IkappaB kinase
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In enzymology, an IkappaB kinase (EC 2.7.11.10) is an enzyme that catalyzes the chemical reaction
- ATP + [IkappaB protein] ADP + [IkappaB phosphoprotein]
Thus, the two substrates of this enzyme are ATP and [[[IkappaB protein]]], whereas its two products are ADP and [[[IkappaB phosphoprotein]]].
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:[IkappaB protein] phosphotransferase. Other names in common use include CHUK, IKBKA, IKBKB, IKK, IKK-1, IKK-2, inhibitor of NFkappaB kinase, inhibitor of NF-kappaB kinase, STK12, TANK-binding kinase 1, and TBK1. This enzyme participates in 15 metabolic pathways: mapk signaling pathway, apoptosis, toll-like receptor signaling pathway, t cell receptor signaling pathway, b cell receptor signaling pathway, insulin signaling pathway, adipocytokine signaling pathway, type ii diabetes mellitus, epithelial cell signaling in helicobacter pylori, [[]], pancreatic cancer, prostate cancer, chronic myeloid leukemia, acute myeloid leukemia, and small cell lung cancer.
[edit] References
- IUBMB entry for 2.7.11.10
- BRENDA references for 2.7.11.10 (Recommended.)
- PubMed references for 2.7.11.10
- PubMed Central references for 2.7.11.10
- Google Scholar references for 2.7.11.10
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