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| Aspartate aminotransferase | |
|---|---|
 Aspartate aminotransferase. Aspartate aminotransferase from Escherichia coli bound with cofactor pyridoxal 5-phosphate (PDB 1AAM) |
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| Genetic data | |
| Gene code: | [1] ID#: GI:41011 |
| Protein Structure/Function | |
| Structure: | [2]1AAM |
Aspartate transaminase (AST) also called serum glutamic oxaloacetic transaminase (SGOT) or aspartate aminotransferase (ASAT/AAT) (EC 2.6.1.1) is similar to alanine transaminase (ALT) in that it is another enzyme associated with liver parenchymal cells.
Contents |
Function
It facilitates the conversion of aspartate and alpha-ketoglutarate to oxaloacetate and glutamate.
Isozymes
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.
Clinical significance
It is raised in acute liver damage. It is also present in red blood cells and cardiac muscle, skeletal muscle, and kidney and brain tissue, and may be elevated due to damage to those sources as well.
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 However the use of AST for such a diagnosis is now redundant and has been superseded by the cardiac troponins.[1]
AST (SGOT) is commonly measured clinically as a part of diagnostic liver function tests, to determine liver health.
References
- ^ Gaze DC (2007). "The role of existing and novel cardiac biomarkers for cardioprotection". Curr. Opin. Invest. Drugs 8 (9): 711–717. PMID 17729182.
Journal articles
- 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. doi:. 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. doi:. PMID 1868057.
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Wikipedia content modification information:
- This page was last modified on 22 June 2008, at 12:53.
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