KT5720

Last updated
KT5720
KT 5720.svg
Names
IUPAC name
(5R,6S,8S)-Hexyl 6-hydroxy-5-methyl-13-oxo-6,7,8,13,14,15-hexahydro-5H-16-oxa-4b,8a,14-triaza-5,8-methanodibenzo[b,h]cycloocta[jkl]cyclopenta[e]-as-indacene-6-carboxylate
Other names
KT 5720
Identifiers
3D model (JSmol)
ChEBI
ChemSpider
ECHA InfoCard 100.238.838 OOjs UI icon edit-ltr-progressive.svg
PubChem CID
UNII
  • InChI=1S/C32H31N3O5/c1-3-4-5-10-15-39-30(37)32(38)16-23-34-21-13-8-6-11-18(21)25-26-20(17-33-29(26)36)24-19-12-7-9-14-22(19)35(28(24)27(25)34)31(32,2)40-23/h6-9,11-14,23,38H,3-5,10,15-17H2,1-2H3,(H,33,36)/t23-,31+,32+/m0/s1 X mark.svgN
    Key: ZHEHVZXPFVXKEY-RUAOOFDTSA-N X mark.svgN
  • InChI=1/C32H31N3O5/c1-3-4-5-10-15-39-30(37)32(38)16-23-34-21-13-8-6-11-18(21)25-26-20(17-33-29(26)36)24-19-12-7-9-14-22(19)35(28(24)27(25)34)31(32,2)40-23/h6-9,11-14,23,38H,3-5,10,15-17H2,1-2H3,(H,33,36)/t23-,31+,32+/m0/s1
    Key: ZHEHVZXPFVXKEY-RUAOOFDTBS
  • CCCCCCOC(=O)[C@@]1(C[C@H]2N3C4=CC=CC=C4C5=C6C(=C7C8=CC=CC=C8N(C7=C53)[C@@]1(O2)C)CNC6=O)O
Properties
C32H31N3O5
Molar mass 537.616 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Infobox references

KT5720 is a kinase inhibitor with specificity towards protein kinase A. [1] It is a semi-synthetic derivative of K252a [2] and analog of staurosporine.

Related Research Articles

Protein kinase enzyme that adds phosphate groups to other proteins

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 and the other 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.

Kinase Enzyme catalyzing transfer of phosphate groups onto specific substrates

In biochemistry, a kinase is an enzyme that catalyzes the transfer of phosphate groups from high-energy, phosphate-donating molecules to specific substrates. This process is known as phosphorylation, where the substrate gains a phosphate group and the high-energy ATP molecule donates a phosphate group. This transesterification produces a phosphorylated substrate and ADP. Conversely, it is referred to as dephosphorylation when the phosphorylated substrate donates a phosphate group and ADP gains a phosphate group. These two processes, phosphorylation and dephosphorylation, occur four times during glycolysis.

Tyrosine kinase Class of enzymes that phosphorylate protein tyrosine residues

A tyrosine kinase is an enzyme that can transfer a phosphate group from ATP to the tyrosine residues of specific proteins inside a cell. It functions as an "on" or "off" switch in many cellular functions.

Aurora kinases are serine/threonine kinases that are essential for cell proliferation. They are phosphotransferase enzymes that help the dividing cell dispense its genetic materials to its daughter cells. More specifically, Aurora kinases play a crucial role in cellular division by controlling chromatid segregation. Defects in this segregation can cause genetic instability, a condition which is highly associated with tumorigenesis.

Serine/threonine-specific protein kinase

A serine/threonine protein kinase is a kinase enzyme that phosphorylates the OH group of serine or threonine. At least 125 of the 500+ human protein kinases are serine/threonine kinases (STK).

PRKCD

Protein kinase C delta type is an enzyme that in humans is encoded by the PRKCD gene.

PRKCB1

Protein kinase C beta type is an enzyme that in humans is encoded by the PRKCB gene.

MAP2K6

Dual specificity mitogen-activated protein kinase kinase 6 also known as MAP kinase kinase 6 or MAPK/ERK kinase 6 is an enzyme that in humans is encoded by the MAP2K6 gene, on chromosome 17.

MAP2K3

Dual specificity mitogen-activated protein kinase kinase 3 is an enzyme that in humans is encoded by the MAP2K3 gene.

In enzymology, a dephospho-[reductase kinase] kinase is an enzyme that catalyzes the chemical reaction

In biochemistry, a dual-specificity kinase is a kinase that can act as both tyrosine kinase and serine/threonine kinase.

In enzymology, a polo kinase is a kinase enzyme i.e. one that catalyzes the chemical reaction

In enzymology, a protein-histidine pros-kinase is an enzyme that catalyzes the chemical reaction

In enzymology, a protein-histidine tele-kinase is an enzyme that catalyzes the chemical reaction

Tau-protein kinase Class of enzymes

In enzymology, a tau-protein kinase is an enzyme that catalyzes the chemical reaction

Protein kinase D1

Serine/threonine-protein kinase D1 is an enzyme that in humans is encoded by the PRKD1 gene.

PRKD3

Serine/threonine-protein kinase D3 (PKD3) or PKC-nu is an enzyme that in humans is encoded by the PRKD3 gene.

CAMK1

Calcium/calmodulin-dependent protein kinase type 1 is an enzyme that in humans is encoded by the CAMK1 gene.

MAPKAPK3

MAP kinase-activated protein kinase 3 is an enzyme that in humans is encoded by the MAPKAPK3 gene.

PRKG1

cGMP-dependent protein kinase 1, alpha isozyme is an enzyme that in humans is encoded by the PRKG1 gene.

References

  1. Makarevich, A. V.; Sirotkin, A. V.; Rafay, J. (2010). "Comparison of Effects of Protein Kinase A, Mitogen-activated Protein Kinase, and Cyclin-dependent Kinase Blockers on Rabbit Ovarian Granulosa Cell Functions". Hormone and Metabolic Research. 42 (13): 936–43. doi:10.1055/s-0030-1267226. PMID   20972940.
  2. CID 3844 from PubChem