P)+ + H2O
-
-
?
dodecane + reduced rubredoxin + O2
1-dodecanol + oxidized rubredoxin + H2O
-
-
-
?
eicosapentaenoic acid + NAD(P)H + H+ + O2
? + NAD(P)+ + H2O
-
is less omega-hydroxylated than 5,8,11-eicosatrienoic acid and arachidonic acid
-
?
ethyl tert-butyl ether + NAD(P)H + H+ + O2
tert-butyl-alcohol + NAD(P)+ + H2O + acetaldehyde
heptadecane + reduced rubredoxin + O2
1-heptadecanol + oxidized rubredoxin + H2O
-
-
-
?
heptanoate + NADPH + H+ + O2
?
-
59% activity compared to octane
-
r
hexadecane + reduced rubredoxin + O2
1-hexadecanol + oxidized rubredoxin + H2O
-
-
-
?
hexane + reduced rubredoxin + O2
1-hexanol + oxidized rubredoxin + H2O
-
-
-
?
hexane + reduced rubredoxin + O2 + H+
1-hexanol + oxidized rubredoxin + H2O
-
-
-
r
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxydodecanoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
methane sulfonic acid + reduced rubredoxin + O2
? + oxidized rubredoxin + H2O
-
-
-
?
methyl tert-butyl ether + NAD(P)H + H+ + O2
tert-butyl-alcohol + NAD(P)+ + H2O + formaldehyde
methyl tert-butyl ether + NAD(P)H + H+ + O2
tert-butyl-alcohol + NAD(P)+ + H2O + methanol
-
-
?
methylphenylcyclopropane + reduced rubredoxin + O2
1-phenylbut-3-en-1-ol + oxidized rubredoxin + H2O
-
reaction via formation of a substrate radical that persists in the active site
-
?
monoolein + NADH + H+ + O2
18-hydroxyoctadec-9-enoic acid 2,3-dihydroxypropyl ester + NAD+ + H2O
-
-
-
?
nitromethane + reduced rubredoxin + O2
? + oxidized rubredoxin + H2O
-
-
-
?
norcarane + reduced rubredoxin + O2
? + oxidized rubredoxin + H2O
-
i.e. bicyclo[4.1.0]heptane, oxidation preferentially occurs at the less sterically hindered 3-position, reaction via formation of a substrate radical that persists in the active site
-
?
octadecane + reduced rubredoxin + O2
1-octadecanol + oxidized rubredoxin + H2O
-
-
-
?
pentadecane + reduced rubredoxin + O2
1-pentadecanol + oxidized rubredoxin + H2O
-
best substrate
-
?
pentane + reduced rubredoxin + O2
1-pentanol + oxidized rubredoxin + H2O
-
-
-
?
propane + NADPH + H+ + O2
propan-1-ol + NADP+ + H2O
-
-
?
tert-amyl methyl ether + NAD(P)H + H+ + O2
tert-amyl-alcohol + NAD(P)+ + H2O + formaldehyde
tetracosane + reduced rubredoxin + O2
1-tetracosanol + oxidized rubredoxin + H2O
-
-
-
?
(n-1)-alkanoate + NADPH + H+ + O2
(omega-1)-hydroxy-n-alkanoate + NADP+ + H2O
-
-
-
?
(n-1)-alkanoate + NADPH + H+ + O2
(omega-1)-hydroxy-n-alkanoate + NADP+ + H2O
-
-
-
?
(n-1)-alkanoate + NADPH + H+ + O2
(omega-1)-hydroxy-n-alkanoate + NADP+ + H2O
-
-
-
?
(n-1)-alkanoate + NADPH + H+ + O2
(omega-1)-hydroxy-n-alkanoate + NADP+ + H2O
-
-
-
?
(n-1)-alkanoate + NADPH + H+ + O2
(omega-1)-hydroxy-n-alkanoate + NADP+ + H2O
-
chain length C10-C16
-
?
1-octene + reduced rubredoxin + O2
1,2-epoxyoctane + oxidized rubredoxin + H2O
epoxidation reaction catalysed by AlkB
-
?
1-octene + reduced rubredoxin + O2
1,2-epoxyoctane + oxidized rubredoxin + H2O
Pseudomonas putida GPo1 / ATCC29347
epoxidation reaction catalysed by AlkB
-
?
arachidonic acid + NAD(P)H + H+ + O2
(5Z,8Z,11Z,14Z)-20-hydroxyeicosa-5,8,11,14-tetraenoic acid + NAD(P)+ + H2O
-
-
-
?
arachidonic acid + NAD(P)H + H+ + O2
(5Z,8Z,11Z,14Z)-20-hydroxyeicosa-5,8,11,14-tetraenoic acid + NAD(P)+ + H2O
-
product formation relaxes distal human pulmonary arteries
-
?
arachidonic acid + NAD(P)H + H+ + O2
(5Z,8Z,11Z,14Z)-20-hydroxyeicosa-5,8,11,14-tetraenoic acid + NAD(P)+ + H2O
-
the rate of metabolism by CYPA11 P450 is 10-100fold less as compared to lauric acid
-
?
arachidonic acid + NAD(P)H + H+ + O2
(5Z,8Z,11Z,14Z)-20-hydroxyeicosa-5,8,11,14-tetraenoic acid + NAD(P)+ + H2O
-
-
-
?
arachidonic acid + NAD(P)H + H+ + O2
(5Z,8Z,11Z,14Z)-20-hydroxyeicosa-5,8,11,14-tetraenoic acid + NAD(P)+ + H2O
-
-
-
?
arachidonic acid + NAD(P)H + H+ + O2
20-hydroxyicosa-5,8,11,14-tetraenoic acid + NAD(P)+ + H2O
-
-
-
?
arachidonic acid + NAD(P)H + H+ + O2
20-hydroxyicosa-5,8,11,14-tetraenoic acid + NAD(P)+ + H2O
-
-
-
?
arachidonic acid + NAD(P)H + H+ + O2
20-hydroxyicosa-5,8,11,14-tetraenoic acid + NAD(P)+ + H2O
-
-
-
?
arachidonic acid + NADPH + H+ + O2
20-hydroxyeicosatetraenoic acid + NADP+ + H2O
-
-
-
?
arachidonic acid + NADPH + H+ + O2
20-hydroxyeicosatetraenoic acid + NADP+ + H2O
-
-
-
?
arachidonic acid + NADPH + H+ + O2
20-hydroxyeicosatetraenoic acid + NADP+ + H2O
-
-
-
?
cyclooctane + NAD(P)H + H+ + O2
cyclooctanol + NAD(P)+ + H2O
-
poor substrate
-
?
cyclooctane + NAD(P)H + H+ + O2
cyclooctanol + NAD(P)+ + H2O
-
poor substrate
-
?
ethyl tert-butyl ether + NAD(P)H + H+ + O2
tert-butyl-alcohol + NAD(P)+ + H2O + acetaldehyde
-
-
-
?
ethyl tert-butyl ether + NAD(P)H + H+ + O2
tert-butyl-alcohol + NAD(P)+ + H2O + acetaldehyde
Pseudomonas putida GPo1 / ATCC29347
-
-
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
-
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
protein from CYP52A3 has a higher affinity for fatty acids than for alkanes
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
high affinity for short chain fatty acids
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
protein from CYP52A3 has a higher affinity for fatty acids than for alkanes
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
-
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
-
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
-
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
NADPH-P-450 reductase and omega-hydrolase are 1 protein
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
-
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
-
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
pig liver NADPH-P450 reductase and cytochrome b5 are part of the system
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
3D-structure analysis, substrate pocket determination
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
medium-chain fatty acids
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
chain length C12-C16, arachidonic acid and oleic acid
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
-
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
-
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
laurate and arachidonic acid
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
chain length C10-C19
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
NADPH-P450 reductase and cytochrome b5 are part of the enzyme system
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
-
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
chain length C6-C14
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
chain length C6-C11, maximal activity with heptanoate
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
-
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
-
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
chain length C12-C16, arachidonic acid and oleic acid
-
?
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
-
-
-
?
lauric acid + NAD(P)H + H+ + O2
12-hydroxydodecanoic acid + NAD(P)+ + H2O
-
-
-
?
lauric acid + NAD(P)H + H+ + O2
12-hydroxydodecanoic acid + NAD(P)+ + H2O
-
-
-
?
lauric acid + NAD(P)H + H+ + O2
12-hydroxydodecanoic acid + NAD(P)+ + H2O
-
-
-
?
lauric acid + NAD(P)H + H+ + O2
12-hydroxydodecanoic acid + NAD(P)+ + H2O
-
-
-
?
lauric acid + NAD(P)H + H+ + O2
12-hydroxydodecanoic acid + NAD(P)+ + H2O
-
-
-
?
lauric acid + NAD(P)H + H+ + O2
12-hydroxydodecanoic acid + NAD(P)+ + H2O
-
-
-
?
lauric acid + NAD(P)H + H+ + O2
12-hydroxydodecanoic acid + NAD(P)+ + H2O
-
CYPA11 P450 efficiently and selectively omega-hydroxylates lauric acid
-
?
lauric acid + NAD(P)H + H+ + O2
12-hydroxydodecanoic acid + NAD(P)+ + H2O
-
-
-
?
lauric acid + NAD(P)H + H+ + O2
12-hydroxydodecanoic acid + NAD(P)+ + H2O
-
-
-
?
lauric acid + NAD(P)H + H+ + O2
12-hydroxydodecanoic acid + NAD(P)+ + H2O
-
-
-
?
lauric acid + NAD(P)H + H+ + O2
12-hydroxydodecanoic acid + NAD(P)+ + H2O
-
-
-
?
methyl tert-butyl ether + NAD(P)H + H+ + O2
tert-butyl-alcohol + NAD(P)+ + H2O
-
-
-
?
methyl tert-butyl ether + NAD(P)H + H+ + O2
tert-butyl-alcohol + NAD(P)+ + H2O
Pseudomonas putida GPo1 / ATCC29347
-
-
-
?
methyl tert-butyl ether + NAD(P)H + H+ + O2
tert-butyl-alcohol + NAD(P)+ + H2O + formaldehyde
-
-
-
?
methyl tert-butyl ether + NAD(P)H + H+ + O2
tert-butyl-alcohol + NAD(P)+ + H2O + formaldehyde
Pseudomonas putida GPo1 / ATCC29347
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
protein from CYP52A3 has a higher affinity for alkanes than for fatty acids
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
protein from CYP52A3 has a higher affinity for alkanes than for fatty acids
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
acts on C5-C13 alkanes, highest activity with n-hexane
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
acts on C5-C13 alkanes, highest activity with n-hexane
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
oxidizes C10-C16 alkanes
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
oxidizes C10-C16 alkanes
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
alkanes above C6
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
alkanes above C6
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
rubredoxin is electron carrier
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
chain length C6-C14
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
chain length C6-C16, maximal activity with n-octane
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
possible role in compensating low hydrocarbon concentrations
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
native strain oxidizes C6-C13 alkanes
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
oxidizes C5-C12 alkanes
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
Pseudomonas putida GPo1 / ATCC29347
-
possible role in compensating low hydrocarbon concentrations
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
Pseudomonas putida GPo1 / ATCC29347
-
oxidizes C5-C12 alkanes
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
Pseudomonas putida GPo1 / ATCC29347
-
native strain oxidizes C6-C13 alkanes
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
?
n-alkane + NADPH + H+ + O2
n-alkanol + NADP+ + H2O
-
initial activation of alkanes
-
?
n-butane + reduced rubredoxin + O2
1-butanol + oxidized rubredoxin + H2O
-
-
-
?
n-butane + reduced rubredoxin + O2
1-butanol + oxidized rubredoxin + H2O
-
-
-
?
n-dodecane + 2 reduced rubredoxin + O2 + 2 H+
1-dodecanol + 2 oxidized rubredoxin + H2O
-
-
?
n-dodecane + 2 reduced rubredoxin + O2 + 2 H+
1-dodecanol + 2 oxidized rubredoxin + H2O
-
-
?
n-hexadecane + NADPH + H+ + O2
n-hexadecanol + NADP+ + H2O
-
-
-
?
n-hexadecane + NADPH + H+ + O2
n-hexadecanol + NADP+ + H2O
-
-
-
?
n-hexadecane + NADPH + H+ + O2
n-hexadecanol + NADP+ + H2O
-
NADPH-cyt P-450-reductase
-
?
n-hexadecane + NADPH + H+ + O2
n-hexadecanol + NADP+ + H2O
-
NADPH-cyt P-450-reductase
-
?
n-hexadecane + NADPH + H+ + O2
n-hexadecanol + NADP+ + H2O
-
-
-
?
n-octane + NADH + H+ + O2
n-octanol + NAD+ + H2O
-
cytochrome P450 is electron carrier
-
?
n-octane + NADH + H+ + O2
n-octanol + NAD+ + H2O
-
cytochrome P450 is electron carrier
-
?
n-octane + reduced rubredoxin + O2
n-octanol + oxidized rubredoxin + H2O
-
-
-
?
n-octane + reduced rubredoxin + O2
n-octanol + oxidized rubredoxin + H2O
-
-
-
?
n-octane + reduced rubredoxin + O2
n-octanol + oxidized rubredoxin + H2O
-
-
-
?
n-propane + reduced rubredoxin + O2
1-propanol + oxidized rubredoxin + H2O
-
-
-
?
n-propane + reduced rubredoxin + O2
1-propanol + oxidized rubredoxin + H2O
-
-
-
?
octane + reduced rubredoxin + O2
1-octanol + oxidized rubredoxin + H2O
-
-
-
?
octane + reduced rubredoxin + O2
1-octanol + oxidized rubredoxin + H2O
-
-
-
?
octane + reduced rubredoxin + O2
1-octanol + oxidized rubredoxin + H2O
Pseudomonas putida GPo1 / ATCC29347
-
-
-
?
octane + reduced rubredoxin + O2
1-octanol + oxidized rubredoxin + H2O
-
-
-
?
palmitic acid + NAD(P)H + H+ + O2
16-hydroxyhexadecanoic acid + NAD(P)+ + H2O
-
-
-
?
palmitic acid + NAD(P)H + H+ + O2
16-hydroxyhexadecanoic acid + NAD(P)+ + H2O
-
-
-
?
palmitic acid + NAD(P)H + H+ + O2
16-hydroxyhexadecanoic acid + NAD(P)+ + H2O
-
-
-
?
palmitic acid + NAD(P)H + H+ + O2
16-hydroxyhexadecanoic acid + NAD(P)+ + H2O
-
-
-
?
palmitic acid + NAD(P)H + H+ + O2
16-hydroxyhexadecanoic acid + NAD(P)+ + H2O
-
-
-
?
palmitic acid + NAD(P)H + H+ + O2
16-hydroxyhexadecanoic acid + NAD(P)+ + H2O
-
CYPA11 P450 shows less selectivity in the metabolism of palmitic acid where both omega and omega-1 products are produced
-
?
palmitic acid + NAD(P)H + H+ + O2
16-hydroxyhexadecanoic acid + NAD(P)+ + H2O
-
-
-
?
propane + NADPH + H+ + O2
1-propanol + NADP+ + H2O
-
-
?
prostaglandin A1 + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
tert-amyl methyl ether + NAD(P)H + H+ + O2
tert-amyl-alcohol + NAD(P)+ + H2O + formaldehyde
-
-
-
?
tert-amyl methyl ether + NAD(P)H + H+ + O2
tert-amyl-alcohol + NAD(P)+ + H2O + formaldehyde
Pseudomonas putida GPo1 / ATCC29347
-
-
-
?
additional information
?
-
-
substrates are alkanes of chain length C8 to C12
-
?
additional information
?
-
-
AbAlkB can catalyze the hydroxylation of a large number of aromatic compounds and linear and cyclic alkanes. It does not catalyze the hydroxylation of alkanes with a chain length longer than 15 carbons, nor does it hydroxylate sterically hindered C-H bonds. GC-MS product analysis, overview. AbAlkB hydroxylates the terminal methyl group of medium chain alkanes, where octane is apparently close to the optimal chain length
-
?
additional information
?
-
-
20-hydroxyeicosatetraenoic acid modulates renal transport activities
-
?
additional information
?
-
-
CYP4A prefers to metabolize medium chain fatty acids (C10-C16)
-
?
additional information
?
-
-
CYP4A prefers to metabolize medium chain fatty acids (C10–C16)
-
?
additional information
?
-
-
substrates are alkanes of chain length C10 to C16
-
?
additional information
?
-
-
substrates are alkanes of chain length C10 to C16
-
?
additional information
?
-
-
substrates are alkanes of chain length C12 to C16
-
?
additional information
?
-
-
substrates of one isoform are alkanes of chain length C12 to C16, the second isoform hydroxylates octadecan or eicosan
-
?
additional information
?
-
-
the enzyme also catalyzes the oxygenative O-demethylation of ethers, the sulfoxidation of methyl sulfides and the stereoselective epoxidation of terminal olefins
-
?
additional information
?
-
-
physiological role of enzyme complex is to initiate the monoterminal oxidation of alkane chains
-
?
additional information
?
-
-
does not catalyze the hydroxylation of 1,1-dimethylcyclopropane or 1,1,2,2-tetramethylcyclopropane
-
?
additional information
?
-
-
AlkB, a nonheme diiron monooxygenase, performs regioselectibe hydroxylation of gem-difluorinated octanes, synthesis of 2,2-, 3,3- and 4,4-difluorooctan-1-ols from 1-octanal and 2-, 3-, 4-octanones, NMR and GC/MS product analysis, overview. Reactions of AlkB with 3,3- and 4,4-difluorooctanes and 1,1,1-trifluoroctane, synthesis of 2,2-, 3,3- 4,4-difluorooctan-1-ols, and of 8,8-, 7,7-, 6,6- and 5,5-difluorooctan-1-ols, overview
-
?
additional information
?
-
Pseudomonas putida GPo1 / ATCC29347
-
does not catalyze the hydroxylation of 1,1-dimethylcyclopropane or 1,1,2,2-tetramethylcyclopropane
-
?
additional information
?
-
Pseudomonas putida GPo1 / ATCC29347
-
AlkB, a nonheme diiron monooxygenase, performs regioselectibe hydroxylation of gem-difluorinated octanes, synthesis of 2,2-, 3,3- and 4,4-difluorooctan-1-ols from 1-octanal and 2-, 3-, 4-octanones, NMR and GC/MS product analysis, overview. Reactions of AlkB with 3,3- and 4,4-difluorooctanes and 1,1,1-trifluoroctane, synthesis of 2,2-, 3,3- 4,4-difluorooctan-1-ols, and of 8,8-, 7,7-, 6,6- and 5,5-difluorooctan-1-ols, overview
-
?
additional information
?
-
-
substrate specificity of the alkane hydroxylase large subunit, overview. Poor activity with 1-tetradecanol, no activity with octacosane, benzene, sodium benzoate, toluene, catechol, biphenyl, 1-hexadecanol, 1-stearyl alcohol, isooctane, pristine, and squalane
-
?
additional information
?
-
dodecane strongly binds to Cyp153D17 with similar Kd values as C10-C12 fatty acids
-
?
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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
arachidonic acid + NADPH + H+ + O2
20-hydroxyeicosatetraenoic acid + NADP+ + H2O
-
-
-
-
?
arachidonic acid + NADPH + H+ + O2
20-hydroxyeicosatetraenoic acid + NADP+ + H2O
-
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
possible role in compensating low hydrocarbon concentrations
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
Pseudomonas putida GPo1 / ATCC29347
-
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
Pseudomonas putida GPo1 / ATCC29347
-
possible role in compensating low hydrocarbon concentrations
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
Pseudomonas putida GPo1 / ATCC29347
-
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
-
-
-
?
n-alkane + NADPH + H+ + O2
n-alkanol + NADP+ + H2O
-
initial activation of alkanes
-
-
?
octane + reduced rubredoxin + O2
1-octanol + oxidized rubredoxin + H2O
-
-
-
-
?
octane + reduced rubredoxin + O2
1-octanol + oxidized rubredoxin + H2O
-
-
-
-
?
octane + reduced rubredoxin + O2
1-octanol + oxidized rubredoxin + H2O
Pseudomonas putida GPo1 / ATCC29347
-
-
-
-
?
additional information
?
-
-
20-hydroxyeicosatetraenoic acid modulates renal transport activities
-
-
?
additional information
?
-
-
physiological role of enzyme complex is to initiate the monoterminal oxidation of alkane chains
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ferredoxin
-
Rieske-type alkane monooxygenase with Rieske-type [2Fe-2S]2 center
-
heme
dodecane, capric acid, and lauric acid binding to CYP153D17 induces a 90% shift in the heme spin state from low-spin (Soret maximum at 420 nm) to high-spin (Soret maximum at 390 nm), whereas decane and myristic acid induces a 80% shift in the same heme spin state
NADH
-
hydroxylation needs also a NADH-dependent bacterial reductase
NADH
-
NADH-dependent alkane monooxygenase activity (C5 to C24), the alkane oxidation is coupled to NADH consumption
rubredoxin
endogenous, recombinantly expressed in Escherichia coli TG10 cells
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
Fe2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,1-dichloroethene
-
50% of BMO activity is irreversibly lost after oxidation of approximately 25 nmol/mg protein
1,2-cis-dichloroethene
-
50% of BMO activity is lost after oxidation of 120 nmol/mg protein
1,2-trans-dichloroethene
-
50% of BMO activity is lost after oxidation of 20 nmol/mg protein
1,7-octadiyne
-
inhibits oxidation of methyl tert-butyl ether; putative mechanism-based inactivator, strongly inhibitory at 0.1% (v/v)
n-alkanes
-
C5-C10 inhibits oxidation of methyl tert-butyl ether, weaker inhibition at longer chain length
N-hydroxy-N'-(4-n-butyl-2-methylphenyl)formamidine
-
HET0016, a potent and selective inhibitor of CYP omega-hydroxylase, significantly inhibits myocardial apoptosis. Pretreatment with PD98059, the inhibitor of ERK1/2, but not SB203580 or SP600125, almost completely blocks the effect exerted by HET0016. Exogenous 20-hydroxyeicosatetraenoic acid administration exerts opposite effects
N-methylsulfonyl-12, 12-dibromododec-11-enamide
-
a selective CYP omega-hydroxylase inhibitor, significantly inhibits myocardial apoptosis
(E)-N'-(4-butyl-2-methylphenyl)-N-hydroxyformimidamide
-
HET0016, almost completely abolishes hypotonic solutions- or 2,4,6-trinitrophenol-induced enhancement of receptor-activated cationic current I(TRPC6)
(E)-N'-(4-butyl-2-methylphenyl)-N-hydroxyformimidamide
-
HET0016, diminishes TRPC6-like channel activity in myocytes
1-octyne
-
irreversible inhibition, oxidation product hexylketene or its equivalent, covalently binds to AlkB
11-dodecynoic acid
-
completely inhibited lauric acid omega-hydroxylation
17-octadecynoic acid
-
almost completely abolishes hypotonic solutions- or 2,4,6-trinitrophenol-induced enhancement of receptor-activated cationic current I(TRPC6)
17-octadecynoic acid
-
irreversible CYP omega-hydroxylase inhibitor, significantly inhibits myocardial apoptosis
N-methylsulfonyl-12,12-dibromododec-11-enamide
-
0.4 mg/kg, significant inhibition
N-methylsulfonyl-12,12-dibromododec-11-enamide
-
specific inhibitor, results in an increased phenylephrine-induced tension
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
formate and propionate do not increase activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0182
pentadecane
-
pH 7.5, 30°C, recombinant alkane hydroxylase large subunit
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.17
arachidonic acid
-
CYP4A7, H206Y/S255F mutant, omega-hydroxylation
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
Pseudomonas putida GPo1 / ATCC29347
AlkW1; gene alkW1, alkane hydroxylase-Rd fusion gene homolog
UniProt
brenda
AlkW2; gene alkW2, a alkane hydroxylase-Rd fusion gene homolog
UniProt
brenda
formerly Pseudomonas oleovorans, strain PpG6, only 1 isoform of enzyme arranged in a complex
-
-
brenda
Q08KD8 i.e. subunit Prm1A, Q08KD7 i.e. subunit Prm1B, Q08KD6 i.e. subunit Prm1C, Q08KD5 i.e. subunit Prm1D, respectively
Q08KD8; Q08KD7 and Q08KD6; Q08KD5
UniProt
brenda
Q08KD8 i.e. subunit Prm2A, Q08KD7 i.e. subunit Prm2B, Q08KD6 i.e. subunit Prm2C, Q08KD5 i.e. subunit Prm2D, respectively
Q08KD8; Q08KD7 and Q08KD6; Q08KD5
UniProt
brenda
Q08KE2 i.e. subunit Prm1A, Q08KE1 i.e. subunit Prm1B, Q08KD0 i.e. subunit Prm1C, Q08KE9 i.e. subunit Prm1D, respectively
Q08KE2; Q08KE1 and Q08KE0; Q08KD9
UniProt
brenda
Q08KE2 i.e. subunit Prm1A, Q08KE1 i.e. subunit Prm1B, Q08KE0 i.e. subunit Prm1C, Q08KD9 i.e. subunit Prm1D, respectively
Q08KE2; Q08KE1 and Q08KE0; Q08KD9
UniProt
brenda
alkB1 gene from Rhodococcus Q15; strains Q15 and NRRL B-16531, strain NRRL B-16531 (ATCC 15960) formerly Corynebacterium hydrocarboclastus
SwissProt
brenda
alkB2 gene from Rhodococcus NRRL B-16531; strains Q15 and NRRL B-16531, strain NRRL B-16531 (ATCC 15960) formerly Corynebacterium hydrocarboclastus
SwissProt
brenda
alkB2 gene from Rhodococcus Q15; strains Q15 and NRRL B-16531, strain NRRL B-16531 (ATCC 15960) formerly Corynebacterium hydrocarboclastus
SwissProt
brenda
alkB3 gene from Rhodococcus Q15; strains Q15 and NRRL B-16531, strain NRRL B-16531 (ATCC 15960) formerly Corynebacterium hydrocarboclastus
SwissProt
brenda
alkB4 gene from Rhodococcus Q15; strains Q15 and NRRL B-16531, strain NRRL B-16531 (ATCC 15960) formerly Corynebacterium hydrocarboclastus
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
in the vibrissae, ventral outside edge of compound eyes, only males
brenda
additional information
strong root specificity and a localized expression in the root endodermis, high expression levels in all three root zones from the tip to the base
brenda
additional information
no detectable CYP86A1 transcript levels in above-ground organs such as leaves, stems, flowers, and siliques
brenda
additional information
strain DQ12-45-1b can grow on crude oil and n-alkanes ranging in length from 6 to 40 carbon atoms as sole carbon sources
brenda
additional information
strain DQ12-45-1b can grow on crude oil and n-alkanes ranging in length from 6 to 40 carbon atoms as sole carbon sources
brenda
additional information
-
SXE1 protein expression is restricted to nonneuronal cells associated with diverse sensory bristles of both the chemo- and mechanosensory systems. Is present in labial palps and tips of maxillary palps in males and females, and in the base of bristles of the forelegs and the base of arista of males
brenda
additional information
-
the alkane hydroxylase system of Pseudomonas putida GPo1 allows it to use alkanes as the sole source of carbon and energy
brenda
additional information
Pseudomonas putida GPo1 / ATCC29347
-
the alkane hydroxylase system of Pseudomonas putida GPo1 allows it to use alkanes as the sole source of carbon and energy
brenda
additional information
-
strain T7-7 is able to utilize diesel oils, C5 to C30 alkane, as a sole carbon and energy source
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
membrane-bound enzyme, needs 20 molecules phospholipid per polypeptide chain
-
brenda
-
in nonneuronal cells associated largely with sensory bristles
brenda
transgenic expression of CYP86A1 fused to GFP distributes CYP86A1 to the endoplasmic reticulum, indicating that suberin monomer biosynthesis takes place in this sub-cellular compartment before intermediates are exported in the apoplast
brenda
-
integral membrane protein with six membrane-spanning segments
brenda
-
integral membrane protein with six membrane-spanning segments
brenda
-
integral membrane protein with six membrane-spanning segments
brenda
-
integral membrane protein with six membrane-spanning segments
brenda
-
integral membrane protein with six membrane-spanning segments
brenda
-
AlkB is the integral membrane component of the Pseudomonas putida alkane hydroxylase system
brenda
Pseudomonas putida GPo1 / ATCC29347
-
AlkB is the integral membrane component of the Pseudomonas putida alkane hydroxylase system
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
loss-of-function cyp86B1/ralph mutants display a novel suberin monomer composition. Complete knockout of CYP86B1 in ralph1 and ralph2 leads to an almost complete lack of C22 and C24 omega-hydroxyacids and alpha,omega-dicarboxylic fatty acids in the seed coat polyester and is accompanied by a strong increase in C22 and C24 unsubstituted, saturated fatty acids
malfunction
-
mutations in CYP703A2 or CYP704B1 genes result in pollen with remarkably similar zebra phenotypes (impaired pollen walls that lack a normal exine layer and exhibit a characteristic striped surface). Double and triple mutant combinations do not result in the appearance of novel phenotypes or enhancement of single mutant phenotypes
malfunction
-
several diseases are genetically linked to the expression of CYP4 gene polymorphic variants, which may link human susceptibility to diseases of lipid metabolism and the activation and resolution phases of inflammation
malfunction
-
suppression or knockout of sxe1 significantly reduces mating success in males throughout the diurnal cycle
metabolism
-
CYP4A functions in liver fatty acid metabolism. Increased expression of the CYP4A omega hydroxylase during steatohepatitis and their induction in animals fed a high fat diet suggest they may play a pivotal role in preventing lipotoxicity, and may be responsible for induction of oxidative stress and progression to steatohepatitis. Omega-hydroxylation of the CYP2C arachidonic acid metabolite epoxyeicosatrienonic acid to omega-hydroxylated eicosatrienoic acid can induce peroxisome proliferation in rodents
metabolism
-
CYP4A11 is the least efficient CYP450 omega-hydroxylase in PUFA metabolism. PUFA hydroxylation by CYP4A11 is low and only slightly regiospecific
metabolism
-
the metabolomic profile of wild-type and sxe1 mutant males reveals that sxe1 likely functions as a fatty acid omega-hydroxylase, suggesting that male courtship and mating success is mediated by small compounds generated by this enzyme
metabolism
-
multiple alkane hydroxylase systems ensure the utilization of substrates of a broad chain length range
metabolism
-
multiple alkane hydroxylase systems ensure the utilization of substrates of a broad chain length range
physiological function
-
CYP omega-hydroxylase inhibition exerts significant anti-apoptosis effects, at least in part, by activation of ERK1/2 in ischemia/reperfusion heart. Inhibition reduces the infarct size of heart, decreases DNA fragmentation, reduces TUNEL-positive cells, attenuates caspase-3 activation, and modulates genes associated with apoptosis in rats rendered ischemia followed by reperfusion
physiological function
-
CYP703A2 and CYP704B1 together with the fatty acyl reductase MALE STERILITY2 are required to provide an indispensable subset of fatty acid-derived components within the sporopollenin biosynthesis framework
physiological function
CYP86B1 is involved in polyester monomer biosynthesis during the course of plant development, has a role in suberin biogenesis
physiological function
is a key enzyme for aliphatic root suberin biosynthesis. In contrast to wild-type, no CYP86A1 transcript in total RNA from horst-1 seedlings (carries the T-DNA insertion in the first exon of CYP86A1) and horst-2 seedlings (T-DNA insertion is located in the second exon). Complemented CYP86A1-transformed horst-1 plants reveal a quantitative and qualitative aliphatic suberin composition similar to the wild-type
physiological function
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simultaneous operation of receptor and mechanical stimulations may synergistically amplify transmembrane Ca2+ mobilization through the activation of the non-voltage-gated Ca2+ entry/depolarization channel TRPC6, thereby enhancing the vascular tone via phospholipase C/diacylglycerol and phospholipase A(2)/omega-hydroxylase/20-hydroxyeicosatetraenoic acid pathways
physiological function
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simultaneous operation of receptor and mechanical stimulations may synergistically amplify transmembrane Ca2+ mobilization through the activation of the non-voltage-gated Ca2+ entry/depolarization channel TRPC6, thereby enhancing the vascular tone via phospholipase C/diacylglycerol and phospholipase A(2)/omega-hydroxylase/20-hydroxyeicosatetraenoic acid pathways. Activation of the cytosolic phospholipase A(2)/omega-hydroxylase cascade and consequent production of 20-hydroxyeicosatetraenoic acid is essential for the mechanical enhancement of receptor-activated TRPC6 current/channel activity
physiological function
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SXE1 is necessary for efficient male mating. Male-specific transcriptional regulator DSX(M) and the clock genes are necessary for cycling of sxe1 mRNA during the diurnal cycle
physiological function
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the alkane hydroxylase system of Pseudomonas putida GPo1 allows it to use alkanes as the sole source of carbon and energy. The alkane hydroxylase system of Pseudomonas putida GPo1 comprises three protein components: AlkB, soluble NADH-rubredoxin reductase, and soluble electron transfer protein rubredoxin. AlkB transfers one oxygen atom from O2 to the alkane molecule, while the other oxygen is reduced to H2O using the electrons provided by NADH-rubredoxin reductase via rubredoxin
physiological function
Mycobacterium sp. TY-6 has two distinct gene clusters for multicomponent monooxygenases involved in alkane oxidation. Propane is oxidized to 1-propanol through terminal oxidation in Mycobacterium sp. TY-6
physiological function
propane is oxidized to 1-propanol and 2-propanol through both terminal and subterminal oxidations in Pseudonocardia sp. TY-7
physiological function
Pseudonocardia sp. TY-7 has two distinct gene clusters for multicomponent monooxygenases involved in alkane oxidation. Propane is oxidized to 1-propanol through terminal oxidation in Mycobacterium sp. TY-6
physiological function
an AlkW1 gene knockout strain is able to grow with C28 n-alkane as the sole carbon source, presence of two further long-chain alkane hydroxylase genes G1 and G2 whose expression in induced upon growth on C28 n-alkane
physiological function
an isoform AlkB1 mutant demonstrates a markedly lower degradative rate for C21 to C32 n-alkanes compared to wild-type. An isoform AlkB1/AlkB2 a double mutant shows a trend towards recovery when C20-C24 are used as sole carbon source
physiological function
degradation of n-alkanes in Rhodococcus opacus R7 with consumption rates of 88% for n-dodecane, 69% for n-hexadecane, 51% for n-eicosane and 78% for n-tetracosane. Expression of the AlkB gene in Rhodococcus erythropolis leads to increased biodegradation of n-dodecane
physiological function
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for the medium-chain n-alkanes (C12-C16), single-knockout mutants of isoforms AlkB1 and AlkB2 show an obvious delay as compared to the wild type SJTD-1, and double-knockout mutants cannot utilize the n-alkanes at all. The loss of AlkB2 show a more pronounced effect on the cell growth than the loss of AlkB1. The poor viability of the double mutant recovers to a normal state when C18-C24 alkanes are used as the sole source of carbon
physiological function
isoform AlkB2 acts in the early growth phase and plays a major role in the utilization of C12-C18. An isoform AlkB1/AlkB2 a double mutant shows a trend towards recovery when C20-C24 are used as sole carbon source
physiological function
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one rubredoxin AlkG with two Fe-4S electron transfer centres can bind with two membrane-bound AlkB to form an AlkG:2AlkB adduct, facilitating an efficient conversion of n-octane to 1-octanol. the specific activity among all chain length linear alkanes tested varies, there is no particular relationship between the specific activity and the chain length of alkanes
physiological function
the expression of isoforms MAH1-1 and MAH1-2 is barely detected in stem and leaf of a wax deficient cultivar
physiological function
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degradation of n-alkanes in Rhodococcus opacus R7 with consumption rates of 88% for n-dodecane, 69% for n-hexadecane, 51% for n-eicosane and 78% for n-tetracosane. Expression of the AlkB gene in Rhodococcus erythropolis leads to increased biodegradation of n-dodecane
physiological function
Pseudomonas putida GPo1 / ATCC29347
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the alkane hydroxylase system of Pseudomonas putida GPo1 allows it to use alkanes as the sole source of carbon and energy. The alkane hydroxylase system of Pseudomonas putida GPo1 comprises three protein components: AlkB, soluble NADH-rubredoxin reductase, and soluble electron transfer protein rubredoxin. AlkB transfers one oxygen atom from O2 to the alkane molecule, while the other oxygen is reduced to H2O using the electrons provided by NADH-rubredoxin reductase via rubredoxin
physiological function
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isoform AlkB2 acts in the early growth phase and plays a major role in the utilization of C12-C18. An isoform AlkB1/AlkB2 a double mutant shows a trend towards recovery when C20-C24 are used as sole carbon source
physiological function
-
an isoform AlkB1 mutant demonstrates a markedly lower degradative rate for C21 to C32 n-alkanes compared to wild-type. An isoform AlkB1/AlkB2 a double mutant shows a trend towards recovery when C20-C24 are used as sole carbon source
physiological function
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one rubredoxin AlkG with two Fe-4S electron transfer centres can bind with two membrane-bound AlkB to form an AlkG:2AlkB adduct, facilitating an efficient conversion of n-octane to 1-octanol. the specific activity among all chain length linear alkanes tested varies, there is no particular relationship between the specific activity and the chain length of alkanes
physiological function
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for the medium-chain n-alkanes (C12-C16), single-knockout mutants of isoforms AlkB1 and AlkB2 show an obvious delay as compared to the wild type SJTD-1, and double-knockout mutants cannot utilize the n-alkanes at all. The loss of AlkB2 show a more pronounced effect on the cell growth than the loss of AlkB1. The poor viability of the double mutant recovers to a normal state when C18-C24 alkanes are used as the sole source of carbon
additional information
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AlkB contains a nonheme diiron center as a catalytic site
additional information
both AlkW1 and AlkW2 have an integral-membrane alkane monooxygenase, AlkB, conserved domain and a rubredoxin conserved domain which are fused together
additional information
both AlkW1 and AlkW2 have an integral-membrane alkane monooxygenase, AlkB, conserved domain and a rubredoxin conserved domain which are fused together
additional information
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reconstitution of enzyme activity with the purified protein in an assay with purified rubredoxin, purified maize ferredoxin reductase, NADPH, and selected substrates. i.e. bicyclo[4.1.0]heptane (norcarane), bicyclo[3.1.0]hexane (bicyclohexane), methylphenylcyclopropane and deuterated and non-deuterated cyclohexane. Purified AbAlkB hydroxylates substrates by forming a substrate radical, the rate-determining step has a significant C-H bond breaking character
additional information
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the alkane hydroxylase system consists of the alkane hydroxylase large subunit, the alkane hydroxylase small subunit, the NADH-dependent reductase subunit, and the ferredoxin subunit. Analysis of the interaction between large and small subunits of the monooxygenase, overview
additional information
Pseudomonas putida GPo1 / ATCC29347
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AlkB contains a nonheme diiron center as a catalytic site
Show AA Sequence and Transmembrane Helices (1166 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
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recombinant His6-tagged alkane hydroxylase large subunit, native PAGE
2000000
53000
53000
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3 * 53000, recombinant His6-tagged alkane hydroxylase large subunit, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
additional information
?
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x * 42100, calculated for isoform AlkB1, x * 41600, calculated for isoform AlkB2
?
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x * 42100, calculated for isoform AlkB1, x * 41600, calculated for isoform AlkB2
trimer
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3 * 53000, recombinant His6-tagged alkane hydroxylase large subunit, SDS-PAGE
additional information
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the physiologically active form of membrane-embedded AlkB may be a multimer, the monomeric form of AlkB produced by purification in n-decyl-beta-D-maltopyranoside, n-dodecyl-beta-D-maltopyranoside, octyl glucose neopentyl glycol, and n-dodecyl-N,N-dimethylamine-N-oxide is largely inactive. In contrast, detergents that do not disrupt the AlkB oligomeric state, i.e. decyl maltose neopentyl glycol, lauryl maltose neopentyl glycol, and octaethylene glycol monododecyl ether, preserve the enzyme activity at a level close to that of the detergent-free control sample
additional information
Pseudomonas putida GPo1 / ATCC29347
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the physiologically active form of membrane-embedded AlkB may be a multimer, the monomeric form of AlkB produced by purification in n-decyl-beta-D-maltopyranoside, n-dodecyl-beta-D-maltopyranoside, octyl glucose neopentyl glycol, and n-dodecyl-N,N-dimethylamine-N-oxide is largely inactive. In contrast, detergents that do not disrupt the AlkB oligomeric state, i.e. decyl maltose neopentyl glycol, lauryl maltose neopentyl glycol, and octaethylene glycol monododecyl ether, preserve the enzyme activity at a level close to that of the detergent-free control sample
additional information
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the alkane hydroxylase system consists of the alkane hydroxylase large subunit, the alkane hydroxylase small subunit, the NADH-dependent reductase subunit, and the ferredoxin subunit
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology miodeling of structure and docking of octane, octanol and 1-octyne. Residues Ala53, Trp55, Val15 and Tyr339 of AlkB are involved in the octane uptake/binding, octanol binding/exit, and the 1-octyne uptake/binding
to 3.1 A resolution, the alkane-like substrate is in the hydrophobic pocket containing residues Thr74, Met90, Ala175, Ile240, Leu241, Val244, Leu292, Met295, and Phe393. Conformational changes in the beta1-beta2, alpha3-alpha4 and alpha6-alpha7 connecting loop are important for incorporating the long hydrophobic substrate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE