Aspartate transaminase

Frae Wikipedia
Jump to navigation Jump to search
aspartate transaminase
Aspartate transaminase.png
Aspartate aminotransferase frae Escherichia coli boond wi cofactor pyridoxal 5-phosphate.[1]
Identifiers
EC nummer 2.6.1.1
CAS nummer 9000-97-9
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structurs RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

Aspartate transaminase (AST) or aspartate aminotransferase, an aa kent as AspAT/ASAT/AAT or serum glutamic oxaloacetic transaminase (SGOT), is a pyridoxal phosphate (PLP)-dependent transaminase enzyme (EC 2.6.1.1) that wis first descrived bi Arthur Karmen an colleagues in 1954.[2][3][4]

References[eedit | eedit soorce]

  1. PDB: 1AAM Almo SC, Smith DL, Danishefsky AT, Ringe D (Mairch 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): 405–412. doi:10.1093/protein/7.3.405. PMID 7909946. 
  2. KARMEN, A; WROBLEWSKI, F; LADUE, JS (Januar 1955). "Transaminase activity in human blood". The Journal of Clinical Investigation. 34 (1): 126–31. doi:10.1172/jci103055. PMC 438594Freely accessible. PMID 13221663. 
  3. KARMEN, A (Januar 1955). "A note on the spectrometric assay of glutamic-oxalacetic transaminase in human blood serum". The Journal of Clinical Investigation. 34 (1): 131–3. doi:10.1172/JCI103055. PMC 438594Freely accessible. PMID 13221664. 
  4. LADUE, JS; WROBLEWSKI, F; KARMEN, A (24 September 1954). "Serum glutamic oxaloacetic transaminase activity in human acute transmural myocardial infarction". Science. 120 (3117): 497–9. doi:10.1126/science.120.3117.497. PMID 13195683.