IntEnz

EC 2.3.1.225 - Protein S-acyltransferase

IntEnz Enzyme Nomenclature
EC 2.3.1.225

Names

Reaction

• 36683 [IUBMB]
  [protein]-L-cysteine

  [protein]-L-cysteine

  GENERIC:10131

  Is ROOT: no
  ROOT compound: GENERIC:9624

  Number of residues: 1

  L-cysteine residue L-cysteine residue Name origin: UniProt - CHECKED (C) CHEBI:29950 Formula: C3H5NOS Charge: 0 Position: undefined ChEBI compound status: CHECKED (C)

  +

  hexadecanoyl-CoA

  hexadecanoyl-CoA

  Name origin: UniProt - CHECKED (C)

  CHEBI:57379

  Formula: C37H62N7O17P3S
  Charge: -4

  ChEBI compound status: CHECKED (C)

  

  =

  [protein]-S-hexadecanoyl-L-cysteine

  [protein]-S-hexadecanoyl-L-cysteine

  GENERIC:11032

  Is ROOT: no
  ROOT compound: GENERIC:9624

  Number of residues: 1

  S-palmitoyl-L-cysteine residue S-palmitoyl-L-cysteine residue Name origin: UniProt - CHECKED (C) CHEBI:74151 Formula: C19H35NO2S Charge: 0 Position: undefined ChEBI compound status: CHECKED (C)

  +

  CoA

  CoA

  Name origin: UniProt - CHECKED (C)

  CHEBI:57287

  Formula: C21H32N7O16P3S
  Charge: -4

  ChEBI compound status: CHECKED (C)

  

Comments:

The enzyme catalyses the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.

Links to other databases

References

1. Dunphy, J. T., Greentree, W. K., Manahan, C. L., Linder, M. E.
   G-protein palmitoyltransferase activity is enriched in plasma membranes.
   J. Biol. Chem. 271: 7154-7159 (1996). [PMID: 8636152]
2. Veit, M., Dietrich, L. E., Ungermann, C.
   Biochemical characterization of the vacuolar palmitoyl acyltransferase.
   FEBS Lett. 540: 101-105 (2003). [PMID: 12681491]
3. Batistic, O.
   Genomics and localization of the Arabidopsis DHHC-cysteine-rich domain S-acyltransferase protein family.
   Plant Physiol. 160: 1597-1612 (2012). [PMID: 22968831]
4. Jennings, B. C., Linder, M. E.
   DHHC protein S-acyltransferases use similar ping-pong kinetic mechanisms but display different acyl-CoA specificities.
   J. Biol. Chem. 287: 7236-7245 (2012). [PMID: 22247542]
5. Zhou, L. Z., Li, S., Feng, Q. N., Zhang, Y. L., Zhao, X., Zeng, Y. L., Wang, H., Jiang, L., Zhang, Y.
   Protein S-ACYL Transferase10 is critical for development and salt tolerance in Arabidopsis.
   Plant Cell 25: 1093-1107 (2013). [PMID: 23482856]

[EC 2.3.1.225 created 2013]