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Literature summary extracted from

  • Hewitson, K.S.; McNeill, L.A.; Riordan, M.V.; Tian, Y.M.; Bullock, A.N.; Welford, R.W.; Elkins, J.M.; Oldham, N.J.; Bhattacharya, S.; Gleadle, J.M.; Ratcliffe, P.J.; Pugh, C.W.; Schofield, C.J.
    Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family (2002), J. Biol. Chem., 277, 26351-26355.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.11.30
-
 Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.11.30 Co2+
-
 Homo sapiens
1.14.11.30 additional information inhibited by limited hypoxia Homo sapiens
1.14.11.30 N-oxaloylglycine
-
 Homo sapiens
1.14.11.30 Zn2+
-
 Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.11.30 0.01
-
 2-oxoglutarate pH 7.4, 37°C Homo sapiens
1.14.11.30 0.01
-
 PSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN pH 7.4, 37°C Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.11.30 Fe2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.11.30 hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 Homo sapiens activity of the hypoxia-inducible factor (HIF) complex is controlled by oxygen-dependent hydroxylation of prolyl and asparaginyl residues. Hydroxylation of specific prolyl residues by 2-oxoglutarate-dependent oxygenases mediates ubiquitinylation and proteasomal destruction of HIF-alpha. Hydroxylation of an asparagine residue (ASn803) in the C-terminal transactivation domain of HIF-alpha abrogates interaction with p300, preventing transcriptional activation hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.30 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.11.30
-
 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.30 hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 activity of the hypoxia-inducible factor (HIF) complex is controlled by oxygen-dependent hydroxylation of prolyl and asparaginyl residues. Hydroxylation of specific prolyl residues by 2-oxoglutarate-dependent oxygenases mediates ubiquitinylation and proteasomal destruction of HIF-alpha. Hydroxylation of an asparagine residue (ASn803) in the C-terminal transactivation domain of HIF-alpha abrogates interaction with p300, preventing transcriptional activation Homo sapiens hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2
-
 ?
1.14.11.30 hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 the oxygen in the alcohol of the hydroxyasparagine residue is directly derived from dioxygen Homo sapiens hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2
-
 ?
1.14.11.30 PSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN + 2-oxoglutarate + O2 hypoxia-inducible factor-1alpha peptide 775-826. Mutation of Asn803 in GST-HIF-1alpha-(775–826) to alanine, glutamine or glutamate abolishes activity, while an Asp803 mutant still supports some 2-oxoglutarate turnover, at a maximum of 7% of the analogous Asn-803 substrate Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.11.30 factor inhibiting HIF
-
 Homo sapiens
1.14.11.30 HIF asparagine hydroxylase
-
 Homo sapiens
1.14.11.30 HIF asparaginyl hydroxylase
-
 Homo sapiens
1.14.11.30 hypoxia-inducible factor asparagine hydroxylase
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.11.30 37
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.11.30 7.4
-
 assay at Homo sapiens

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.14.11.30 0.01
-
-
 Homo sapiens Zn2+
1.14.11.30 0.01
-
-
 Homo sapiens Co2+
1.14.11.30 0.025
-
-
 Homo sapiens N-oxaloylglycine