Serine acetyltransferase

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spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image 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[1]. SAT is regulated by a feedback inhibition by ots end product - cysteine. Structural highlights

3D structures of serine acetyltransferase

Updated on 21-November-2018 {{#tree:id=OrganizedByTopic|openlevels=0|

• Serine acetyltransferase

• • 4n6a – sSAT – soybean
    
  • 1ssm, 1s80 – HiSAT – Haemophilus influenzae
    
  • 3p1b – EhSAT – Entamoeba histolyca
    
  • 4hzc – BaSAT – Brucella abortus
    
  • 3f1x – SAT – Bacterioides vulgatus
    

• Serine acetyltransferase complex with amino acid

• • 1ssq – HiSAT + cysteine
    
  • 4n69 – sSAT + serine
    
  • 1t3d – SAT + cysteine – Escherichia coli
    
  • 3gvd – SAT + cysteine – Yersinia pestis
    
  • 3p47 – EhSAT + cysteine
    
  • 3q1x – EhSAT + serine
    
  • 4h7o – SAT + cysteine + arginine – Vibrio cholerae
    

• Serine acetyltransferase complex with acetyl-CoA

• • 1sst – HiSAT + Acetyl CoA
    
  • 4n6b – sSAT + Acetyl CoA
    
  • 4hzd – BaSAT + Acetyl CoA
    

References

1. ↑ Gerlt JA, Babbitt PC, Rayment I. Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity. Arch Biochem Biophys. 2005 Jan 1;433(1):59-70. doi: 10.1016/j.abb.2004.07.034. PMID:15581566 doi:http://dx.doi.org/10.1016/j.abb.2004.07.034