Information on EC 1.14.16.5 - alkylglycerol monooxygenase and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC1.14.16.5
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Homo sapiens


The taxonomic range for the selected organisms is: Homo sapiens

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.16.5
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RECOMMENDED NAME
GeneOntology No.
alkylglycerol monooxygenase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
-
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redox reaction
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-
-
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reduction
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-
-
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SYSTEMATIC NAME
IUBMB Comments
1-alkyl-sn-glycerol,tetrahydrobiopterin:oxygen oxidoreductase
The enzyme cleaves alkylglycerols, but does not cleave alkenylglycerols (plasmalogens). Requires non-heme iron [7], reduced glutathione and phospholipids for full activity. The product spontaneously breaks down to form a fatty aldehyde and glycerol.
CAS REGISTRY NUMBER
COMMENTARY hide
37256-82-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-O-pyrenedecyl-sn-glycerol + tetrahydrobiopterin + O2
? + dihydrobiopterin + H2O
show the reaction diagram
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-
-
-
?
1-O-pyrenedecyl-sn-glycerol + tetrahydrobiopterin + O2
glycerol + pyrenedecanal + 6,7[8H]-dihydrobiopterin + H2O
show the reaction diagram
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-
-
-
?
alkylglycerol + tetrahydrobiopterin + O2
glycerol + fatty aldehyde + 6,7[8H]-dihydrobiopterin + H2O
show the reaction diagram
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after rapid decay of the resulting unstable primary product (hemiacetal)
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tetrahydrobiopterin
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dependent on
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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Phenanthroline
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competitive inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011
1-O-pyrenedecyl-sn-glycerol
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measured in CHO cells after transfection, pH not specified in the publication, 37C
0.00183 - 0.0335
tetrahydrobiopterin
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00139
1,10-phenanthroline
Homo sapiens
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pH not specified in the publication, temperature not specified in the publication
0.00069 - 0.00341
Phenanthroline
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
-
x * 60000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 60000, SDS-PAGE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in CHO cell, expressed in Xenopus laevis oocyte, GFP fusion protein expressed in CHO cell, 6x myc tag version expressed in CHO-K1 cell
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expressed in CHO-K1 cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C231A
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the mutant enzyme activity is not significantly different from wild type
C397A
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the mutant enzyme activity is not significantly different from wild type
D153A
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the mutant enzyme activity is not significantly different from wild type
D384A
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the mutant has significantly reduced, but clearly detectable, enzyme activity
E137A
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the mutation leads to an 18fold increase in the Michaelis-Menten constant for tetrahydrobiopterin. The mutant has an approximately 5fold lower affinity for iron
E152A
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the mutant has significantly reduced, but clearly detectable, enzyme activity
E203A
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the mutant has significantly reduced, but clearly detectable, enzyme activity
E212A
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the mutant has significantly reduced, but clearly detectable, enzyme activity
H189A
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the mutant has significantly reduced, but clearly detectable, enzyme activity
H220A
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the mutant enzyme activity is not significantly different from wild type
Q146A
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the mutant enzyme activity is not significantly different from wild type
Q166A
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the mutant has significantly reduced, but clearly detectable, enzyme activity
Q191A
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the mutant has significantly reduced, but clearly detectable, enzyme activity
Q197A
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the mutant has activity of less than 5% of that of the wild type
R396A
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the mutant has significantly reduced, but clearly detectable, enzyme activity
Y174A
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the mutant has significantly reduced, but clearly detectable, enzyme activity
Y230A
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the mutant enzyme activity is not significantly different from wild type
Y338A
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the mutant has activity of less than 5% of that of the wild type
additional information
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mutation of each of 8 conserved His residues (to alanine) which are all essential for activity