Structural highlights
Function
GPAT2_CUCMO Esterifies the acyl-group from acyl-acyl carrier proteins (acyl-ACPs) to the sn-1 position of glycerol-3-phosphate (Ref.3). The physiological acyl donors in chloroplasts are acyl-ACPs, but acyl-CoAs are used as artificial donor for in vitro reactions (Probable). The enzyme from chilling-resistant plants discriminates against non-fluid palmitic acid and selects oleic acid whereas the enzyme from sensitive plants accepts both fatty acids (Ref.3). Squash is chilling-sensitive (Probable). Does not seem to discriminate between the acyl-ACP thioesters 18:1-ACP, 18:0-ACP and 16:0-ACP (Ref.3). Exhibits higher selectivity for 16:0-CoA than 18:1-CoA in vitro (PubMed:9016814, PubMed:14684887).[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Tamada T, Feese MD, Ferri SR, Kato Y, Yajima R, Toguri T, Kuroki R. Substrate recognition and selectivity of plant glycerol-3-phosphate acyltransferases (GPATs) from Cucurbita moscata and Spinacea oleracea. Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):13-21. Epub 2003, Dec 18. PMID:14684887
- ↑ Ferri SR, Toguri T. Substrate specificity modification of the stromal glycerol-3-phosphate acyltransferase. Arch Biochem Biophys. 1997 Jan 15;337(2):202-8. PMID:9016814 doi:10.1006/abbi.1996.9769
- ↑ Ferri SR, Toguri T. Substrate specificity modification of the stromal glycerol-3-phosphate acyltransferase. Arch Biochem Biophys. 1997 Jan 15;337(2):202-8. PMID:9016814 doi:10.1006/abbi.1996.9769
- ↑ Ferri SR, Toguri T. Substrate specificity modification of the stromal glycerol-3-phosphate acyltransferase. Arch Biochem Biophys. 1997 Jan 15;337(2):202-8. PMID:9016814 doi:10.1006/abbi.1996.9769