Serine acetyltransferase

Function Serine acetyltransferase (SAT) catalyzes the reaction converting serine to O-acetyl-serine using acetyl-CoA as a cofactor. This reaction is the first step in the synthesis of cysteine in bacteria and plants. SAT is regulated by a feedback inhibition by ots end product - cysteine. Structural highlights The structure of the complex of SAT with its substrate serine suggest that and that . for (water molecules are shown as red spheres). Arg253 is important for the catalytic efficiency of SAT. Lys230 is required for the cofactor acetyl-CoA binding.

spinqualitylabelsall models Serine acetyltransferase complex with serine and phosphate (PDB code 4n69) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

3D structures of serine acetyltransferase3D structures of serine acetyltransferase

Updated on 15-November-2023

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• Serine acetyltransferase
  • 4n6a – sSAT – soybean
    
  • 1ssm, 1s80 – HiSAT – Haemophilus influenzae
    
  • 3p1b – EhSAT – Entamoeba histolyca
    
  • 4hzc – BaSAT – Brucella abortus
    
  • 3f1x – SAT – Bacterioides vulgatus
    
  • 6lcn – SAT – Planctopirus limnophila<br />
• Serine acetyltransferase complex with amino acid
  • 4n69 – sSAT + Ser
    
  • 1ssq – HiSAT + Cys
    
  • 1t3d – SAT + Cys – Escherichia coli
    
  • 3gvd – SAT + Cys – Yersinia pestis
    
  • 3p47, 7bw9 – EhSAT + Cys
    
  • 3q1x – EhSAT + Ser
    
  • 4h7o – SAT + Cys + Arg – Vibrio cholerae
    
  • 6jvu – SAT + Cys – Klebsiella pneumoniae
    
  • 7ra4 – NgSAT + Ser – Neisseria gonorrhoeae
    
  • 6wye – NgSAT + malate
    
  • 7e3y – SAT + Cys – Salmonella typhimurium
    
• Serine acetyltransferase complex with acetyl-CoA
  • 4n6b – sSAT + Acetyl CoA
    
  • 1sst – HiSAT + Acetyl CoA
    
  • 4hzd – BaSAT + Acetyl CoA