Download MendeleyAnalysis of the structure, substrate specificity, and mechanism of squash glycerol-3-phosphate (1)-acyltransferase.
Turnbull, A.P., Rafferty, J.B., Sedelnikova, S.E., Slabas, A.R., Schierer, T.P., Kroon, J.T., Simon, J.W., Fawcett, T., Nishida, I., Murata, N., Rice, D.W.(2001) Structure 9: 347-353
- PubMed: 11377195
- DOI: https://doi.org/10.1016/s0969-2126(01)00595-0
- Primary Citation of Related Structures:
1K30 - PubMed Abstract:
Glycerol-3-phosphate (1)-acyltransferase(G3PAT) catalyzes the incorporation of an acyl group from either acyl-acyl carrier proteins (acylACPs) or acyl-CoAs into the sn-1 position of glycerol 3-phosphate to yield 1-acylglycerol-3-phosphate. G3PATs can either be selective, preferentially using the unsaturated fatty acid, oleate (C18:1), as the acyl donor, or nonselective, using either oleate or the saturated fatty acid, palmitate (C16:0), at comparable rates. The differential substrate specificity for saturated versus unsaturated fatty acids seen within this enzyme family has been implicated in the sensitivity of plants to chilling temperatures.
Organizational Affiliation:
The Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of Sheffield, S10 2TN, Sheffield, United Kingdom.
