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Editor-In-Chief: C. Michael Gibson, M.S., M.D. 
Aspartate transaminase (AST) also called serum glutamic oxaloacetic transaminase (SGOT) or aspartate aminotransferase (ASAT/AAT) (EC 184.108.40.206) is similar to alanine transaminase (ALT) in that it is another enzyme associated with liver parenchymal cells.
It facilitates the conversion of aspartate and alpha-ketoglutarate to oxaloacetate and glutamate.
Two isoenzymes are present in humans. They have high similarity.
- GOT1, the cytosolic isoenzyme derives mainly from red blood cells and heart.
- GOT2, the mitochondrial isoenzyme is predominantly present in liver.
It is raised in acute liver damage. It is also present in red blood cells and cardiac muscle.
AST was defined as a biochemical marker for the diagnosis of acute myocardial infarction in 1954. However the use of AST for such a diagnosis is now redundant and has been superseded by the cardiac troponins.
AST / ALT is commonly measured clinically as a part of a diagnostic liver function test, to determine liver health. This is because of hepatic deficiency of pyrodoxal-6-phosphate in alcoholics, which is a cofactor for the enzymatic activity of ALT.
Differential Diagnosis of Causes of Elevated AST
- Acute hepatitis
- Alcoholic hepatopathy
- Chronic active hepatitis
- Artemether and lumefantrin
- Asparaginase Erwinia Chrysanthemi
- Asenapine maleate
- Cefotaxime sodium
- Doxorubicin Hydrochloride
- Interferon gamma
- Lincomycin Hydrochloride
- Epstein-Barr Virus
- Fatty liver
- Hepatic tumor
- Hypothyroid myopathy
- Malignant hyperthermia
- Myocardial Infarction
- Open heart surgery
- Primary biliary cirrhosis
- Progressive myodystrophia
- Pulmonary Embolism
- Renal infarction
- Severe muscle trauma
- Spasms, muscle injuries
- Strong physical work
- Kuramitsu S, Okuno S, Ogawa T, Ogawa H, Kagamiyama H (1985). "Aspartate aminotransferase of Escherichia coli: nucleotide sequence of the aspC gene". J. Biochem. 97 (4): 1259–62. PMID 3897210.
- Kondo K, Wakabayashi S, Yagi T, Kagamiyama H (1984). "The complete amino acid sequence of aspartate aminotransferase from Escherichia coli: sequence comparison with pig isoenzymes". Biochem. Biophys. Res. Commun. 122 (1): 62–7. PMID 6378205.
- Inoue K, Kuramitsu S, Okamoto A, Hirotsu K, Higuchi T, Kagamiyama H (1991). "Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes". Biochemistry. 30 (31): 7796–801. PMID 1868057.
- Aspartate+Transaminase at the US National Library of Medicine Medical Subject Headings (MeSH)
de:Aspartat-Aminotransferase it:Aspartato transaminasi fi:Aspartaattiaminotransferaasi sv:Aspartataminotransferas