Adenylate kinase () ( also known as ADK or myokinase ) is a phosphotransferase enzyme that catalyzes the interconversion of adenine nucleotides, and plays an important role in cellular energy homeostasis.

* Adenylate kinase, subfamily

* Adenylate kinase, isozyme 1

* Adenylate kinase, a phosphotransferase enzyme that plays an important role in cellular energy homeostasis

Adenylate Kinase 2 ( AK2 ) deficiency in humans causes hematopoietic defects associated with sensorineural deafness.

Adenylate cyclase (, also known as adenylyl cyclase, adenyl cyclase or AC ) is an enzyme with key regulatory roles in nearly all cells.

Adenylate cyclase is dually regulated by G proteins ( Gs stimulating activity and Gi inhibiting it ), and by forskolin, as well as other isoform-specific effectors:

Adenylate Kinase is a signal transducing protein ; thus, the balance between conformations regulates protein activity.

Magnesium is a cofactor for Adenylate cyclase.

The reaction that Adenylate Cyclase catalyzes is the conversion of ATP to 3 ', 5 '- cyclic AMP.

Adenylate cyclases are often activated or inhibited by G proteins, which are coupled to membrane receptors and thus can respond to hormonal or other stimuli.

" Physiologic-and Adenylate Cyclase-Coupled Beta-Adrenergic Receptors ", " Pathologic Physiology Mechanisms of Disease ", 143-145.

* Pyruvate kinase deficiency

Methemoglobinemia can also arise in patients with pyruvate kinase deficiency due to impaired production of NADH – the essential cofactor for diaphorase I.

DAX-1 mutations may cluster in a syndrome with glycerol kinase deficiency with a number of other symptoms when DAX-1 is deleted together with a number of other genes.

Genetic defects of this enzyme cause the disease known as pyruvate kinase deficiency.

One example is red blood cells, which in a state of pyruvate kinase deficiency rapidly become deficient in ATP and can undergo hemolysis.

Therefore, pyruvate kinase deficiency can cause hemolytic anemia.

This hypothesis has since been confirmed and has been extended to hemoglobin C and hemoglobin E, abnormalities in ankyrin and spectrin ( ovalocytosis, elliptocytosis ), in glucose-6-phosphate dehydrogenase deficiency and pyruvate kinase deficiency, loss of the Gerbich antigen ( glycophorin C ) and the Duffy antigen on the erythrocytes, thalassemias and variations in the major histocompatibility complex classes 1 and 2 and CD32 and CD36.

* Defective red cell metabolism ( as in glucose-6-phosphate dehydrogenase deficiency and pyruvate kinase deficiency )

** Pyruvate kinase deficiency

Other deficiency diseases with similar signs and symptoms include deficiencies of phosphoglycerate kinase, phosphoglycerate mutase, lactate dehydrogenase, beta-enolase and aldolase A.

Pyruvate kinase deficiency, also called erythrocyte pyruvate kinase deficiency, is an inherited metabolic disorder of the enzyme pyruvate kinase which affects the survival of red blood cells and causes them to deform into echinocytes on peripheral blood smears.

Pyruvate kinase deficiency is the second most common cause of enzyme-deficient hemolytic anemia, following G6PD deficiency.

A deficiency in pyruvate kinase, the enzyme that potentiates the last step of glycolysis ( phosphoenolpyruvate converted to pyruvate ), results in red blood cells ( RBCs ) with decreased energy.

Partial splenectomies are sometimes performed as a treatment for anemias due to an underlying inability for RBC deformation ( hereditary spherocytosis and pyruvate kinase deficiency ).

As a result, individuals with pyruvate kinase deficiency may have a greater capacity for physical activity than others with similarly low hemoglobin levels.

The diagnosis can be confirmed in the laboratory by finding an absence or deficiency of the ATM protein in cultured blood cells, an absence or deficiency of ATM function ( kinase assay ), or mutations in both copies of the cell ’ s ATM gene.

In erythrocyte regulation, erythropoietin is a protein containing 165 amino acids that plays a role in activating the cytoplasmic protein kinase JAK.

Overall, this is also how a receptor tyrosine kinase might be activated by a ligand to regulate erythrocyte formation.

The mechanism of inhibition seems likely to be an inhibition of protein kinase A activity within the erythrocyte.

In humans, there are two pyruvate kinase isozymes: type M ( muscle, SwissProt P14618 ) and type L, R ( liver and erythrocyte, SwissProt P30613 ).

Within the erythrocyte it interacts with band 4. 1 ( an 80-kDa protein ) and p55 ( a palmitoylated peripheral membrane phosphoprotein and a member of the membrane-associated guanylate kinase family ) to form a ternary complex that is critical for the shape and stability of erythrocytes.

* A decrease renal protein kinase C is caused.

CheA in turn transfers phosphoryl groups to conserved aspartate residues in the response regulators CheB and CheY CheA is a histidine kinase and it does not actively transfer the phosphoryl group.

BI811283 is a small molecule inhibitor of the Aurora B kinase protein being developed by Boehringer Ingelheim for use as an anti-cancer agent.

Another use of gene therapy is the introduction of enzymes into these cells that make them susceptible to particular chemotherapy agents ; studies with introducing thymidine kinase in gliomas, making them susceptible to aciclovir, are in their experimental stage.

The phosphorylation of molecules requires that ATP is imported into the lumen of the Golgi and utilised by resident kinases such as casein kinase 1 and casein kinase 2.

In hyperthyroidism CK-MB ( Creatine kinase ) is usually elevated.

Like the insulin receptor, the IGF-1 receptor is a receptor tyrosine kinase — meaning the receptor signals by causing the addition of a phosphate molecule on particular tyrosines.

Janus kinase ( JAK ) is a family of intracellular, nonreceptor tyrosine kinases that transduce cytokine-mediated signals via the JAK-STAT pathway.

JH1 is the kinase domain important for the enzymatic activity of the JAK and contains typical features of a tyrosine kinase such as conserved tyrosines necessary for JAK activation ( e. g. Y1038 / Y1039 in JAK1, Y1007 / Y1008 in JAK2, Y980 / Y981 in JAK3, and Y1054 / Y1055 in Tyk2 ).

JH2 is a " pseudokinase domain ", a domain structurally similar to a tyrosine kinase and essential for a normal kinase activity, yet lacks enzymatic activity.

The amino terminal ( NH < sub > 2 </ sub >) end ( JH4-JH7 ) of Jaks is called a FERM domain ( short for band 4. 1 ezrin, radixin and moesin ); this domain is also found in the focal adhesion kinase ( FAK ) family and is involved in association of JAKs with cytokine receptors and / or other kinases.

These include sphingosine-1-phosphate, a sphingolipid derived from ceramide that is a potent messenger molecule involved in regulating calcium mobilization, cell growth, and apoptosis ; diacylglycerol ( DAG ) and the phosphatidylinositol phosphates ( PIPs ), involved in calcium-mediated activation of protein kinase C ; the prostaglandins, which are one type of fatty-acid derived eicosanoid involved in inflammation and immunity ; the steroid hormones such as estrogen, testosterone and cortisol, which modulate a host of functions such as reproduction, metabolism and blood pressure ; and the oxysterols such as 25-hydroxy-cholesterol that are liver X receptor agonists.

This protein is an autonomously active form of the enzyme protein kinase C ( PKC ), known as PKMζ.

A second category of gravis is due to autoantibodies against the MuSK protein ( muscle specific kinase ), a tyrosine kinase receptor which is required for the formation of the neuromuscular junction.

Bcr-Abl codes for a receptor tyrosine kinase, which is constitutively active, leading to uncontrolled cell proliferation.

Gankyrin, a recently identified oncoprotein, is one of the 19S subcomponents that also tightly binds the cyclin-dependent kinase CDK4 and plays a key role in recognizing ubiquitinated p53, via its affinity for the ubiquitin ligase MDM2.

The mechanism for this effect is not clear, but is hypothesized to be specific to cells in quiescent states, or to result from the differential activity of the pro-apoptotic kinase JNK.