Information on EC 1.14.13.151 - linalool 8-monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.151
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RECOMMENDED NAME
GeneOntology No.
linalool 8-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(6E)-8-hydroxylinalool + NADH + H+ + O2 = (6E)-8-oxolinalool + NAD+ + 2 H2O
show the reaction diagram
1b
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linalool + 2 NADH + 2 H+ + 2 O2 = (6E)-8-oxolinalool + 2 NAD+ + 3 H2O
show the reaction diagram
linalool + NADH + H+ + O2 = (6E)-8-hydroxylinalool + NAD+ + H2O
show the reaction diagram
1a
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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Monoterpenoid biosynthesis
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
95329-13-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
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
(6E)-8-hydroxylinalool + NADH + H+ + O2
(6E)-8-oxolinalool + NAD+ + 2 H2O
show the reaction diagram
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product analysis by mass spectrometry
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?
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + NADH + O2
8-oxolinalool + NAD+ + H2O
show the reaction diagram
3,7-dimethylocta-1,6-dien-3-ol + NADH + O2
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + NAD+ + H2O
show the reaction diagram
3,7-dimethylocta-1,6-dien-3-ol + NADH + O2
?
show the reaction diagram
6-methyl-hex-5-en-2-ol + NAD+
6-methyl-hex-5-en-2-one + NADH
show the reaction diagram
linalool + 2 NADH + 2 H+ + 2 O2
(6E)-8-oxolinalool + 2 NAD+ + 3 H2O
show the reaction diagram
linalool + NADH + H+ + O2
(6E)-8-hydroxylinalool + NAD+ + H2O
show the reaction diagram
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product analysis by mass spectrometry
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?
additional information
?
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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
3,7-dimethylocta-1,6-dien-3-ol + NADH + O2
?
show the reaction diagram
linalool + 2 NADH + 2 H+ + 2 O2
(6E)-8-oxolinalool + 2 NAD+ + 3 H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
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redoxin
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an Fe2/S2/Cys4 protein
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CO
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complete inhibition; complete inhibition of the oxidation reactions
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 43
NADH
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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0042
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reductase
0.014
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purified enzyme, pH 7.4, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.65
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sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43700
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1 * 44000, SDS-PAGE, 1 * 43700, about, sequence calculation
44000
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1 * 44000, SDS-PAGE, 1 * 43700, about, sequence calculation
45000
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gel filtration
additional information
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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
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Show AA Sequence (257 entries)
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