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ankyrin repeat domain of endogenous Notch receptor L-asparagine + 2-oxoglutarate + O2
ankyrin repeat domain of endogenous Notch receptor 3-hydroxy-L-asparagine + succinate + CO2
ankyrin repeat domain protein
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a maximum of three ankyrin repeats enables ankyrin repeat domain proteins as a substrate
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first epidermal growth factor-like domain-L-aspartate + 2-oxoglutarate + O2
first epidermal growth factor-like domain-3-hydroxy-L-aspartate + succinate + CO2
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HIF (L-Asn803) + 2-oxoglutarate + O2
HIF (3-hydroxy-L-Asn803) + succinate + CO2
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accepts HIF-1alpha and HIF-2-alpha as substrate, HIF mutant V802A exhibits 4fold lower substrate activity than native protein, no activity with N803A mutant
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HIF-1alpha peptide Asp788-Leu822 (L-Asn803) + 2-oxoglutarate + O2
HIF-1alpha peptide Asp788-Leu822 (3-hydroxy-L-Asn803) + succinate + CO2
much lower activity with peptides lacking residues 819-822, 807-822, and 815-822
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HIF-1alpha peptide Asp788-Leu822 (L-asparagine803) + 2-oxoglutarate + O2
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peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
peptide-L-aspartate + 2-oxoglutarate + O2
peptide-3-hydroxy-L-aspartate + succinate + CO2
[factor X first EGF-like domain]-L-aspartate + 2-oxoglutarate + O2
[factor X first EGF-like domain]-3-hydroxy-L-aspartate + succinate + CO2
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[thioether-linked cyclic peptide hFX-CP101-119]-L-aspartate + 2-oxoglutarate + O2
[thioether-linked cyclic peptide hFX-CP101-119]-3-hydroxy-L-aspartate + succinate + CO2
the enzyme accepts substrates with a noncanonical EGFD disulfide connectivity (i.e. the Cys 1-2, 3-4, 5-6 disulfide pattern). Stable cyclic thioether analogues of the noncanonical EGFD AspH substrates are developed to avoid disulfide shuffling
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additional information
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ankyrin repeat domain of endogenous Notch receptor L-asparagine + 2-oxoglutarate + O2
ankyrin repeat domain of endogenous Notch receptor 3-hydroxy-L-asparagine + succinate + CO2
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hydroxylation of highly conserved asparaginyl residues within the ankyrin repeat
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ankyrin repeat domain of endogenous Notch receptor L-asparagine + 2-oxoglutarate + O2
ankyrin repeat domain of endogenous Notch receptor 3-hydroxy-L-asparagine + succinate + CO2
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hydroxylation of hyghly conserved asparaginyl residues within the ankyrin repeat
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peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
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peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
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first epidermal growth factor-like domain of human protein S with an asparagine replacing the aspartic acid at position 18
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peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
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peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
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peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
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first epidermal growth factor-like domain of bovine protein S with an asparagine replacing the aspartic acid at position 18
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peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
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enzyme catalyzes the erythro-beta-hydroxylation of asparaginyl and aspartyl residues to form the 2S, 3R-product, possible role in the Notch signalling pathway
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peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
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hydroxylation of Asn803 in hypoxia-inducible transcription factor, converted protein is incapable in interacting with the transcripitonal coactivator p300
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peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
hydroxylation of Asn803 in hypoxia-inducible transcription factor, converted protein is incapable in interacting with the transcripitonal coactivator p300
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peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
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peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
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first epidermal growth factor-like domain of human protein S as substrate
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peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
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first epidermal growth factor-like domain of human protein S as substrate
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peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
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specific erythro-hydroxylation
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peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
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second epidermal growth factor-like domain of bovine protein S
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peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
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first epidermal growth factor-like domain of bovine protein S as substrate
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peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
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hydroxylates epidermal growth factor-like domains in transformation-associated proteins
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peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
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peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
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specific erythro-hydroxylation
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peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
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first epidermal growth factor-like domain of human factor IX as substrate
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peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
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specific erythro-hydroxylation
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peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
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first epidermal growth factor-like domain of human factor IX as substrate
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peptide-L-aspartate + 2-oxoglutarate + O2
peptide-3-hydroxy-L-aspartate + succinate + CO2
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peptide-L-aspartate + 2-oxoglutarate + O2
peptide-3-hydroxy-L-aspartate + succinate + CO2
the enzyme catalyses hydroxylation of asparaginyl- and aspartyl-residues in epidermal growth factor-like domains
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peptide-L-aspartate + 2-oxoglutarate + O2
peptide-3-hydroxy-L-aspartate + succinate + CO2
the enzyme catalyzes the post-translational hydroxylation of Asp and Asn residues in epidermal growth factor-like domains
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peptide-L-aspartate + 2-oxoglutarate + O2
peptide-3-hydroxy-L-aspartate + succinate + CO2
the enzyme accepts epidermal growth factor-like domain (EGFD) substrates with a noncanonical (i. e., Cys 1-2, 3-4, 5-6) disulfide pattern. Synthetic thioether linked cyclic peptide, hFX-CP101-119 is used as substrate. hFX-CP101-119 is designed based on 19 EGFD1 amino acid residues of the sequence of human coagulation factor X (hFX amino acids 101-119)
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peptide-L-aspartate + 2-oxoglutarate + O2
peptide-3-hydroxy-L-aspartate + succinate + CO2
the substrate is the synthetic thioether linked cyclic peptide hFX-CP101-119. It is designed based on 19 EGFD1 amino acid residues of the sequence of human coagulation factor X (hFX amino acids 101-119)
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additional information
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overexpression may be associated with malignant transformation
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additional information
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the enzyme hydroxylates epidermal growth factor-like domains in transformation-associated proteins
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additional information
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overexpression may be associated with malignant transformation
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