CATH Classification

Domain Context

CATH Clusters

Superfamily Clavaminate synthase-like
Functional Family Hypoxia-inducible factor 1-alpha inhibitor

Enzyme Information

1.14.11.n4
Ankyrin-repeat-histidine dioxagenase.
based on mapping to UniProt Q9NWT6
(1) [Ankyrin-repeat domain protein]-L-histidine + 2-oxoglutarate + O(2) = [ankyrin-repeat domain protein]-(3S)-3-hydroxy-L-histidine + succinate + CO(2). (2) [Ankyrin-repeat domain protein]-L-asparagine + 2-oxoglutarate + O(2) = [ankyrin-repeat domain protein]-(3S)-3-hydroxy-L-asparagine + succinate + CO(2). (3) [Ankyrin-repeat domain protein]-L-aspartate + 2-oxoglutarate + O(2) = [ankyrin-repeat domain protein]-(3S)-3-hydroxy-L-aspartate + succinate + CO(2).
1.14.11.30
Hypoxia-inducible factor-asparagine dioxygenase.
based on mapping to UniProt Q9NWT6
Hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O(2) = hypoxia- inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO(2).
-!- Contains iron, and requires ascorbate. -!- Catalyzes hydroxylation of an asparagine in the C-terminal transcriptional activation domain of HIF-alpha, the alpha subunit of the transcriptional regulator HIF (hypoxia-inducible factor), which reduces its interaction with the transcriptional coactivator protein p300. -!- The requirement of oxygen for the hydroxylation reaction enables animals to respond to hypoxia.

UniProtKB Entries (1)

Q9NWT6
HIF1N_HUMAN
Homo sapiens
Hypoxia-inducible factor 1-alpha inhibitor

PDB Structure

PDB 5OP6
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Molecular and cellular mechanisms of HIF prolyl hydroxylase inhibitors in clinical trials.
Yeh, T.L., Leissing, T.M., Abboud, M.I., Thinnes, C.C., Atasoylu, O., Holt-Martyn, J.P., Zhang, D., Tumber, A., Lippl, K., Lohans, C.T., Leung, I.K.H., Morcrette, H., Clifton, I.J., Claridge, T.D.W., Kawamura, A., Flashman, E., Lu, X., Ratcliffe, P.J., Chowdhury, R., Pugh, C.W., Schofield, C.J.
Chem Sci
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