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Information on EC 1.14.11.16 - peptide-aspartate beta-dioxygenase
for references in articles please use BRENDA:EC1.14.11.16
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
1.14.11.16 peptide-aspartate beta-dioxygenase
IUBMB Comments
Requires Fe2+. Some vitamin K-dependent coagulation factors, as well as synthetic peptides based on the structure of the first epidermal growth factor domain of human coagulation factor IX or X, can act as acceptors.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.14.11.16
-
prolyl
- hydroxylases
-
oxygen-dependent
- ankyrin
-
hif-alpha
-
oxygen-sensing
-
junctin
-
humbug
-
fih-dependent
-
fih-mediated
-
alpha-ketoglutarate-dependent
-
junctate
- medicine
- analysis
Reaction Schemes
showSynonyms
factor inhibiting hif, aspartyl beta-hydroxylase, aspartyl (asparaginyl) beta-hydroxylase, factor-inhibiting hypoxia-inducible factor, factor inhibiting hypoxia-inducible factor, hif asparaginyl hydroxylase, aspartyl/asparaginyl beta-hydroxylase, aspartyl (asparaginyl)-beta-hydroxylase, aspartate beta-hydroxylase, human aspartyl (asparaginyl) beta-hydroxylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAH
aspartate beta-hydroxylase
aspartyl beta-hydroxylase
aspartyl-(asparaginyl)-beta-hydroxylase
aspartylpeptide beta-dioxygenase
-
-
-
-
ASPH
factor inhibiting hypoxia-inducible transcription factor (HIF)
FIH
HAAH
aspartate beta-hydroxylase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
peptide-L-aspartate + 2-oxoglutarate + O2 = peptide-3-hydroxy-L-aspartate + succinate + CO2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydroxylation
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
hydroxylation
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
peptide-L-aspartate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Requires Fe2+. Some vitamin K-dependent coagulation factors, as well as synthetic peptides based on the structure of the first epidermal growth factor domain of human coagulation factor IX or X, can act as acceptors.
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CAS REGISTRY NUMBER
COMMENTARY
122544-66-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
?
-
Substrates: a maximum of three ankyrin repeats enables ankyrin repeat domain proteins as a substrate
Products: -
Products: -
?
first epidermal growth factor-like domain-L-aspartate + 2-oxoglutarate + O2
first epidermal growth factor-like domain-3-hydroxy-L-aspartate + succinate + CO2
-
Substrates: -
Products: -
Products: -
r
HIF (L-Asn803) + 2-oxoglutarate + O2
HIF (3-hydroxy-L-Asn803) + succinate + CO2
-
Substrates: 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
Products: -
Products: -
?
HIF-1alpha peptide Asp788-Leu822 (L-Asn803) + 2-oxoglutarate + O2
HIF-1alpha peptide Asp788-Leu822 (3-hydroxy-L-Asn803) + succinate + CO2
Substrates: much lower activity with peptides lacking residues 819-822, 807-822, and 815-822
Products: -
Products: -
?
HIF-1alpha peptide Asp788-Leu822 (L-asparagine803) + 2-oxoglutarate + O2
?
Substrates: -
Products: -
Products: -
r
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
[factor X first EGF-like domain]-L-aspartate + 2-oxoglutarate + O2
[factor X first EGF-like domain]-3-hydroxy-L-aspartate + succinate + CO2
Substrates: -
Products: -
Products: -
?
[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
Substrates: 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
Products: -
Products: -
?
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
-
Substrates: hydroxylation of highly conserved asparaginyl residues within the ankyrin repeat
Products: -
Products: -
?
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
-
Substrates: hydroxylation of hyghly conserved asparaginyl residues within the ankyrin repeat
Products: -
Products: -
?
peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
-
Substrates: first epidermal growth factor-like domain of human protein S with an asparagine replacing the aspartic acid at position 18
Products: -
Products: -
?
peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
Substrates: -
Products: -
Products: -
?
peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
-
Substrates: first epidermal growth factor-like domain of bovine protein S with an asparagine replacing the aspartic acid at position 18
Products: -
Products: -
?
peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
-
Substrates: enzyme catalyzes the erythro-beta-hydroxylation of asparaginyl and aspartyl residues to form the 2S, 3R-product, possible role in the Notch signalling pathway
Products: -
Products: -
?
peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
-
Substrates: hydroxylation of Asn803 in hypoxia-inducible transcription factor, converted protein is incapable in interacting with the transcripitonal coactivator p300
Products: -
Products: -
?
peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
Substrates: hydroxylation of Asn803 in hypoxia-inducible transcription factor, converted protein is incapable in interacting with the transcripitonal coactivator p300
Products: -
Products: -
?
peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
-
Substrates: first epidermal growth factor-like domain of human protein S as substrate
Products: -
Products: -
?
peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
-
Substrates: specific erythro-hydroxylation
Products: -
Products: -
?
peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
-
Substrates: second epidermal growth factor-like domain of bovine protein S
Products: -
Products: -
?
peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
-
Substrates: first epidermal growth factor-like domain of bovine protein S as substrate
Products: -
Products: -
?
peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
-
Substrates: hydroxylates epidermal growth factor-like domains in transformation-associated proteins
Products: -
Products: -
?
peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
-
Substrates: specific erythro-hydroxylation
Products: -
Products: -
?
peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
-
Substrates: first epidermal growth factor-like domain of human factor IX as substrate
Products: -
Products: -
?
peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
-
Substrates: specific erythro-hydroxylation
Products: -
Products: -
?
peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
-
Substrates: first epidermal growth factor-like domain of human factor IX as substrate
Products: -
Products: -
?
peptide-L-aspartate + 2-oxoglutarate + O2
peptide-3-hydroxy-L-aspartate + succinate + CO2
Substrates: -
Products: -
Products: -
?
peptide-L-aspartate + 2-oxoglutarate + O2
peptide-3-hydroxy-L-aspartate + succinate + CO2
Substrates: the enzyme catalyses hydroxylation of asparaginyl- and aspartyl-residues in epidermal growth factor-like domains
Products: -
Products: -
?
peptide-L-aspartate + 2-oxoglutarate + O2
peptide-3-hydroxy-L-aspartate + succinate + CO2
Substrates: the enzyme catalyzes the post-translational hydroxylation of Asp and Asn residues in epidermal growth factor-like domains
Products: -
Products: -
?
peptide-L-aspartate + 2-oxoglutarate + O2
peptide-3-hydroxy-L-aspartate + succinate + CO2
Substrates: 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)
Products: -
Products: -
?
peptide-L-aspartate + 2-oxoglutarate + O2
peptide-3-hydroxy-L-aspartate + succinate + CO2
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
-
Substrates: overexpression may be associated with malignant transformation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme hydroxylates epidermal growth factor-like domains in transformation-associated proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: overexpression may be associated with malignant transformation
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
-
Substrates: enzyme catalyzes the erythro-beta-hydroxylation of asparaginyl and aspartyl residues to form the 2S, 3R-product, possible role in the Notch signalling pathway
Products: -
Products: -
?
peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
-
Substrates: hydroxylation of Asn803 in hypoxia-inducible transcription factor, converted protein is incapable in interacting with the transcripitonal coactivator p300
Products: -
Products: -
?
peptide L-asparagine + 2-oxoglutarate + O2
peptide 3-hydroxy-L-asparagine + succinate + CO2
Substrates: hydroxylation of Asn803 in hypoxia-inducible transcription factor, converted protein is incapable in interacting with the transcripitonal coactivator p300
Products: -
Products: -
?
peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
-
Substrates: hydroxylates epidermal growth factor-like domains in transformation-associated proteins
Products: -
Products: -
?
peptide L-aspartate + 2-oxoglutarate + O2
peptide 3-hydroxy-L-aspartate + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
peptide-L-aspartate + 2-oxoglutarate + O2
peptide-3-hydroxy-L-aspartate + succinate + CO2
Substrates: the enzyme catalyses hydroxylation of asparaginyl- and aspartyl-residues in epidermal growth factor-like domains
Products: -
Products: -
?
peptide-L-aspartate + 2-oxoglutarate + O2
peptide-3-hydroxy-L-aspartate + succinate + CO2
Substrates: the enzyme catalyzes the post-translational hydroxylation of Asp and Asn residues in epidermal growth factor-like domains
Products: -
Products: -
?
additional information
?
-
-
Substrates: overexpression may be associated with malignant transformation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme hydroxylates epidermal growth factor-like domains in transformation-associated proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: overexpression may be associated with malignant transformation
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
the enzyme binds divalent calcium, high-affinity regulatory binding site for Ca2+
Fe2+
Fe2+
Fe(II)-binding employs only two Fe(II)-binding ligands (His679/His725)
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Insulin-like growth factor-1
-
stimulates peptide-aspartate beta-dioxygenase protein expression and directional motility. Ethanol reduces the stimulation without inhibition of the mRNA expression
-
ankyrin repeat domain
-
may function as a natural inhibitor and provide an oxygen-dependent interface that modulates hypoxia-induced factor signaling
-
ankyrin repeat domain
-
may function as a natural inhibitor and provide an oxygen-dependent interface that modulates hypoxia-induced factor signaling
-
additional information
several 2-oxoglutarate analogs inhibits enzyme activity
-
additional information
-
development of a ScFv anti-HAAH antibody for specific in vivo inhibition of the enzyme by expression of His-tagged light and heavy chain cloned from the hybridoma cells G3/F11 in Escherichia coli strain BL21(DE3)PlysS/pET-16b, partly in inclusion bodies, or of c-myc-tagged ScFv in Escherichia coli strain HB2151/pHEN1, partly cytosolic. Variable regions of the genes of the heavy chain and light chain are connected with a flexible linker using an overlap extension PCR. Nucleotide sequence analysis revealed that the anti-HAAH VH was a member of the VH V gene family and the VL gene belonged to the Vk gene family VI subgroup
-
additional information
-
phosphorylation by GSK-3beta oder degradation by caspase
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
regulated by insulin and insulin-like growth factor
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Abortion, Missed
[Expression of aspartyl-(asparaginyl) beta-hydroxylase in villi in patients with missed abortion]
Abortion, Spontaneous
Role of aspartyl-(asparaginyl) beta-hydroxylase in placental implantation: Relevance to early pregnancy loss.
Bile Duct Neoplasms
Detection of human aspartyl (asparaginyl) beta-hydroxylase and homeobox B7 mRNA in brush cytology specimens from patients with bile duct cancer.
Breast Neoplasms
Cytoplasmic location of factor-inhibiting hypoxia-inducible factor is associated with an enhanced hypoxic response and a shorter survival in invasive breast cancer.
Breast Neoplasms
DNA methylation analysis of the HIF-1? prolyl hydroxylase domain genes PHD1, PHD2, PHD3 and the factor inhibiting HIF gene FIH in invasive breast carcinomas.
Breast Neoplasms
The key hypoxia regulated gene CAIX is upregulated in basal-like breast tumours and is associated with resistance to chemotherapy.
Breast Neoplasms
[Expression of ASPH Gene in Invasive Breast Cancer and Its Clinical Significance in Promoter Methylation].
Carcinoma
Aspartyl-(asparaginyl)-beta-hydroxylase regulates hepatocellular carcinoma invasiveness.
Carcinoma
Co-targeting of multiple microRNAs on factor-inhibiting hypoxia-inducible factor (FIH) gene for the pathogenesis of head and neck carcinomas.
Carcinoma
Factor-inhibiting hypoxia-inducible factor expression in patients with high-risk locally advanced renal cell carcinoma and its relationship with tumor progression.
Carcinoma
Human aspartyl (asparaginyl) beta-hydroxylase monoclonal antibodies: potential biomarkers for pancreatic carcinoma.
Carcinoma
Prognostic value of aspartyl (asparaginyl)-beta-hydroxylase/humbug expression in non-small cell lung carcinoma.
Carcinoma, Hepatocellular
Aspartyl-(asparaginyl)-beta-hydroxylase regulates hepatocellular carcinoma invasiveness.
Carcinoma, Hepatocellular
Aspartyl-asparagyl beta hydroxylase over-expression in human hepatoma is linked to activation of insulin-like growth factor and notch signaling mechanisms.
Carcinoma, Hepatocellular
Expression of aspartyl beta-hydroxylase and its clinicopathological significance in hepatocellular carcinoma.
Carcinoma, Hepatocellular
Monoclonal antibodies against human aspartyl (asparaginyl) beta-hydroxylase developed by DNA immunization.
Carcinoma, Hepatocellular
Overexpression of aspartyl-(asparaginyl)-beta-hydroxylase in hepatocellular carcinoma is associated with worse surgical outcome.
Carcinoma, Hepatocellular
Prognostic value of humbug gene overexpression in stage II colon cancer.
Carcinoma, Hepatocellular
Prolyl hydroxylase domain protein 3 and asparaginyl hydroxylase factor inhibiting HIF-1 levels are predictive of tumoral behavior and prognosis in hepatocellular carcinoma.
Carcinoma, Renal Cell
Factor-inhibiting hypoxia-inducible factor expression in patients with high-risk locally advanced renal cell carcinoma and its relationship with tumor progression.
Carcinoma, Renal Cell
[Growth Regulation of Factor Inhibiting Hypoxia-Inducible Factor in Renal Carcinoma Cells].
Cholangiocarcinoma
Antisense oligodeoxynucleotides directed against aspartyl (asparaginyl) beta-hydroxylase suppress migration of cholangiocarcinoma cells.
Cholangiocarcinoma
Aspartate beta-hydroxylase promotes cholangiocarcinoma progression by modulating RB1 phosphorylation.
Cholangiocarcinoma
Clinicopathological correlates of aspartyl (asparaginyl) beta-hydroxylase over-expression in cholangiocarcinoma.
Cholangiocarcinoma
Prognostic value of humbug gene overexpression in stage II colon cancer.
Cholangiocarcinoma
Targeting Aspartate Beta-Hydroxylase with the Small Molecule Inhibitor MO-I-1182 Suppresses Cholangiocarcinoma Metastasis.
Fetal Alcohol Spectrum Disorders
Ethanol inhibition of aspartyl-asparaginyl-beta-hydroxylase in fetal alcohol spectrum disorder: potential link to the impairments in central nervous system neuronal migration.
Glioblastoma
The Role of Factor Inhibiting HIF (FIH-1) in Inhibiting HIF-1 Transcriptional Activity in Glioblastoma Multiforme.
Kidney Neoplasms
Factor inhibiting HIF (FIH-1) promotes renal cancer cell survival by protecting cells from HIF-1?-mediated apoptosis.
Myocardial Infarction
Double knockdown of prolyl hydroxylase and factor-inhibiting hypoxia-inducible factor with nonviral minicircle gene therapy enhances stem cell mobilization and angiogenesis after myocardial infarction.
Neoplasm Metastasis
Expression of aspartyl beta-hydroxylase and its clinicopathological significance in hepatocellular carcinoma.
Neoplasm Metastasis
Targeting Aspartate Beta-Hydroxylase with the Small Molecule Inhibitor MO-I-1182 Suppresses Cholangiocarcinoma Metastasis.
Neoplasms
A hypoxic niche regulates glioblastoma stem cells through hypoxia inducible factor 2 alpha.
Neoplasms
Antisense oligonucleotides selectively regulate aspartyl beta-hydroxylase and its truncated protein isoform in vitro but distribute poorly into A549 tumors in vivo.
Neoplasms
Aspartate beta-hydroxylase promotes cholangiocarcinoma progression by modulating RB1 phosphorylation.
Neoplasms
Aspartyl-asparagyl beta hydroxylase over-expression in human hepatoma is linked to activation of insulin-like growth factor and notch signaling mechanisms.
Neoplasms
Clinicopathological correlates of aspartyl (asparaginyl) beta-hydroxylase over-expression in cholangiocarcinoma.
Neoplasms
Detection of human aspartyl (asparaginyl) beta-hydroxylase and homeobox B7 mRNA in brush cytology specimens from patients with bile duct cancer.
Neoplasms
Expression of aspartyl beta-hydroxylase and its clinicopathological significance in hepatocellular carcinoma.
Neoplasms
Expression of HIF-2a in clear-cell renal cell carcinoma independently predicts overall survival.
Neoplasms
Factor-inhibiting hypoxia-inducible factor expression in patients with high-risk locally advanced renal cell carcinoma and its relationship with tumor progression.
Neoplasms
Investigation of FIH-1 and SOCS3 expression in KRAS mutant and wild-type patients with colorectal cancer.
Neoplasms
Isolation and characterization of human antibodies targeting human aspartyl (asparaginyl) beta-hydroxylase.
Neoplasms
Regulation of IL-1?-induced NF-?B by hydroxylases links key hypoxic and inflammatory signaling pathways.
Neoplasms
Role of the aspartyl-asparaginyl-beta-hydroxylase gene in neuroblastoma cell motility.
Neoplasms
Targeting Aspartate Beta-Hydroxylase with the Small Molecule Inhibitor MO-I-1182 Suppresses Cholangiocarcinoma Metastasis.
Neoplasms
The distribution and expression profiles of human Aspartyl/Asparaginyl beta-hydroxylase in tumor cell lines and human tissues.
Neoplasms
The key hypoxia regulated gene CAIX is upregulated in basal-like breast tumours and is associated with resistance to chemotherapy.
Neoplasms
Transcriptional activity and Sp 1/3 transcription factor binding to the P1 promoter sequences of the human AbetaH-J-J locus.
Neoplasms
[Expression of human aspartyl beta-hydroxylase and preparation of its monoclonal antibody].
Neoplasms
[Research on Relationship of HIF-1 Signaling Pathway and Postmenstrual Osteoporosis].
Neoplasms
[The distribution and expression pro-files of Aspartyl/Asparaginyl beta-hydroxylase (ASPH) in some tumorous cell lines and tissues]
Neuroblastoma
Differential growth factor regulation of aspartyl-(asparaginyl)-beta-hydroxylase family genes in SH-Sy5y human neuroblastoma cells.
Neuroblastoma
Role of the aspartyl-asparaginyl-beta-hydroxylase gene in neuroblastoma cell motility.
Squamous Cell Carcinoma of Head and Neck
Co-targeting of multiple microRNAs on factor-inhibiting hypoxia-inducible factor (FIH) gene for the pathogenesis of head and neck carcinomas.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.086
[factor X first EGF-like domain]-L-aspartate
pH and temperature not specified in the publication
-
0.0012
[thioether-linked cyclic peptide hFX-CP101-119]-L-aspartate
pH 7.5, 20°C
-
0.019
first growth factor-like domain-L-aspartate
-
substrate is of human protein S with an asparagine replacing the aspartic acid at position 18, native enzyme
-
0.024
first growth factor-like domain-L-aspartate
-
substrate is of human protein S with an asparagine replacing the aspartic acid at position 18, recombinant enzyme
-
0.034
first growth factor-like domain-L-aspartate
-
substrate is of human protein S with an asparagine replacing the aspartic acid at position 18, 52 kDa protein
-
0.035
first growth factor-like domain-L-aspartate
-
substrate is of human protein S with an asparagine replacing the aspartic acid at position 18, 56 kDa protein
-
0.067
first growth factor-like domain-L-aspartate
-
substrate is of human protein S, 52 kDa protein
-
0.075
first growth factor-like domain-L-aspartate
-
substrate is of human protein S, 56 kDa protein
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.23
[factor X first EGF-like domain]-L-aspartate
pH and temperature not specified in the publication
-
0.2
[thioether-linked cyclic peptide hFX-CP101-119]-L-aspartate
pH 7.5, 20°C
-
0.0167
first growth factor-like domain-L-aspartate
-
substrate is of human protein S, 56 kDa protein
-
0.0217
first growth factor-like domain-L-aspartate
-
substrate is of human protein S with an asparagine replacing the aspartic acid at position 18, 56 kDa protein
-
0.025
first growth factor-like domain-L-aspartate
-
substrate is of human protein S, 52 kDa protein
-
0.0317
first growth factor-like domain-L-aspartate
-
substrate is of human protein S with an asparagine replacing the aspartic acid at position 18, 52 kDa protein
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15
[factor X first EGF-like domain]-L-aspartate
pH and temperature not specified in the publication
-
170
[thioether-linked cyclic peptide hFX-CP101-119]-L-aspartate
pH 7.5, 20°C
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0193
(1S,2S,4R)-3-oxalobicyclo[2.2.1]hept-5-ene-2-carboxylic acid
Homo sapiens
pH 7.5, 20°C
-
0.0063
2-oxo-3-[[4-(trifluoromethoxy)phenyl]methyl]pentanedioic acid
Homo sapiens
pH 7.5, 20°C
-
0.00017
2-[(naphthalen-2-yl)methyl]-4-oxopentanedioic acid
Homo sapiens
pH 7.5, 20°C
-
0.0109
3-((3-phenylpropyl)amino)pyridine-2,4-dicarboxylic acid
Homo sapiens
pH 7.5, 20°C
-
0.00186
3-((4-(trifluoromethyl)benzyl)amino)pyridine-2,4-dicarboxylic acid
Homo sapiens
pH 7.5, 20°C
-
0.00367
3-((4-chlorophenethyl)amino)pyridine-2,4-dicarboxylic acid
Homo sapiens
pH 7.5, 20°C
-
0.00058
3-((4-methoxybenzyl)amino)pyridine-2,4-dicarboxylic acid
Homo sapiens
pH 7.5, 20°C
-