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Literature summary for 1.14.11.29 extracted from

  • Pappalardi, M.B.; McNulty, D.E.; Martin, J.D.; Fisher, K.E.; Jiang, Y.; Burns, M.C.; Zhao, H.; Ho, T.; Sweitzer, S.; Schwartz, B.; Annan, R.S.; Copeland, R.A.; Tummino, P.J.; Luo, L.
    Biochemical characterization of human HIF hydroxylases using HIF protein substrates that contain all three hydroxylation sites (2011), Biochem. J., 436, 363-369.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ascorbate
-
Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expression of N-terminally MBP-tagged PHD3 in Escherichia coli strain BL21(DE3)pRR692 Homo sapiens
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 Homo sapiens
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 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetic analysis and substrate selectivity for hypoxia-inducible factor and 2-oxoglutarate Homo sapiens
0.000016
-
hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-L-proline pH 7.5, 25°C, PHD3 Homo sapiens
0.00075 0.00094 hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-L-proline pH 7.5, 25°C, PHD2 Homo sapiens
0.0047 0.023 hypoxia-inducible factor2alpha C-terminal oxygen-dependent degradation domain-L-proline pH 7.5, 25°C, PHD3 Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ dependent on Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 Homo sapiens
-
hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 Homo sapiens HIF1alpha is a better substrate than HIF2alpha for PHD2 hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q96KS0 isozyme PHD1
-
Homo sapiens Q9GZT9 isozyme PHD2
-
Homo sapiens Q9H6Z9 isozyme PHD3
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His- and Strep-tagged tobacco etch virus-PHD1 from Escherichia coli strain BL21(DE3)pRR692 by nickel affinity and avidin affinity chromatography Homo sapiens
recombinant His- and Strep-tagged tobacco etch virus-PHD2 from Escherichia coli strain BL21(DE3)pRR692 by nickel affinity and avidin affinity chromatography Homo sapiens
recombinant N-terminally MBP-tagged PHD3 from Escherichia coli strain BL21(DE3)pRR692 by amylosse affinity chromatography Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
-
Homo sapiens hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 HIF1alpha is a better substrate than HIF2alpha for PHD2 Homo sapiens hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 differential regulation of HIF1alpha and HIF2alpha at the N-terminal oxygen-dependent degradation domain site by PHD2 Homo sapiens hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 the HIF1alpha C-terminal oxygen-dependent degradation domain is highly preferred for hydroxylation, no N-terminal oxygen-dependent degradation domain hydroxylation for both HIF2alpha and HIF1alpha Homo sapiens hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 the PHD1 reaction at the N-terminal oxygen-dependent degradation domain site shows low level hydroxylation Homo sapiens hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
?
hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2
-
Homo sapiens hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
-
?
hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2 low activity Homo sapiens hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
-
?
hypoxia-inducible factor1alpha N-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2
-
Homo sapiens hypoxia-inducible factor1alpha N-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
-
?
hypoxia-inducible factor1alpha N-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2 low activity Homo sapiens hypoxia-inducible factor1alpha N-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
-
?
hypoxia-inducible factor2alpha C-terminal oxygen dependent degradation domain-L-proline + 2-oxoglutarate + O2
-
Homo sapiens hypoxia-inducible factor2alpha C-terminal oxygen dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
-
?
hypoxia-inducible factor2alpha C-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2
-
Homo sapiens hypoxia-inducible factor2alpha C-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
-
?
hypoxia-inducible factor2alpha N-terminal oxygen dependent degradation domain-L-proline + 2-oxoglutarate + O2
-
Homo sapiens hypoxia-inducible factor2alpha N-terminal oxygen dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
-
?
additional information the substrate contains a C-terminal and a N-terminal oxygen-dependent degradation domain, as well as a C-terminal transactivation domain Homo sapiens ?
-
?
additional information the subtrate contains a C-terminal and a N-terminal oxygen-dependent degradation domain, as well as a C-terminal transactivation domain Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
HIF hydroxylase
-
Homo sapiens
PHD1
-
Homo sapiens
PHD2
-
Homo sapiens
PHD3
-
Homo sapiens
prolyl hydroxylase domain
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0005
-
hypoxia-inducible factor2alpha C-terminal oxygen-dependent degradation domain-L-proline pH 7.5, 25°C, PHD3 Homo sapiens
0.0012
-
hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-L-proline pH 7.5, 25°C, PHD3 Homo sapiens
0.0032
-
hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-L-proline pH 7.5, 25°C, PHD2 Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Homo sapiens

General Information

General Information Comment Organism
evolution the enzyme belongs to the of the 2-oxoglutarate- and iron-dependent dioxygenase family of enzymes Homo sapiens
physiological function the prolyl hydroxylases control the abundance of hypoxia-inducible factor through oxygen-dependent hydroxylation of specific proline residues in hypoxia-inducible factor proteins, triggering subsequent ubiquitination and proteasomal degradation Homo sapiens
physiological function the prolyl hydroxylases control the abundance of hypoxia-inducible factor through oxygen-dependent hydroxylation of specific proline residues in hypoxia-inducible factor proteins, triggering subsequent ubiquitination and proteasomal degradation. Differential regulation of HIF1alpha and HIF2alpha at the NODDD site by PHD2 Homo sapiens