Aspartate transaminase (AST), also called aspartate aminotransferase is commonly known as sgot (AspAT/ASAT/AAT) or serum glutamic oxaloacetic transaminase

(SGOT), is a pyridoxal phosphate (PLP)-dependent transaminase enzyme (EC 2.6.1.1). AST catalyzes the reversible transfer of an -amino group between aspartate and glutamate and, as such, is an important enzyme in amino acid metabolism. AST is found in theliver, heart, skeletal muscle, kidneys, brain, and red blood cells, and it is commonly measured clinically as a marker for liver health.

Function[edit source | editbeta]

Aspartate transaminase catalyzes the interconversion of aspartate and ketoglutarate to oxaloacetate and glutamate. Aspartate (Asp) + -ketoglutarate oxaloacetate + glutamate (Glu)

Reaction catalyzed by aspartate aminotransferase

As a prototypical transaminase, AST relies on PLP as a cofactor to transfer the amino group from aspartate or glutamate to the correspondingketoacid. In the process, the cofactor shuttles between PLP [2] and the pyridoxamine phosphate (PMP) form. The amino group transfer catalyzed by this enzyme is crucial in both amino acid degradation and biosynthesis. In amino acid degradation, following the conversion of -ketoglutarate to glutamate, glutamate subsequently undergoes oxidative deamination to form ammonium ions, which are excreted as urea. In the reverse reaction, aspartate may be synthesized from oxaloacetate, which is a key intermediate in the citric acid cycle

Creatine kinase (CK), also known as creatine phosphokinase (CPK) or phospho-creatine kinase (and sometimes incorrectly as creatininekinase), is an enzyme (EC 2.7.3.2) expressed by various tissues and cell types. CK catalyses the conversion of creatine and consumes adenosine triphosphate (ATP) to create phosphocreatine (PCr) and adenosine diphosphate (ADP). This CK enzyme [2] reaction is reversible and thus ATP can be generated from PCr and ADP. In tissues and cells that consume ATP rapidly, especially skeletal muscle, but also brain, photoreceptor cells of the retina, hair cells of the inner ear,spermatozoa and smooth muscle, PCr serves as an energy reservoir for the rapid buffering and regeneration of ATP in situ, as well as for intracellular energy [3] [4] transport by the PCr shuttle or circuit. Thus creatine kinase is an important enzyme in such tissues. Clinically, creatine kinase is assayed in blood tests as a marker of myocardial infarction (heart attack), rhabdomyolysis (severe muscle breakdown),muscular dystrophy, the autoimmune myositides and in acute renal failure.

Functions[edit source]
The mitochondrial creatine kinase (CKm) is present in the mitochondrial intermembrane space, where it produces phosphocreatine (PCr) from mitochondrially generated ATP and creatine (Cr) imported from the cytosol. Apart from the two mitochondrial CK isoenzyme forms, that is, ubiquitous mtCK (present in non-

muscle tissues) and sarcomeric mtCK (present in sarcomeric muscle), there are three cytosolic CK isoforms present in the cytosol, depending on the tissue. Whereas MM-CK is expressed in sarcomeric muscle, that is, skeletal and cardiac muscle, MB-CK is expressed in cardiac muscle, and BB-CK is expressed in smooth muscle and in most non-muscle tissues. Mitochondrial mtCK and cytosolic CK are connected in a so-called PCr/Cr-shuttle or circuit. PCr generated by mtCK in mitochondria is shuttled to cytosolic CK that is coupled to ATP-dependent processes, e.g. ATPases, like acto-myosin ATPase for muscle contraction, or ion pumps, like the calcium pump for muscle relaxation. There, the bound cytosolic CK accepts the PCr shuttled through the cell and uses it to regenerate ATP, which can then be used as energy source by the ATPases. (CK is associated intimately with the ATPases, forming a functionally coupled microcompartment.) Thus, PCr is not only an energy buffer but also a cellular transport form of energy between subcellular sites of energy (ATP) production (mitochondria and glycolysis) and those of energy utilization (ATPases) A prothrombin time test measures how quickly your blood clots. Sometimes called a pro time test or PT test, a prothrombin time test uses a sample of your blood. Prothrombin is a protein produced by your liver that helps your blood to clot. When you bleed, a series of chemicals (clotting factors) activate in a stepwise fashion. The end result is a clot which stops the bleeding. One step in the process is prothrombin turning into another protein called thrombin. The prothrombin time test measures how well the clotting process works and how long it takes to occur.