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Enzyme Nomenclature
Information on EC 1.14.13.151 - linalool 8-monooxygenase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.13.151
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RECOMMENDED NAME
GeneOntology No.
linalool 8-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(6E)-8-hydroxylinalool + NADH + H+ + O2 = (6E)-8-oxolinalool + NAD+ + 2 H2O
1b
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-
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linalool + NADH + H+ + O2 = (6E)-8-hydroxylinalool + NAD+ + H2O
1a
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-
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linalool + 2 NADH + 2 H+ + 2 O2 = (6E)-8-oxolinalool + 2 NAD+ + 3 H2O
overall reaction
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-
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linalool + 2 NADH + 2 H+ + 2 O2 = (6E)-8-oxolinalool + 2 NAD+ + 3 H2O
mixed function monooxygenase consisting of LIN-reductase, Fe2S2-redoxin and cytochrome LIN P-450
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linalool + 2 NADH + 2 H+ + 2 O2 = (6E)-8-oxolinalool + 2 NAD+ + 3 H2O
mixed function monooxygenase consisting of LIN-reductase, Fe2S2-redoxin and cytochrome LIN P-450
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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-
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reduction
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
linalool,NADH:oxygen oxidoreductase (8-hydroxylating)
A heme-thiolate protein (P-450). The secondary electron donor is a specific [2Fe-2S] ferredoxin from the same bacterial strain.
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CAS REGISTRY NUMBER
COMMENTARY
95329-13-8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
evolution
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the enzyme belongs to the CYP111 family of heme-dependent cytochrome P450 monooxygenases
evolution
P45O1in is a member of the CYPIll P-450 monooxygenase gene family
evolution
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the enzyme belongs to the CYP111 family of heme-dependent cytochrome P450 monooxygenases
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evolution
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P45O1in is a member of the CYPIll P-450 monooxygenase gene family
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metabolism
P-4501in catalyzes the 8-methyl hydroxylation of linalool as the first committed step of its utilization by Pseudomonas putida as the sole carbon source
metabolism
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P-4501in catalyzes the 8-methyl hydroxylation of linalool as the first committed step of its utilization by Pseudomonas putida as the sole carbon source; the enzyme catalyzes the first step in linalool catabolism
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additional information
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analysis of the heme-thiolate reaction center, molecular domains of substrate specificity, redox-pair interactions, and the regulation of the reaction cycle, overview
additional information
P-4501in exhibits conservation in the axial cysteine heme ligand-containing peptide and the threonine region postulated to form an 02-binding pocket
additional information
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analysis of the heme-thiolate reaction center, molecular domains of substrate specificity, redox-pair interactions, and the regulation of the reaction cycle, overview; P-4501in exhibits conservation in the axial cysteine heme ligand-containing peptide and the threonine region postulated to form an 02-binding pocket
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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
(6E)-8-hydroxylinalool + NADH + H+ + O2
(6E)-8-oxolinalool + NAD+ + 2 H2O
-
-
product analysis by mass spectrometry
-
?
3,7-dimethylocta-1,6-dien-3-ol + NADH + O2
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + NAD+ + H2O
linalool + NADH + H+ + O2
(6E)-8-hydroxylinalool + NAD+ + H2O
-
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product analysis by mass spectrometry
-
?
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + NADH + O2
8-oxolinalool + NAD+ + H2O
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8-hydroxylinalool
-
?
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + NADH + O2
8-oxolinalool + NAD+ + H2O
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8-hydroxylinalool
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?
3,7-dimethylocta-1,6-dien-3-ol + NADH + O2
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + NAD+ + H2O
-
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8-hydroxylinalool
?
3,7-dimethylocta-1,6-dien-3-ol + NADH + O2
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + NAD+ + H2O
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both isomers of linalool, strict substrate specificity: geraniol, nerol or citronellol are not hydroxylated
-
?
3,7-dimethylocta-1,6-dien-3-ol + NADH + O2
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + NAD+ + H2O
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both isomers of linalool, strict substrate specificity: geraniol, nerol or citronellol are not hydroxylated
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?
3,7-dimethylocta-1,6-dien-3-ol + NADH + O2
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + NAD+ + H2O
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8-hydroxylinalool
?
3,7-dimethylocta-1,6-dien-3-ol + NADH + O2
?
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linalool, initial reaction in linalool catabolism
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-
?
3,7-dimethylocta-1,6-dien-3-ol + NADH + O2
?
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linalool, initial reaction in linalool catabolism
-
-
?
6-methyl-hex-5-en-2-ol + NAD+
6-methyl-hex-5-en-2-one + NADH
-
-
-
-
ir
linalool + 2 NADH + 2 H+ + 2 O2
(6E)-8-oxolinalool + 2 NAD+ + 3 H2O
-
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NMR spectroscopy product analysis
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?
linalool + 2 NADH + 2 H+ + 2 O2
(6E)-8-oxolinalool + 2 NAD+ + 3 H2O
-
-
-
-
?
linalool + 2 NADH + 2 H+ + 2 O2
(6E)-8-oxolinalool + 2 NAD+ + 3 H2O
-
-
-
-
?
linalool + 2 NADH + 2 H+ + 2 O2
(6E)-8-oxolinalool + 2 NAD+ + 3 H2O
-
-
-
?
linalool + 2 NADH + 2 H+ + 2 O2
(6E)-8-oxolinalool + 2 NAD+ + 3 H2O
-
overall reaction
product analysis by mass spectrometry
-
?
linalool + 2 NADH + 2 H+ + 2 O2
(6E)-8-oxolinalool + 2 NAD+ + 3 H2O
-
-
-
-
?
linalool + 2 NADH + 2 H+ + 2 O2
(6E)-8-oxolinalool + 2 NAD+ + 3 H2O
-
-
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?
additional information
?
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overview: synthetic analogues of linalool
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additional information
?
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the enzyme does not perform 10-methyl hydroxylation of linalool
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additional information
?
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overview: synthetic analogues of linalool
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additional information
?
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the enzyme does not perform 10-methyl hydroxylation of linalool
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
3,7-dimethylocta-1,6-dien-3-ol + NADH + O2
?
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linalool, initial reaction in linalool catabolism
-
-
?
3,7-dimethylocta-1,6-dien-3-ol + NADH + O2
?
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linalool, initial reaction in linalool catabolism
-
-
?
linalool + 2 NADH + 2 H+ + 2 O2
(6E)-8-oxolinalool + 2 NAD+ + 3 H2O
-
-
-
-
?
linalool + 2 NADH + 2 H+ + 2 O2
(6E)-8-oxolinalool + 2 NAD+ + 3 H2O
-
-
-
-
?
linalool + 2 NADH + 2 H+ + 2 O2
(6E)-8-oxolinalool + 2 NAD+ + 3 H2O
-
-
-
-
?
linalool + 2 NADH + 2 H+ + 2 O2
(6E)-8-oxolinalool + 2 NAD+ + 3 H2O
Q59723
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-
-
?
linalool + 2 NADH + 2 H+ + 2 O2
(6E)-8-oxolinalool + 2 NAD+ + 3 H2O
-
-
-
-
?
linalool + 2 NADH + 2 H+ + 2 O2
(6E)-8-oxolinalool + 2 NAD+ + 3 H2O
Q59723
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-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
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heme-containing cytochrome P450 enzyme; requirement of two enzyme components, iron-heme protein and iron-sulfur protein
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Pseudomonas putida
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overview: values for cytochrome LIN P-450 with various synthetic substrates
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2
NADH
Pseudomonas putida
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substrate-stimulated NADH oxidation using excess amounts of P-450 and FAD component of the enzyme
32
NADH
Pseudomonas putida
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substrate-stimulated NADH oxidation using excess amounts of iron-sulfur and FAD component of the enzyme
43
NADH
Pseudomonas putida
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substrate-stimulated NADH oxidation using excess amounts of iron sulfur and P-450 component of the enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.014
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purified enzyme, pH 7.4, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
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strain PpG777 utilizes linalool as sole carbon and energy source
additional information
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strain PpG777 utilizes linalool as sole carbon and energy source
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
multi-component enzyme consisting of LIN-reductase, Fe2-S2-redoxin and cytochrome LIN-P450. MW of the reductase: 43700 Da, analytical data from amino acid composition and prosthetic group quantification, 45000 Da, gel filtration. MW of Fe2-S2-redoxin: 11000 Da, gel filtration, 12800 Da, analytical data from amino acid composition and prosthetic group quantification. MW of cytochrome LIN-P450: 44800 Da, analytical data from amino acid composition and prosthetic group quantification, 45000 Da, gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
-
enzyme consists of LIN-reductase, MW 44000 Da, and Fe2S2-redoxin, MW 10700 Da, and cytochrome LIN-P450, MW 47000 Da, SDS-PAGE
additional information
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enzyme consists of LIN-reductase, MW 44000 Da, and Fe2S2-redoxin, MW 10700 Da, and cytochrome LIN-P450, MW 47000 Da, SDS-PAGE
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-196°C, LIN-redoxin reductase and cytochrome LINP-450 in solution stable over a long period after ultrafiltration or dialysis and repeated freeze/thaw-cycles
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0°C, LIN-redoxin loses its prosthetic group, 5 mM DTT retards apoprotein formation
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme by anion exchange chromatography, ammonium sulfate fractionation, a second step of anion exchange chromatography, affinity chromatography, a thrid step of anion exchange chromatography, and two further different steps of affinity chromatography to over 90% hommogeneity; purification of 3 enzyme components: iron-sulphur, FAD and P-450
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recombinant enzyme from Escherichia coli by anion exchange chromatography, ammonium sulfate fractionation, gel filtration, and a second step of anion exchange chromatography
recombinant enzyme from Escherichia coli by ultrafiltration and anion exchange chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CYP111A2 cloning, expression in Escherichia coli strain DH5alpha
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gene linC, DNA and amino acid sequence determination and analysis, constitutive functional expression in Escherichia coli from plasmid pUC18 under control of the lac promoter
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
interaction and coupling of CYP enzyme reactions from Novosphingobium aromaticivorans with ferredoxin reductases ArR from Novosphingobium aromaticivorans and PdR from from Rhodopseudomonas palustris CGA009, activity reconstitution with the electron transfer system of ArR and Arx, overview
additional information
-
interaction and coupling of CYP enzyme reactions from Novosphingobium aromaticivorans with ferredoxin reductases ArR from Novosphingobium aromaticivorans and PdR from from Rhodopseudomonas palustris CGA009, activity reconstitution with the electron transfer system of ArR and Arx, overview
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.151)
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