Information on EC 1.14.11.29 - hypoxia-inducible factor-proline dioxygenase

New: Word Map on EC 1.14.11.29
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Coelomata

EC NUMBER
COMMENTARY hide
1.14.11.29
-
RECOMMENDED NAME
GeneOntology No.
hypoxia-inducible factor-proline dioxygenase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 = hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
hypoxia-inducible factor-L-proline, 2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating)
Contains iron, and requires ascorbate. Specifically hydroxylates a proline residue in HIF-alpha, the alpha subunit of the transcriptional regulator HIF (hypoxia-inducible factor), which targets HIF for proteasomal destruction. The requirement of oxygen for the hydroxylation reaction enables animals to respond to hypoxia.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
-
silencing FIH, EC 1.14.11.30, under conditions where prolyl hydroxylase, is inhibited results in increased HIF-1alpha transcriptional activity, but paradoxically decreases HIF-1alpha stability
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
DALDLEMLAPYISMDDDFQL + 2-oxoglutarate + O2
?
show the reaction diagram
a HIF-3alpha peptide. Vmax is 120% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DALDLEMLAPYISMDDDFQL + 2-oxoglutarate + O2
DALDLEMLA-((4R)-4-hydroxy-L-proline)-YISMDDDFQL + succinate + CO2
show the reaction diagram
DALTLLAPAAGDTIISLFG + 2-oxoglutarate + O2
DALTLLA-((4R)-4-hydroxy-L-proline)-AAGDTIISLFG + succinate + CO2
show the reaction diagram
DLDLEMLAPAIPMDDDFQL + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-AIPMDDDFQL + succinate + CO2
show the reaction diagram
Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DLDLEMLAPAIPMDDDFQL + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-AIPMDDDFQL succinate + CO2
show the reaction diagram
Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DLDLEMLAPGIPMDDDFQL + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-GIPMDDDFQL + succinate + CO2
show the reaction diagram
Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DLDLEMLAPYIPMD + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMD + succinate + CO2
show the reaction diagram
Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DLDLEMLAPYIPMDD + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDD + succinate + CO2
show the reaction diagram
Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DLDLEMLAPYIPMDDDF + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDF + succinate + CO2
show the reaction diagram
Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DLDLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2
show the reaction diagram
-
-
-
?
DLDLEMLAPYIPMDDDFQLRSFDQ + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQLRSFDQ + succinate + CO2
show the reaction diagram
Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2
show the reaction diagram
Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2
DLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2
show the reaction diagram
Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
EEPDLSCLAPFVDTYDMMQM + 2-oxoglutarate + O2
?
show the reaction diagram
ELDLETLAPYIPMDGEDFQ + 2-oxoglutarate + O2
?
show the reaction diagram
ELDLETLAPYIPMDGEDFQ + 2-oxoglutarate + O2
ELDLETLA-((4R)-4-hydroxy-L-proline)-YIPMDGEDFQ + succinate + CO2
show the reaction diagram
C-terminal hydroxylation site of HIF-2alpha. Vmax is 80% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
EMLAPYIPMDD + 2-oxoglutarate + O2
EMLA-((4R)-4-hydroxy-L-proline)-YIPMDD + succinate + CO2
show the reaction diagram
Vmax is 30% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
EMLAPYIPMDDDFQL + 2-oxoglutarate + O2
EMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2
show the reaction diagram
EPEELAQLAPTPGDAIISLD + 2-oxoglutarate + O2
?
show the reaction diagram
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2
show the reaction diagram
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
show the reaction diagram
hypoxia-inducible factor-L-proline peptide + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline peptide + succinate + CO2
show the reaction diagram
-
peptide substrate is a peptide derived from the natural sequence of HIF-1alpha residues 556-574
hydroxylation at Pro564
-
?
hypoxia-inducible factor-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-(3S)-3-hydroxy-proline + succinate + CO2
show the reaction diagram
-
HIF-1alpha
-
-
?
hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
show the reaction diagram
hypoxia-inducible factor1alpha N-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor1alpha N-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
show the reaction diagram
hypoxia-inducible factor2alpha C-terminal oxygen dependent degradation domain-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor2alpha C-terminal oxygen dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
show the reaction diagram
-
-
-
?
hypoxia-inducible factor2alpha C-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor2alpha C-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
show the reaction diagram
-
-
-
?
hypoxia-inducible factor2alpha N-terminal oxygen dependent degradation domain-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor2alpha N-terminal oxygen dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
show the reaction diagram
-
-
-
?
LAPYIPMDDDFQL + 2-oxoglutarate + O2
LA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2
show the reaction diagram
Vmax is 90% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
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
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2
show the reaction diagram
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
show the reaction diagram
hypoxia-inducible factor-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-(3S)-3-hydroxy-proline + succinate + CO2
show the reaction diagram
-
HIF-1alpha
-
-
?
additional information
?
-
-
HIF prolyl-4-hydroxylase 2 substrate binding analysis using isolated sequences of the C-terminal oxygen degradation domain DLDLEALAP564YIPADDDFQL mutant M561A/M568A, and the N-terminal oxygen degradation domain DALTLLAP402AAGDTIISLDYG mutant F413Y, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,1',1'',1'''-(1,4,7,10-tetraazacyclododecane-1,4,7,10-tetrayl)tetrapropan-2-ol
2,2',2'',2'''-(1,4,7,10-tetraazacyclododecane-1,4,7,10-tetrayl)tetraacetamide
-
chelates Fe2+ in a hexacoordinative mode through four nitrogens of the macrocycle and two oxygens in side arms
2,3-dihydroxypyridine
-
-
2-hydroxypyridine 1-oxide
-
-
3,3'-[(pyridin-2-ylmethyl)imino]dipropanenitrile
-
noncompetitive inhibition
3,3'-[(pyridin-4-ylimino)bis(propane-3,1-diyliminomethanediyl)]diphenol
-
noncompetitive inhibition
3,3'-[(pyridin-4-ylimino)bis[propane-3,1-diylnitrilo(Z)methylylidene]]diphenol
-
noncompetitive inhibition
3,6,9-tris(naphthalen-1-ylmethyl)-3,6,9,15-tetraazabicyclo[9.3.1]pentadeca-1(15),11,13-triene
-
coordinates Fe2+ via triad or tetrad from nitrogen atoms of the parent ring, which leaves vacant position for other ligands binding
3-carboxy-4-oxo-3,4-dihydro-1,10-phenanthroline
-
3-cyano-6-methyl-2(H)-pyridinone
-
-
3-hydroxy-1,2-dimethyl-4(1H)-pyridinone
-
-
3-hydroxy-2-methyl-4-pyrone
-
-
3-hydroxypyridine-2-carbonyl-glycine
-
4-Methylcatechol
-
-
4-nitrocatechol
-
-
4-tert-butylcatechol
-
-
5-hydroxy-2-hydroxymethyl-4-pyrone
-
-
5-hydroxy-4-oxo-4H-pyran-2-carboxylic acid
-
-
Cu2+
-
binding analysis
DLDLEALA-L-3,4-dehydroproline-YIPADDDFQLR
-
-
DLDLEALA-L-4-thioproline-YIPADDDFQLR
-
-
DLDLEALA-L-piperidine-2-carboxylic acid-YIPADDDFQLR
-
-
DLDLEALA-L-trans-4-fluoroproline-YIPADDDFQLR
-
-
DLDLEALA-L-trans-4-hydroxyproline-YIPADDDFQLR
-
-
H2O2
-
poor inhibition. Prolyl hydroxylase is less sensitive to peroxide, preferential inhibition of N803-hydroxylation by FIH, EC 1.14.11.30, compared with inhibition of P402/P564 hydroxylation by PHDs
JNJ1935
-
a prolyl-hydroxylase selective inhibitor. Low concentrations of JNJ1935 selectively inhibit PHDs, whereas higher concentrations inhibit all hydroxylases, including FIH, EC 1.14.11.30, in vitro and in vivo inhibition
N,N-dimethyl-5-[3,6,9,15-tetraazabicyclo[9.3.1]pentadeca-1(15),11,13-trien-6-ylsulfonyl]naphthalen-1-amine
-
coordinates Fe2+ via triad or tetrad from nitrogen atoms of the parent ring, which leaves vacant position for other ligands binding
N-((3-hydroxy-6-chloroquinolin-2-yl)carbonyl)glycine
-
N-(methoxyoxoacetyl)-glycine methyl ester
-
a pan-hydroxylase inhibitor, in vitro and in vivo inhibition
N-oxalyl-(2S)-alanine
-
competed by 2-oxoglutarate, no inhibition by the enantiomer N-oxalyl-(2R)-alanine
N-oxalylglycine
-
competed by 2-oxoglutarate
oxalylglycine
-
oxygen
the transiently overexpressed HPH-1 enzyme is inhibited by a low-oxygen environment
Pyridine-2,4-dicarboxylate
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007 - 0.06
2-oxoglutarate
0.006 - 0.015
DALDLEMLAPYISMDDDFQL
0.13 - 0.38
DALTLLAPAAGDTIISLFG
0.01 - 0.02
DLDLEMLAPAIPMDDDFQL
0.02
DLDLEMLAPGIPMDDDFQL
pH 7.8, 37C; pH 7.8, 37C; pH 7.8, 37C
0.03 - 0.1
DLDLEMLAPYIPMD
0.009 - 0.1
DLDLEMLAPYIPMDD
0.007 - 0.07
DLDLEMLAPYIPMDDDF
0.008
DLDLEMLAPYIPMDDDFQL
pH 7.8, 37C
0.006 - 0.008
DLDLEMLAPYIPMDDDFQLRSFDQ
0.007 - 0.014
DLEMLAPYIPMDDDFQL
0.07 - 0.1
EEPDLSCLAPFVDTYDMMQM
0.011 - 0.03
ELDLETLAPYIPMDGEDFQ
0.05
EMLAPYIPMDD
pH 7.8, 37C
0.007 - 0.08
EMLAPYIPMDDDFQL
0.06 - 0.1
EPEELAQLAPTPGDAIISLD
0.001 - 0.067
hypoxia-inducible factor-L-proline
0.000016 - 0.00094
hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-L-proline
0.0047 - 0.023
hypoxia-inducible factor2alpha C-terminal oxygen-dependent degradation domain-L-proline
pH 7.5, 25C, PHD3
-
0.015
LAPYIPMDDDFQL
pH 7.8, 37C
0.23 - 0.25
O2
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0101 - 0.02
hypoxia-inducible factor-L-proline
0.0012 - 0.0032
hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-L-proline
0.0005
hypoxia-inducible factor2alpha C-terminal oxygen-dependent degradation domain-L-proline
Homo sapiens
Q96KS0, Q9GZT9, Q9H6Z9
pH 7.5, 25C, PHD3
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.72 - 18.8
hypoxia-inducible factor-L-proline
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00628 - 0.067
1,1',1'',1'''-(1,4,7,10-tetraazacyclododecane-1,4,7,10-tetrayl)tetrapropan-2-ol
0.00998
2,2',2'',2'''-(1,4,7,10-tetraazacyclododecane-1,4,7,10-tetrayl)tetraacetamide
-
recombinant enzyme, pH 7.0, 37C
0.0821
3,3'-[(pyridin-2-ylmethyl)imino]dipropanenitrile
-
recombinant enzyme, pH 7.0, 37C
0.0673
3,3'-[(pyridin-4-ylimino)bis(propane-3,1-diyliminomethanediyl)]diphenol
-
recombinant enzyme, pH 7.0, 37C
0.0253
3,3'-[(pyridin-4-ylimino)bis[propane-3,1-diylnitrilo(Z)methylylidene]]diphenol
-
recombinant enzyme, pH 7.0, 37C
0.00191
3,6,9-tris(naphthalen-1-ylmethyl)-3,6,9,15-tetraazabicyclo[9.3.1]pentadeca-1(15),11,13-triene
-
recombinant enzyme, pH 7.0, 37C
0.01 - 0.03
3-carboxy-4-oxo-3,4-dihydro-1,10-phenanthroline
0.001 - 0.015
3-hydroxypyridine-2-carbonyl-glycine
0.00249
N,N-dimethyl-5-[3,6,9,15-tetraazabicyclo[9.3.1]pentadeca-1(15),11,13-trien-6-ylsulfonyl]naphthalen-1-amine
-
recombinant enzyme, pH 7.0, 37C
0.0002 - 0.0008
N-((3-hydroxy-6-chloroquinolin-2-yl)carbonyl)glycine
0.008 - 0.05
oxalylglycine
0.007 - 0.04
Pyridine-2,4-dicarboxylate
additional information
additional information
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0295 - 0.0397
1,1',1'',1'''-(1,4,7,10-tetraazacyclododecane-1,4,7,10-tetrayl)tetrapropan-2-ol
0.0309
2,2',2'',2'''-(1,4,7,10-tetraazacyclododecane-1,4,7,10-tetrayl)tetraacetamide
Homo sapiens
-
recombinant enzyme, pH 7.0, 37C
0.005
2,3-dihydroxypyridine
Homo sapiens
-
pH 7.0, 37C
0.003
2-hydroxypyridine 1-oxide
Homo sapiens
-
pH 7.0, 37C
0.0604
3,3'-[(pyridin-2-ylmethyl)imino]dipropanenitrile
Homo sapiens
-
recombinant enzyme, pH 7.0, 37C
0.0128
3,3'-[(pyridin-4-ylimino)bis(propane-3,1-diyliminomethanediyl)]diphenol
Homo sapiens
-
recombinant enzyme, pH 7.0, 37C
0.016
3,3'-[(pyridin-4-ylimino)bis[propane-3,1-diylnitrilo(Z)methylylidene]]diphenol
Homo sapiens
-
recombinant enzyme, pH 7.0, 37C
0.0103
3,6,9-tris(naphthalen-1-ylmethyl)-3,6,9,15-tetraazabicyclo[9.3.1]pentadeca-1(15),11,13-triene
Homo sapiens
-
recombinant enzyme, pH 7.0, 37C
1
3-cyano-6-methyl-2(H)-pyridinone
Homo sapiens
-
above, pH 7.0, 37C
0.04
3-hydroxy-1,2-dimethyl-4(1H)-pyridinone
Homo sapiens
-
pH 7.0, 37C
1
3-hydroxy-2-methyl-4-pyrone
Homo sapiens
-
above, pH 7.0, 37C
0.004
4-Methylcatechol
Homo sapiens
-
pH 7.0, 37C
0.006
4-nitrocatechol
Homo sapiens
-
pH 7.0, 37C
0.03
4-tert-butylcatechol
Homo sapiens
-
pH 7.0, 37C
0.4
5-hydroxy-2-hydroxymethyl-4-pyrone
Homo sapiens
-
pH 7.0, 37C
0.03
5-hydroxy-4-oxo-4H-pyran-2-carboxylic acid
Homo sapiens
-
pH 7.0, 37C
0.0207
N,N-dimethyl-5-[3,6,9,15-tetraazabicyclo[9.3.1]pentadeca-1(15),11,13-trien-6-ylsulfonyl]naphthalen-1-amine
Homo sapiens
-
recombinant enzyme, pH 7.0, 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at; assay at; assay at
7.8
assay at; assay at; assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at; assay at; assay at
30
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression level of of HIF-P4H-3 mRNA is highest in the adult heart, brain, placenta, lung, and skeletal muscle and in the fetal heart, spleen, and skeletal muscle; the level of HIF-P4H-1 mRNA expression is highest in the adult brain, placenta, lung, and kidney; the levels of HIF-P4H-2 mRNA expression is highest in the adult heart, brain, lung, and liver and in the fetal brain, heart, spleen, and skeletal muscle
Manually annotated by BRENDA team
-
C-terminal domain and N-terminal domain of PDH2
Manually annotated by BRENDA team
expression level of of HIF-P4H-3 mRNA is highest in the adult heart, brain, placenta, lung, and skeletal muscle and in the fetal heart, spleen, and skeletal muscle; the levels of HIF-P4H-2 mRNA expression is highest in the adult heart, brain, lung, and liver and in the fetal brain, heart, spleen, and skeletal muscle
Manually annotated by BRENDA team
the level of HIF-P4H-1 mRNA expression is highest in the adult brain, placenta, lung, and kidney
Manually annotated by BRENDA team
the levels of HIF-P4H-2 mRNA expression is highest in the adult heart, brain, lung, and liver and in the fetal brain, heart, spleen, and skeletal muscle
Manually annotated by BRENDA team
expression level of of HIF-P4H-3 mRNA is highest in the adult heart, brain, placenta, lung, and skeletal muscle and in the fetal heart, spleen, and skeletal muscle; the level of HIF-P4H-1 mRNA expression is highest in the adult brain, placenta, lung, and kidney; the levels of HIF-P4H-2 mRNA expression is highest in the adult heart, brain, lung, and liver and in the fetal brain, heart, spleen, and skeletal muscle
Manually annotated by BRENDA team
expression level of of HIF-P4H-3 mRNA is highest in the adult heart, brain, placenta, lung, and skeletal muscle and in the fetal heart, spleen, and skeletal muscle; the level of HIF-P4H-1 mRNA expression is highest in the adult brain, placenta, lung, and kidney
Manually annotated by BRENDA team
expression level of of HIF-P4H-3 mRNA is highest in the adult heart, brain, placenta, lung, and skeletal muscle and in the fetal heart, spleen, and skeletal muscle; the levels of HIF-P4H-2 mRNA expression is highest in the adult heart, brain, lung, and liver and in the fetal brain, heart, spleen, and skeletal muscle
Manually annotated by BRENDA team
expression level of of HIF-P4H-3 mRNA is highest in the adult heart, brain, placenta, lung, and skeletal muscle and in the fetal heart, spleen, and skeletal muscle; the levels of HIF-P4H-2 mRNA expression is highest in the adult heart, brain, lung, and liver and in the fetal brain, heart, spleen, and skeletal muscle
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 45642, recombinant N-terminally Trx- and C-terminally His-tagged enzyme, mass spectrometry, x * 45651, recombinant His-tagged enzyme, mass spectrometry, x * 45000, recombinant His-tagged enzyme, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged PHD2 by glutathione affinity chromatography
-
recombinant His- and Strep-tagged tobacco etch virus-PHD1 from Escherichia coli strain BL21(DE3)pRR692 by nickel affinity and avidin affinity chromatography; recombinant His- and Strep-tagged tobacco etch virus-PHD2 from Escherichia coli strain BL21(DE3)pRR692 by nickel affinity and avidin affinity chromatography; recombinant N-terminally MBP-tagged PHD3 from Escherichia coli strain BL21(DE3)pRR692 by amylosse affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant N-terminally GST-tagged PHD2 residues 178-426 from Escherichia coli strain L21(DE3) by glutathione affinity chromatography
-
recombinant Trx- and His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography to over 94% purity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Spodoptera frugiperda Sf9 cells and Escherichia coli; expression in Spodoptera frugiperda Sf9 cells and Escherichia coli; expression in Spodoptera frugiperda Sf9 cells and Escherichia coli
expression of His-tagged human PHD3 in Escherichia coli strain BL21(DE3)
-
expression of N-terminally GST-tagged PHD2 residues 178-426 in Escherichia coli strain L21(DE3)
-
expression of N-terminally MBP-tagged PHD3 in Escherichia coli strain BL21(DE3)pRR692; expression of PHD1-(1-407) in Spodoptera frugiperda Sf9 cells using the baculovirus expression vector, expression of His- and Strep-tagged tobacco etch virus-PHD1 in Escherichia coli strain BL21(DE3)pRR692; expression of PHD2-(1-426) in Spodoptera frugiperda Sf9 cells uing the baculovirus expression vector, expression of His- and Strep-tagged tobacco etch virus-PHD2 in Escherichia coli strain BL21(DE3)pRR692
expression of PHD2 catalytic domain residues 177-426, expression of N-terminally GST-tagged PHD2 in Escherichia coli strain BL21(DE3)
-
recombinant expression of GST-tagged PHD2
-
the coding region of human PHD3 DNA is optimized by using synonymous codons according to the code bias of Escherichia coli, expression of soluble and active N-terminally Trx- and C-terminally His-tagged human PHD3 in Escherichia coli strain BL21(DE3)pLysS at lower induction temperature of 25C
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D137A
mutation eliminates prolyl hydroxylase activity of HPH-1
H135A
mutation eliminates prolyl hydroxylase activity of HPH-1
H196A
mutation eliminates prolyl hydroxylase activity of HPH-1
R367K
inactive mutant of HIF-P4H-1
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
the unique function of PHD2 makes it a prime target for selective inhibition leading to regulatory control of diseases such as cancer and stroke