Loading AI tools
Enzyme type From Wikipedia, the free encyclopedia
CAMK, also written as CaMK or CCaMK, is an abbreviation for the Ca2+/calmodulin-dependent protein kinase class of enzymes. CAMKs are activated by increases in the concentration of intracellular calcium ions (Ca2+) and calmodulin. When activated, the enzymes transfer phosphates from ATP to defined serine or threonine residues in other proteins, so they are serine/threonine-specific protein kinases. Activated CAMK is involved in the phosphorylation of transcription factors and therefore, in the regulation of expression of responding genes. CAMK also works to regulate the cell life cycle (i.e. programmed cell death), rearrangement of the cell's cytoskeletal network, and mechanisms involved in the learning and memory of an organism.[1]
Ca2+/calmodulin-dependent protein kinase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 2.7.11.17 | ||||||||
CAS no. | 97350-82-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
|
There are 2 common types of CAM Kinase proteins: specialized and multi-functional CAM kinases.
Once calcium concentrations in the cell rise, CAM kinases become saturated and bind the maximum of four calcium molecules.[1] This calcium saturation activates the kinase and allows it to undergo a conformational change which permits the kinase to bind to its phosphorylation target sites. CAMK removes a phosphate group from ATP, most typically using a Mg2+ ion, and adds it to the CAM protein, rendering it active.[2] The CAM Kinase contains a highly concentrated glycine loop where the gamma phosphate from the donor ATP molecule is easily able to bind to the enzyme which then utilizes the metal ion to facilitate a smooth phosphate transfer to the target protein.[3] This phosphate transfer then activates the kinase's target and completes the phosphorylation cycle.
Figure 1 shows how the presence of calcium or calmodulin allows for the activation of CAM kinases (CAMK II).
All kinases have a common structure of a catalytic core including an ATP binding site along with a larger substrate binding site.[4] The catalytic core is typically composed of β-strands with the substrate binding site composed of α-helices.[5] Most all CAM kinases includes a variety of domains, including: a catalytic domain, a regulatory domain, an association domain, and a calcium/calmodulin binding domain.[6]
Members of the CAMK enzyme class include, but are not limited to:
Pseudokinases are pseudoenzymes, proteins that resemble enzymes structurally, but lack catalytic activity.
Some of these pseudokinases that are related to the CAMK family include:
Seamless Wikipedia browsing. On steroids.
Every time you click a link to Wikipedia, Wiktionary or Wikiquote in your browser's search results, it will show the modern Wikiwand interface.
Wikiwand extension is a five stars, simple, with minimum permission required to keep your browsing private, safe and transparent.