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| Chemical and physical data | |
| Formula | C29H26N4O |
| Molar mass | 446.554 g·mol−1 |
| 3D model (JSmol) | |
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CDD-2807 is a chemical compound which acts as a potent and selective inhibitor of serine/threonine-protein kinase 33 (STK33), with a IC50 of 9.2 nM. In animal studies it causes production of abnormal sperm with reduced motility, and it has been investigated as a potential male contraceptive drug. [1] [2]
A protein kinase is a kinase which selectively modifies other proteins by covalently adding phosphates to them (phosphorylation) as opposed to kinases which modify lipids, carbohydrates, or other molecules. Phosphorylation usually results in a functional change of the target protein (substrate) by changing enzyme activity, cellular location, or association with other proteins. The human genome contains about 500 protein kinase genes and they constitute about 2% of all human genes. There are two main types of protein kinase. The great majority are serine/threonine kinases, which phosphorylate the hydroxyl groups of serines and threonines in their targets. Most of the others are tyrosine kinases, although additional types exist. Protein kinases are also found in bacteria and plants. Up to 30% of all human proteins may be modified by kinase activity, and kinases are known to regulate the majority of cellular pathways, especially those involved in signal transduction.
In cell biology, protein kinase A (PKA) is a family of serine-threonine kinase whose activity is dependent on cellular levels of cyclic AMP (cAMP). PKA is also known as cAMP-dependent protein kinase. PKA has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism. It should not be confused with 5'-AMP-activated protein kinase.
Glycogen synthase kinase 3 (GSK-3) is a serine/threonine protein kinase that mediates the addition of phosphate molecules onto serine and threonine amino acid residues. First discovered in 1980 as a regulatory kinase for its namesake, glycogen synthase (GS), GSK-3 has since been identified as a protein kinase for over 100 different proteins in a variety of different pathways. In mammals, including humans, GSK-3 exists in two isozymes encoded by two homologous genes GSK-3α (GSK3A) and GSK-3β (GSK3B). GSK-3 has been the subject of much research since it has been implicated in a number of diseases, including type 2 diabetes, Alzheimer's disease, inflammation, cancer, addiction and bipolar disorder.
cGMP-dependent protein kinase or protein kinase G (PKG) is a serine/threonine-specific protein kinase that is activated by cGMP. It phosphorylates a number of biologically important targets and is implicated in the regulation of smooth muscle relaxation, platelet function, sperm metabolism, cell division, and nucleic acid synthesis.
A serine/threonine protein kinase is a kinase enzyme, in particular a protein kinase, that phosphorylates the OH group of the amino-acid residues serine or threonine, which have similar side chains. At least 350 of the 500+ human protein kinases are serine/threonine kinases (STK).
In molecular biology, biochemistry and cell signaling the kinome of an organism is the complete set of protein kinases encoded in its genome. Kinases are usually enzymes that catalyze phosphorylation reactions and fall into several groups and families, e.g., those that phosphorylate the amino acids serine and threonine, those that phosphorylate tyrosine and some that can phosphorylate both, such as the MAP2K and GSK families. The term was first used in 2002 by Gerard Manning and colleagues in twin papers analyzing the 518 human protein kinases, and refers to both protein kinases and protein pseudokinases and their evolution of protein kinases throughout the eukaryotes. Other kinomes have been determined for rice, several fungi, nematodes, and insects, sea urchins, Dictyostelium discoideum, and the process of infection by Mycobacterium tuberculosis. Although the primary sequence of protein kinases shows substantial divergence between unrelated eukaryotes, and amino acid differences in catalytic motifs have permitted their separation of kinomes into canonical and pseudokinase subtypes, the variation found in the amino acid motifs adjacent to the site of actual phosphorylation of substrates by eukaryotic kinases is much smaller.
RAF kinases are a family of three serine/threonine-specific protein kinases that are related to retroviral oncogenes. The mouse sarcoma virus 3611 contains a RAF kinase-related oncogene that enhances fibrosarcoma induction. RAF is an acronym for Rapidly Accelerated Fibrosarcoma.
RAC(Rho family)-alpha serine/threonine-protein kinase is an enzyme that in humans is encoded by the AKT1 gene. This enzyme belongs to the AKT subfamily of serine/threonine kinases that contain SH2 protein domains. It is commonly referred to as PKB, or by both names as "Akt/PKB".
Serine/threonine-protein kinase PAK 2 is an enzyme that in humans is encoded by the PAK2 gene.
LIM domain kinase 1 is an enzyme that in humans is encoded by the LIMK1 gene.
In enzymology, a [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] is an enzyme that catalyzes the chemical reaction
Serine/threonine-protein kinase Sgk3 is an enzyme that in humans is encoded by the SGK3 gene.
PAS domain-containing serine/threonine-protein kinase is an enzyme that in humans is encoded by the PASK gene.
Serine/threonine-protein kinase 10 is an enzyme that in humans is encoded by the STK10 gene.
Serine/threonine-protein kinase Sgk2 is an enzyme that in humans is encoded by the SGK2 gene.
Serine/threonine-protein kinase PCTAIRE-2 is an enzyme that in humans is encoded by the CDK17 gene.
Doublecortin-like kinase protein 1 (DCLK1) is an enzyme that in humans is encoded by the DCLK1 gene. Its C-terminal domain in rats is expressed independently from an alternative transcript, cpg16, and can function alone as a serine/threonine protein kinase that is cyclic AMP dependent.
Microtubule-associated serine/threonine-protein kinase 1 is an enzyme that in humans is encoded by the MAST1 gene.
Myosin light chain kinase 4 also known as MYLK4 is an enzyme which in humans is encoded by the MYLK2 gene. MYLK4 is a member of the myosin light-chain kinase family of serine/threonine-specific protein kinases that phosphorylate the regulatory light chain of myosin II.
Serine/threonine-protein kinase Nek8, also known as never in mitosis A-related kinase 8, is an enzyme that in humans is encoded by the NEK8 gene.
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