Information on EC 1.14.15.3 - alkane 1-monooxygenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.14.15.3
-
RECOMMENDED NAME
GeneOntology No.
alkane 1-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
octane + 2 reduced rubredoxin + O2 + 2 H+ = 1-octanol + 2 oxidized rubredoxin + H2O
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydroxylation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
octane oxidation
Fatty acid degradation
-
-
Arachidonic acid metabolism
-
-
Retinol metabolism
-
-
Caprolactam degradation
-
-
Metabolic pathways
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9059-16-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
genes alkB1, alkB2, p450 and almA
-
-
Manually annotated by BRENDA team
genes alkB1, alkB2, p450 and almA
-
-
Manually annotated by BRENDA team
strain ATCC22711
-
-
Manually annotated by BRENDA team
strain ATCC22711
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment; strain ATCC 12670
Q5K1Y1
SwissProt
Manually annotated by BRENDA team
fragment
Q5K1Z0
SwissProt
Manually annotated by BRENDA team
fragment
Q5K1Z0
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
2 isoforms
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-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(n-1)-alkanoate + NADPH + H+ + O2
(omega-1)-hydroxy-n-alkanoate + NADP+ + H2O
show the reaction diagram
1,1-diethylcyclopropane + NADPH + H+ + O2
?
show the reaction diagram
1,7-octadiene + NADH + H+ + O2
1,2-epoxy-7-octene + NAD+ + H2O
show the reaction diagram
-
epoxidation of simple, aliphatic terminal olefins
-
-
?
1-hexadecene + reduced rubredoxin + O2
? + oxidized rubredoxin + H2O
show the reaction diagram
-
-
-
-
?
1-octadecene + reduced rubredoxin + O2
? + oxidized rubredoxin + H2O
show the reaction diagram
-
-
-
-
?
1-octene + reduced rubredoxin + O2
1,2-epoxyoctane + oxidized rubredoxin + H2O
show the reaction diagram
1-octyne + NADH + H+ + O2
1-octanoic acid + oct-7-ynoic acid + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
2,5-dimethylhexane + NADH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
5,8,11-eicosatrienoic acid + NAD(P)H + H+ + O2
? + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
arachidonic acid + NAD(P)H + H+ + O2
(5Z,8Z,11Z,14Z)-20-hydroxyeicosa-5,8,11,14-tetraenoic acid + NAD(P)+ + H2O
show the reaction diagram
arachidonic acid + NAD(P)H + H+ + O2
20-hydroxyicosa-5,8,11,14-tetraenoic acid + NAD(P)+ + H2O
show the reaction diagram
arachidonic acid + NADPH + H+ + O2
20-hydroxyeicosatetraenoic acid + NADP+ + H2O
show the reaction diagram
bicyclohexane + reduced rubredoxin + O2
? + oxidized rubredoxin + H2O
show the reaction diagram
-
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
-
-
?
butane + NADPH + H+ + O2
1-butanol + NADP+ + H2O
show the reaction diagram
cycloheptane + NAD(P)H + H+ + O2
cycloheptanol + NAD(P)+ + H2O
show the reaction diagram
cyclohexane + NAD(P)H + H+ + O2
cyclohexanol + NAD(P)+ + H2O
show the reaction diagram
cyclohexane + NADH + H+ + O2
cyclohexanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
cyclooctane + NAD(P)H + H+ + O2
cyclooctanol + NAD(P)+ + H2O
show the reaction diagram
cyclopentane + NAD(P)H + H+ + O2
cyclopentanol + NAD(P)+ + H2O
show the reaction diagram
-
very poor substrate
-
-
?
decane + reduced rubredoxin + O2
1-decanol + oxidized rubredoxin + H2O
show the reaction diagram
-
-
-
-
?
dicyclopropylketone + NAD(P)H + H+ + O2
? + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
docosahexaenoic acid + NAD(P)H + H+ + O2
? + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
dodecane + reduced rubredoxin + O2
1-dodecanol + oxidized rubredoxin + H2O
show the reaction diagram
-
-
-
-
?
eicosapentaenoic acid + NAD(P)H + H+ + O2
? + NAD(P)+ + H2O
show the reaction diagram
-
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
show the reaction diagram
fatty acid + NAD(P)H + H+ + O2
omega-hydroxy fatty acid + NAD(P)+ + H2O
show the reaction diagram
heptadecane + reduced rubredoxin + O2
1-heptadecanol + oxidized rubredoxin + H2O
show the reaction diagram
-
-
-
-
?
hexadecane + reduced rubredoxin + O2
1-hexadecanol + oxidized rubredoxin + H2O
show the reaction diagram
-
-
-
-
?
hexane + reduced rubredoxin + O2
1-hexanol + oxidized rubredoxin + H2O
show the reaction diagram
-
-
-
-
?
lauric acid + NAD(P)H + H+ + O2
12-hydroxydodecanoic acid + NAD(P)+ + H2O
show the reaction diagram
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxydodecanoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
lecithin + NADH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
methane + NADPH + H+ + O2
methanol + NADP+ + H2O
show the reaction diagram
methane sulfonic acid + reduced rubredoxin + O2
? + oxidized rubredoxin + H2O
show the reaction diagram
-
-
-
-
?
methyl tert-butyl ether + NAD(P)H + H+ + O2
tert-butyl-alcohol + NAD(P)+ + H2O
show the reaction diagram
methyl tert-butyl ether + NAD(P)H + H+ + O2
tert-butyl-alcohol + NAD(P)+ + H2O + formaldehyde
show the reaction diagram
methyl tert-butyl ether + NAD(P)H + H+ + O2
tert-butyl-alcohol + NAD(P)+ + H2O + methanol
show the reaction diagram
-
-
-
?
methylcyclohexane + NADH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
methylphenylcyclopropane + reduced rubredoxin + O2
1-phenylbut-3-en-1-ol + oxidized rubredoxin + H2O
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
show the reaction diagram
n-alkane + NADPH + H+ + O2
n-alkanol + NADP+ + H2O
show the reaction diagram
n-butane + NADPH + H+ + O2
n-butanol + NADP+ + H2O
show the reaction diagram
n-butane + reduced rubredoxin + O2
1-butanol + oxidized rubredoxin + H2O
show the reaction diagram
n-dodecane + 2 reduced rubredoxin + O2 + 2 H+
1-dodecanol + 2 oxidized rubredoxin + H2O
show the reaction diagram
n-hexadecane + NADPH + H+ + O2
n-hexadecanol + NADP+ + H2O
show the reaction diagram
n-octane + NADH + H+ + O2
n-octanol + NAD+ + H2O
show the reaction diagram
n-octane + reduced rubredoxin + O2
n-octanol + oxidized rubredoxin + H2O
show the reaction diagram
n-propane + reduced rubredoxin + O2
1-propanol + oxidized rubredoxin + H2O
show the reaction diagram
nitromethane + reduced rubredoxin + O2
? + oxidized rubredoxin + H2O
show the reaction diagram
-
-
-
-
?
norcarane + NADPH + H+ + O2
?
show the reaction diagram
norcarane + reduced rubredoxin + O2
? + oxidized rubredoxin + H2O
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
octane + reduced rubredoxin + O2
1-octanol + oxidized rubredoxin + H2O
show the reaction diagram
palmitic acid + NAD(P)H + H+ + O2
16-hydroxyhexadecanoic acid + NAD(P)+ + H2O
show the reaction diagram
pentadecane + reduced rubredoxin + O2
1-pentadecanol + oxidized rubredoxin + H2O
show the reaction diagram
-
best substrate
-
-
?
pentane + reduced rubredoxin + O2
1-pentanol + oxidized rubredoxin + H2O
show the reaction diagram
-
-
-
-
?
phosphatidylethanolamine + NADH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
phosphatidylserine + NADH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
propane + NADPH + H+ + O2
1-propanol + NADP+ + H2O
show the reaction diagram
propane + NADPH + H+ + O2
propan-1-ol + NADP+ + H2O
show the reaction diagram
Q08KD8; Q08KD7 andQ08KD6; Q08KD5;, Q08KE2; Q08KE1 andQ08KD0; Q08KE9;, Q08KE2; Q08KE1 andQ08KE0; Q08KD9;
-
-
-
?
propane + NADPH + H+ + O2
propanol + NADP+ + H2O
show the reaction diagram
prostaglandin A1 + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
prostaglandin A2 + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
prostaglandin E1 + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
spirooctane + NADPH + H+ + O2
?
show the reaction diagram
stearic acid + NAD(P)H + H+ + O2
? + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
suberin + NADPH + H+ + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
?
tert-amyl methyl ether + NAD(P)H + H+ + O2
tert-amyl-alcohol + NAD(P)+ + H2O + formaldehyde
show the reaction diagram
tetracosane + reduced rubredoxin + O2
1-tetracosanol + oxidized rubredoxin + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
arachidonic acid + NADPH + H+ + O2
20-hydroxyeicosatetraenoic acid + NADP+ + H2O
show the reaction diagram
n-alkane + NAD(P)H + H+ + O2
n-alkanol + NAD(P)+ + H2O
show the reaction diagram
n-alkane + NADPH + H+ + O2
n-alkanol + NADP+ + H2O
show the reaction diagram
octane + reduced rubredoxin + O2
1-octanol + oxidized rubredoxin + H2O
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
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
NAD(P)+
-
-
NAD(P)H
NAD+
-
very little activity at 1 mM level
rubredoxin
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Al3+
-
activates
Cu
-
0.03 atoms per 42000 g/mol peptide
Iron
-
required, diiron enzyme
additional information
-
no or poor effects by Na and K+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(E)-N'-(4-butyl-2-methylphenyl)-N-hydroxyformimidamide
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)
1-octyne
11-dodecynoic acid
17-octadecynoic acid
8-hydroxyquinoline
diethyldithiocarbamate
-
reduces activity to 88%
Fe2+
-
in 0.5 mM concentration, 100% inhibition
Hg2+
-
0.1 mM concentration, 100% inhibition
menadione
-
-
n-alkanes
-
C5-C10 inhibits oxidation of methyl tert-butyl ether, weaker inhibition at longer chain length
n-butane
-
inhibits oxidation of methyl tert-butyl ether
n-decane
-
0.1% (v/v)
n-decyl-beta-D-maltopyranoside
-
-
n-dodecane
-
0.1% (v/v)
n-dodecyl-beta-D-maltopyranoside
-
-
n-dodecyl-N,N-dimethylamine-n-oxide
-
-
n-heptane
-
0.1% (v/v)
n-hexane
-
0.1% (v/v)
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
N-methylsulfonyl-12,12-dibromododec-11-enamide
n-nonane
-
0.1% (v/v)
n-octane
-
0.1% (v/v)
n-pentane
-
0.1% (v/v)
octyl glucose neopentyl glycol
-
-
p-chloromercuribenzoate
-
0.1 mM concentration, 51% inhibition
propane
-
inhibits oxidation of methyl tert-butyl ether
propionate
-
0.01 mM, strong inhibition
retinoic acid
-
0.005 mM, 56% reduction of activity
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-butanol
-
2 mM
Butyraldehyde
-
2 mM
dilauroylphosphatidylcholine
-
needs detergent
Emulgen 911
-
needs detergent 0.3%
-
Emulgen 913
-
needs detergent 0.1%
Phospholipid
-
enhances enzyme activity
Triton X-100
-
needs detergent, 0.04%
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
1-octene
pH 7.4, 30°C, recombinant enzyme
0.228
arachidonic acid
-
-
0.58
decane
-
-
5.2
Heptanoate
-
-
22
hexanoate
-
-
0.032 - 0.057
laurate
0.029 - 0.16
lauric acid
0.69
Nonanoate
-
-
0.77
Octane
-
-
0.0182
pentadecane
-
pH 7.5, 30°C, recombinant alkane hydroxylase large subunit
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0025 - 2.33
arachidonic acid
0.0267 - 2.67
laurate
0.0085 - 0.163
lauric acid
0.013
palmitate
-
omega-hydroxylation
0.0105 - 0.0367
palmitic acid
0.00133
PGA1
-
omega-hydroxylation
0.183 - 0.417
prostaglandin E1
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037
n-butane
-
inhibits oxidation of methyl tert-butyl ether
0.192
propane
-
inhibits oxidation of methyl tert-butyl ether
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00012
-
using ethyl tert-butyl ether as a substrate
0.00313
-
using tert-amyl methyl ether as a substrate
0.0077
-
pH 7.0, 30°C
0.00773
-
using methyl tert-butyl ether as a substrate
0.57
-
H318A mutant enzyme, 22°C
0.67
-
H308A mutant enzyme, 22°C
1.11
-
H163A mutant enzyme, 22°C
1.23
-
hydroxylation of octane
1.75
-
epoxidation of 1,7-octadiene
2.03
-
native enzyme, 22°C
6.5
-
hydroxylation of lauric acid
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
assay conditions
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7 - 7.5
-
laurate hydroxylation in Tris buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
25
-
assay conditions
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
second antennal segment, only males
Manually annotated by BRENDA team
-
in the vibrissae, ventral outside edge of compound eyes, only males
Manually annotated by BRENDA team
high expression level; high expression level
Manually annotated by BRENDA team
-
at the base of machrochaetae, only males
Manually annotated by BRENDA team
-
CYP4A11 is one of the major kidney CYP4 P450s
Manually annotated by BRENDA team
highest expression level; highest expression level
Manually annotated by BRENDA team
elevated expression
Manually annotated by BRENDA team
high expression level; high expression level
Manually annotated by BRENDA team
high expression level; high expression level
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
guard cells in the epidermis
Manually annotated by BRENDA team
PDB
SCOP
CATH
UNIPROT
ORGANISM
Q5F4D9
Sphingopyxis macrogoltabida;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40100
-
x * 40100, amino acid composition
42000
-
x * 42000, SDS-PAGE
46000
-
x * 46000, recombinant Strep-tagged AlkB, SDS-PAGE
52000
-
Western blot analysis
55000
-
gene expression CYP52A3, SDS-PAGE
56500
-
gene expression CYP52A4, SDS-PAGE
58000
-
Western blot analysis
59800
-
gene expression CYP52A3, amino acid composition
61800
-
gene expression CYP52A4, amino acid composition
118000
-
SDS-PAGE
150000
-
above, native enzyme, gel filtration
160000
-
recombinant His6-tagged alkane hydroxylase large subunit, native PAGE
800000
-
gel filtration
2000000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
5% carbohydrate
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2D crystallization
-
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
molecular modeling of the transmembrane domain
-
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
purified recombinant enzyme, 15 min, inactivation
71.2
-
melting temperature, mutant K18A
74.5
-
melting temperature, wild-type
75.3
-
melting temperature, mutant K359A
78.7
-
melting temperature, mutant K193A
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
after 24 h 15 mM EDTA 60% activity and iron retained
-
after 4 h 15 mM EDTA and 10 mM dithionite 10% activity and iron retained
-
treatment with 0.1 M EDTA and 0.1 M dithionite reduces activity to 10%
-
treatment with sodium cholate and subsequent precipitation with ammonium sulfate reduces activity to 40%
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1 month, under 50% activity retained
-
-20°C, loss of 30% activity by freezing and subsequent thawing
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-30°C, 1 month, loss of 50% activity towards prostaglandin A1
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-30°C, 3 years, no loss of activity towards laurate
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-70°C, 12 days, over 90% activity retained
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-70°C, 6 months, over 50% activity retained
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4°C, 5 days, under 50% activity retained
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme is solubilized from membranes and further purified by anion exchange chromatography and gel filtration
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recombinant C-terminally StrepII-tagged AlkB from membranes of Escherichia coli strain NovaBlue by detergent solubilization, and Strep-tag affinity chromatography
recombinant enzyme
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recombinant His6-tagged enzyme system components from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant Strep-tagged enzyme from Escherichia coli strains BL21(DE3), C41(DE3), Rosetta-2(DE3), pLysS, and BL21-CondonPlus(DE3)-RIPL by Strep-tag affinity chromatography, ultrafiltration, and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alkB genes expressed in Escherichia coli und Pseudomonas fluorescence; alkB genes expressed in Escherichia coli und Pseudomonas fluorescence; alkB genes expressed in Escherichia coli und Pseudomonas fluorescence; alkB genes expressed in Escherichia coli und Pseudomonas fluorescence
all components of the alkane ydroxylase system expressed in Escherichia coli TOP10
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baculovirus expressed human CYP4A11
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CYP86B1-YFP fusion protein expressed under the control of the 35S promoter in a transient expression assay in Nicotiana benthamiana leaves. ProCYP86B1::GUS transgenic plants
expressed in Escherichia coli , human gene CYP4AII
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expressed in Escherichia coli BL21(DE3)pLysS
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expressed in Escherichia coli strain XL1 and SCS1
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expressed in Escherichia coli XL-1 blue, human gene CYP4A1
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expressed in Escherichia coli, genes CYP4A1, CYP4A2, CYP4A3 and CYP4A8
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expressed in Escherichia coli, human gene CYP4A11
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expressed in Pseudomonas fluorescence KOB2delta1
expressed in Pseudomonas putida strain GPo12
expressed in Saccharomyces cerevisiae strain GRF18
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expressed in Saccharomyces cerevisiae strain WAT11
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expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli
gene alkB, expression of C-terminally StrepII-tagged AlkB in membranes of Escherichia coli strain NovaBlue
gene alkB, expression of Strep-tagged enzyme in Escherichia coli strains BL21(DE3), C41(DE3), Rosetta-2(DE3), pLysS, and BL21-CondonPlus(DE3)-RIPL under different growth conditions
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gene alkW1, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons and phylogenetic analysis, quantitative RT-PCR expression analysis, heterologous expression of alkW1 in alkB-deficient P.seudomonas fluorescens and functional complementation; gene alkW2, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons and phylogenetic analysis, quantitative RT-PCR expression analysis
genes alkB1, alkB2, p450 and almA, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons and phylogenetic analysis, one copy of alkB1 in the B-5 chromosome. Expression of genes alkB1, alkB2, p450 and almA in Pseudomonas putida GPo12 pGEc47DELTAB or Pseudomonas fluorescens KOB2DELTA1, quantitative real-time RT-PCR expression analysis
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recombinant expression of His6-tagged enzyme system components in Escherichia coli strain BL21(DE3)
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the 1.4 kb putative promoter region upstream of the predicted CYP86A1 start codon fused in frame to the beta-glucuronidase gene and used to transform wild-type Arabidopsis under the control of the native promoter. Transgenic expression of CYP86A1 fused to GFP, CYP86A1:GFP heterologously and transiently expressed under the control of the CaMV35S-promoter in the epidermis of Nicotiana benthamiana leaves