H
IPR016035

Acyl transferase/acyl hydrolase/lysophospholipase

InterPro entry
Short nameAcyl_Trfase/lysoPLipase
Overlapping entries
 

Description

This superfamily represents a structural domain with a 3-layer α/β/α topology. This domain can be found in acyl transferases such as bacterial malonyl-CoA ACP transacylase (FabD) and the homologous domain from eukaryotic fatty acid synthase
[1]
. This domain is also found in lysophospholipases such as cytosolic phospholipase A2 (which has additional structural features)
[2]
, and in patatin proteins, which are plant glycoproteins that act as non-specific lipid acyl hydrolases
[3]
.

References

1.Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase. Keatinge-Clay AT, Shelat AA, Savage DF, Tsai SC, Miercke LJ, O'Connell JD 3rd, Khosla C, Stroud RM. Structure 11, 147-54, (2003). View articlePMID: 12575934

2.Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism. Dessen A, Tang J, Schmidt H, Stahl M, Clark JD, Seehra J, Somers WS. Cell 97, 349-60, (1999). View articlePMID: 10319815

3.The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad. Rydel TJ, Williams JM, Krieger E, Moshiri F, Stallings WC, Brown SM, Pershing JC, Purcell JP, Alibhai MF. Biochemistry 42, 6696-708, (2003). View articlePMID: 12779324

Cross References

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