Information on EC 1.14.11.18 - phytanoyl-CoA dioxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.11.18
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RECOMMENDED NAME
GeneOntology No.
phytanoyl-CoA dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phytanoyl-CoA + 2-oxoglutarate + O2 = 2-hydroxyphytanoyl-CoA + succinate + CO2
show the reaction diagram
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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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SYSTEMATIC NAME
IUBMB Comments
phytanoyl-CoA, 2-oxoglutarate:oxygen oxidoreductase (2-hydroxylating)
Part of the peroxisomal phytanic acid alpha-oxidation pathway. Requires Fe2+ and ascorbate.
CAS REGISTRY NUMBER
COMMENTARY hide
185402-46-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
26 T4-like myoviruses, including 10 from non-cyanobacterial myoviruses and 16 from marine cyanobacterial myoviruses, isolated from Prochlorococcus sp. and Synechococcus sp.
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Manually annotated by BRENDA team
mouse
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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role of 2-oxoglutarate during cyanophage infection, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3,7-dimethyloctan-6-enoyl-CoA + 2-oxoglutarate + O2
3,7-dimethyl-2-hydroxyocta-7-enoyl-CoA + succinate + CO2
show the reaction diagram
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75.2 of the activity with 3-methylhexadecanoyl-CoA
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?
3-ethylnonanoyl-CoA + 2-oxoglutarate + O2
3-ethoxy-2-hydroxyhexadecanoyl-CoA + succinate + CO2
show the reaction diagram
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64.7% of the activity with 3-methylhexadecanoyl-CoA
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?
3-methyl-5-phenyl-pentanoyl-CoA + 2-oxoglutarate + O2
2-hydroxy-3-methyl-5-phenylpentanoyl-CoA + succinate + CO2
show the reaction diagram
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53% of the activity with 3-methylhexadecanoyl-CoA
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?
3-methyldodecanoyl-CoA + 2-oxoglutarate + O2
2-hydroxy-3-methyldodecanoyl-CoA + succinate + CO2
show the reaction diagram
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110% of the activity with 3-methylhexadecanoyl-CoA
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?
3-methylheptanoyl-CoA + 2-oxoglutarate + O2
2-hydroxy-3-methylheptanoyl-CoA + succinate + CO2
show the reaction diagram
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16.2% of the activity with 3-methylhexadecanoyl-CoA
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?
3-methylhexadecanoyl-CoA + 2-oxoglutarate + O2
2-hydroxy-3-methylhexadecanoyl-CoA + succinate + CO2
show the reaction diagram
3-methylnonanoyl-CoA + 2-oxoglutarate + O2
2-hydroxy-3-methylnonanoyl-CoA + succinate + CO2
show the reaction diagram
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111% of the activity with 3-methylhexadecanoyl-CoA
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?
3-methylundecanoyl-CoA + 2-oxoglutarate + O2
2-hydroxy-3-methylundecanoyl-CoA + succinate + CO2
show the reaction diagram
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110% of the activity with 3-methylhexadecanoyl-CoA
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?
butanoyl-CoA + 2-oxoglutarate + O2
2-hydroxybutanoyl-CoA + succinate + CO2
show the reaction diagram
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?
decanoyl-CoA + 2-oxoglutarate + O2
2-hydroxydecanoyl-CoA + succinate + CO2
show the reaction diagram
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?
dodecanoyl-CoA + 2-oxoglutarate + O2
2-hydroxydodecanoyl-CoA + succinate + CO2
show the reaction diagram
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?
hexadecanoyl-CoA + 2-oxoglutarate + O2
2-hydroxyhexadecanoyl-CoA + succinate + CO2
show the reaction diagram
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?
hexanoyl-CoA + 2-oxoglutarate + O2
2-hydroxyhexanoyl-CoA + succinate + CO2
show the reaction diagram
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?
isovaleryl-CoA + 2-oxoglutarate + O2
?
show the reaction diagram
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?
octadecanoyl-CoA + 2-oxoglutarate + O2
2-hydroxyoctadecanoyl-CoA + succinate + CO2
show the reaction diagram
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?
octanoyl-CoA + 2-oxoglutarate + O2
2-hydroxyoctanoyl-CoA + succinate + CO2
show the reaction diagram
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?
phytanoyl-CoA + 2-oxoglutarate
2-hydroxyphytanoyl-CoA + succinate + CO2
show the reaction diagram
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ir
phytanoyl-CoA + 2-oxoglutarate + O2
2-hydroxyphytanoyl-CoA + succinate + CO2
show the reaction diagram
phytanoyl-CoA + 2-oxoglutarate + O2
alpha-hydroxyphytanoyl-CoA + succinate + CO2
show the reaction diagram
tetradecanoyl-CoA + 2-oxoglutarate + O2
2-hydroxytetradecanoyl-CoA + succinate + CO2
show the reaction diagram
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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
phytanoyl-CoA + 2-oxoglutarate + O2
2-hydroxyphytanoyl-CoA + succinate + CO2
show the reaction diagram
O14832
Refsum‘s disease ia a neurological syndrome characterized by adult-onset retinitis pigmentosa, anosemia, sensory neuropathy and phytanic acidaemia. Many cases are caused by mutations in peroxidomal oxygenase phytanoyl-CoA 2-hydroxylase
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?
additional information
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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UTP, CTP, ITP, AMP, ADP, NAD+ and FAD can not act as cofactors, ATP and GTP can be replaced by adenosine-5'-O-(3-thiotriphosphate), adenylylimidodiphosphate, adenylyl-(beta,gamma-methylene)-diphosphonate and guanylyl-imidodiphosphate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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Cu2+, Mn2+ or Zn2+ can not replace Fe2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-methylhexadecanoyl-CoA
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56% of control activity
ATP
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at 0.1 mM Fe2+ 4 mM ATP inhibits enzyme activity. At increased Fe2+ concentrations ATP stimulates with a maximum at 64 mM ATP for 1.0 mM Fe2+
GTP
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at 0.1 mM Fe2+ 4 mM ATP inhibits enzyme activity. At increased Fe2+ concentrations ATP stimulates with a maximum at 64 mM ATP for 1.0 mM Fe2+
hexadecanoyl-CoA
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74% of control activity
propyl gallate
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no activity with 1 mM, interacts with iron binding
additional information
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not inhibited by bifonazole, clotrimazole, miconazole, ketoconazole
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-hydroxyphytanoyl-CoA
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albumin
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0.05 mM 3-methylhexadecanoyl-CoA, no hydroxylation in absence of albumin. Hydroxylation of 3-methylnonanoyl-CoA or 3-methyldodecanoyl-CoA is much less dependent on the presence of albumin
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ascorbate
ATP
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at 0.1 mM Fe2+ 4 mM ATP inhibits enzyme activity. At increased Fe2+ concentrations ATP stimulates with a maximum at 64 mM ATP for 1.0 mM Fe2+
GTP
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at 0.1 mM Fe2+ 4 mM GTP inhibits enzyme activity. At increased Fe2+ concentrations ATP stimulates with a maximum at 64 mM GTP for 1.0 mM Fe2+
imidazole
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at 0.1 mM Fe2+ 4 mM ATP inhibits enzyme activity. At increased Fe2+ concentrations ATP stimulates with a maximum at 64 mM ATP for 1.0 mM Fe2+; stimulates at 1.0 mM Fe2+
SCP-2
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phytanoylis efficiently 2-hydroxylated by PAHX in vitro in the presence of mature SCO-2. SCP-2 increases discrimination between straight-chain and branched-chain substrates, i.e. it decreases activity with straight chain substrates and increase activity with branched-chain substrates. In vivo substrates for PAHX may be SCP-2 complexes
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.049
2-oxoglutarate
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0.0408
3-methylhexadecanoyl-CoA
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000001
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in kidney cell line COS-1, activity can be induced 4fold by phytanic acid
0.0000018
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in embryonic carcinoma cell line P19-EC, activity can be induced 4fold by phytanic acid
0.000002
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in kidney cell line 293, activity can be induced 4fold by phytanic acid
0.0000022
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in fibroblast homogenate
0.0000031
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in hepatoma cell line HepG2, no induction by phytanic acid
0.000024
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in hepatoma cell line FaO, activity can be induced 2.5fold by phytanic acid
0.000041
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in liver homogenate
0.0001
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in purified peroxisomes
0.00026
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in purified liver peroxisomes
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
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at pH 6.5 over 80%, at pH 8.5 50% of control activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
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purified protein, SDS-PAGE
35000
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purified protein, SDS-PAGE
35400
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mature protein after cleavage of presumed leader sequence, calculation from cDNA sequence
35440
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calculated from amino acid sequence without N-terminal methionine
38600
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calculated from amino acid sequence
41200
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precursor protein with peroxisomal targeting signal type 2, calculation from cDNA sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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unprocessed proenzyme contains a N-terminal peroxisomal targeting sequence that is cleaved to give mature PAHX. Both forms are able to hydroxylate a range of CoA derivatives, but under the same assay conditions, the N-terminal Hexa-His-tagged unprocessed form is less active than the nontagged mature form
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method in 21% polyethylene glycol 3350, 0.3 M triammonium citrate, pH 7.1, at 18°C
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
carboxymethyl-Sepharose cation exchange chromatography and Superdex S75 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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in bacterial expression vector pMALc2
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in bacterial expression vector pQE-31
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in mammalian expression vector pcDNA3
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in yeast expression vector
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in yeast expression vector pEL26 and pEL30
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T4-like cyanopohage, marine cyanobacterial and non-cyanobacterial, genotyping, overview
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wild-type and mutant enzymes, expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E197Q
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disruption of the 2-oxoglutarate binding pocket
F275S
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places a polar side chain in a hydrophobic pocket and possibly interferes with the overall structure or impair protein folding
H213A
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insoluble mutant enzyme
H259A
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mutation removes two of the hydrogen bonds and probably destabilizes the beta-turn, which in turn destabilizes the core double stranded beta-helix
H264A
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activity with phytanoyl-CoA is 7.5 of the wild-type activity
I199F
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disruption of the 2-oxoglutarate binding pocket
N83Y
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disruption of protein-protein interactions proposed to involve PAHX, such as that with sterol carrier protein-2, proposed to be responsible for solubilization and presentation of phytanoyl-CoA to PAHX
P29S
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clinically observed mutant is fully active, mutation may result in a defective targeting of the protein to peroxisomes
Q176A
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activity with phytanoyl-CoA is 16.3% of the wild-type activity
Q176K
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mutation causes partial uncoupling of 2-oxoglutarate conversion from phytanoyl-CoA oxidation
R245Q
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disruption of protein-protein interactions proposed to involve PAHX, such as that with sterol carrier protein-2, proposed to be responsible for solubilization and presentation of phytanoyl-CoA to PAHX
W193R
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disruption of the 2-oxoglutarate binding pocket
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
medicine
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treatment of Refsum disease