Palmitoyl acyltransferase is a group of enzymes that transfer palmityl group to -SH group on cysteine on a protein. This modification increases the hydrophobicity of the protein, thereby increasing the association to plasma membrane or other intramembraneous compartments.

Contents

• Domain structure
• Substrate proteins
• Physiological Functions
• References

Domain structure

The palmitoyl acyltransferase was isolated and identified in 1999. The catalytic domain of the protein has aspartate-histidine-histidine-cysteine (DHHC) in the core and therefore is called DHHC domain.

Substrate proteins

The example of substrate includes H-Ras, N-ras, R-Ras, RhoB, Cdc42 inform 2, Rab10, Galpha subunit of trimeric GTP binding proteins, Src family tyrosine kinases, GAP53, eNOS, AMPA receptor subunit GluR1 and GluR2, GABA_A receptor gamma2 subunit, aquaporin, KV1.1, rhodopsin, beta2-adrenergic receptor, and PSD-95. https://swisspalm.org/enzymes

Physiological Functions

The protein palmitoylation is a reversible process. The addition of palmitoyl group increase the membrane association of the substrate protein while the removal by palmitoyl thioesterase decreases the membrane association.

References

• Draper, J. M.; Smith, C. D. (2009). "Palmitoyl acyltransferase assays and inhibitors (Review)". Molecular Membrane Biology. 26 (1): 5–13. doi:10.1080/09687680802683839. PMC   2635919 . PMID   19152182.
• Creaser, S. P.; Peterson, B. R. (2002). "Sensitive and rapid analysis of protein palmitoylation with a synthetic cell-permeable mimic of SRC oncoproteins". Journal of the American Chemical Society. 124 (11): 2444–2445. Bibcode:2002JAChS.124.2444C. doi:10.1021/ja017671x. PMID   11890786.