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Aspartate transaminase: Wikis


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aspartate transaminase
Aspartate aminotransferase from Escherichia coli bound with cofactor pyridoxal 5-phosphate.[1]
EC number
CAS number 9000-97-9
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures
Gene Ontology AmiGO / EGO

Aspartate transaminase (AST) also called serum glutamic oxaloacetic transaminase (SGOT) or aspartate aminotransferase (ASAT/AAT) (EC 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, and vice-versa.

Aspartate + α-ketoglutarate ⇌ oxaloacetate + glutamate


Two isoenzymes are present in humans. They have high similarity.

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 However the use of AST for such a diagnosis is now redundant and has been superseded by the cardiac troponins.[2]

AST (SGOT) is commonly measured clinically as a part of diagnostic liver function tests, to determine liver health.

Patient type Reference ranges[3]
Female 6 - 34 IU/L
Male 8 - 40 IU/L


  1. ^ PDB 1AAMAlmo SC, Smith DL, Danishefsky AT, Ringe D (March 1994). "The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli". Protein Eng. 7 (3): 405–12. PMID 7909946.  
  2. ^ Gaze DC (2007). "The role of existing and novel cardiac biomarkers for cardioprotection". Curr. Opin. Invest. Drugs 8 (9): 711–717. PMID 17729182.  
  3. ^ GPnotebook > reference range (AST) Retrieved on Dec 7, 2009

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:10.1016/0006-291X(84)90439-X. 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:10.1021/bi00245a019. PMID 1868057.  

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