Literature summary for 1.14.11.30 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.

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Activating Compound

Activating Compound	Comment	Organism	Structure
ascorbate	-	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

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-asparagine + 2-oxoglutarate + O2	Homo sapiens	-	hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His- and MBP-tagged FIH from Escherichia coli strain BL21(DE3)pRR692 by nickel affinity and anion exchange chromatography	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2	-	Homo sapiens	hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2	-	?
hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2	HIF1alpha substrate domain structure, overview. Usage of recombinantly expressed HIFalpha proteins spanning the CODDD region, His6-GB1-TEV-HIF1alpha-(498-603) or His6-GB1-TEV-HIF2alpha-(467-575). The enzyme hydroxylates Asn803 of HIF1alpha and Asn847 of HIF2alpha	Homo sapiens	hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + 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 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 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 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
asparaginyl hydroxylase	-	Homo sapiens
factor inhibiting HIF	-	Homo sapiens
FIH	-	Homo sapiens
HIF hydroxylase	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	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 2-oxoglutarate- and iron-dependent dioxygenase family of enzymes	Homo sapiens
physiological function	the enzyme inhibits the hypoxia-inducible factor transcription activation through asparagine hydroxylation	Homo sapiens

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Release 2023.1 (January 2023)