Literature summary extracted from

Hayman, M.W.; Fawcett, T.; Schierer, T.F.; Simon, J.W.; Kroon, J.T.M.; Gilroy, J.S.; Rice, D.W.; Rafferty, J.; Turnbull, A.P.; Sedelnikova, S.E.; Slabas, A.R.
Mutagenesis of squash (Cucurbita moschata) glycerol-3-phosphate acyltransferase (GPAT) to produce an enzyme with altered substrate selectivity (2000), Biochem. Soc. Trans., 28, 680-681.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
2.3.1.15	expression in Escherichia coli	Arabidopsis thaliana
2.3.1.15	expression of wild-type and PCR-mutated cDNA in Escherichia coli	Cucurbita moschata

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.3.1.15	Arabidopsis thaliana	-	-	-
2.3.1.15	Cucurbita moschata	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.3.1.15	oleoyl-CoA + sn-glycerol 3-phosphate	-	Cucurbita moschata	CoA + 1-oleoyl-sn-glycerol 3-phosphate	-	?
2.3.1.15	oleoyl-CoA + sn-glycerol 3-phosphate	preferred over palmitoyl-CoA with a ratio of approx. 3:1	Arabidopsis thaliana	CoA + 1-oleoyl-sn-glycerol 3-phosphate	-	?
2.3.1.15	palmitoyl-CoA + sn-glycerol 3-phosphate	wild-type acyltransferase uses palmitoyl-CoA and oleoyl-CoA at comparable rates, recombinant mutant acyltransferase prefers oleoyl-CoA	Cucurbita moschata	CoA + 1-palmitoyl-sn-glycerol 3-phosphate	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)