glycerol-3-phosphate O-acyltransferase

{{infobox enzyme

| Name = glycerol-3-phosphate O-acyltransferase

| EC_number = 2.3.1.15

| CAS_number = 9029-96-3

| GO_code = 0004366

| image =

| width =

| caption =

}}

In enzymology, a glycerol-3-phosphate O-acyltransferase ({{EC number|2.3.1.15}}) is an enzyme that catalyzes the chemical reaction

:acyl-CoA + sn-glycerol 3-phosphate $\rightleftharpoons$ CoA + 1-acyl-sn-glycerol 3-phosphate

Thus, the two substrates of this enzyme are acyl-CoA and sn-glycerol 3-phosphate, whereas its two products are CoA and 1-acyl-sn-glycerol 3-phosphate.

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:sn-glycerol-3-phosphate 1-O-acyltransferase. Other names in common use include alpha-glycerophosphate acyltransferase, 3-glycerophosphate acyltransferase, ACP:sn-glycerol-3-phosphate acyltransferase, glycerol 3-phosphate acyltransferase, glycerol phosphate acyltransferase, glycerol phosphate transacylase, glycerophosphate acyltransferase, glycerophosphate transacylase, sn-glycerol 3-phosphate acyltransferase, and sn-glycerol-3-phosphate acyltransferase. This enzyme participates in glycerolipid metabolism and glycerophospholipid metabolism. The later pathways in human is part of the WikiPathways{{Cite journal|url=https://www.wikipathways.org/index.php/Pathway:WP2533|title=Glycerophospholipid Biosynthetic Pathway|date=2019-11-01|website=WikiPathways |last1=D |first1=Arturo Manzo-Fontes P. |last2=Bot |first2=Wikipathways Maintenance |last3=Summer-Kutmon |first3=Martina |last4=Willighagen |first4=Egon |last5=Slenter |first5=Denise |last6=Cirillo |first6=Elisa |last7=Dupuis |first7=Lauren J. |last8=Weitz |first8=Eric |last9=Lipids |first9=Conroy |last10=Hanspers |first10=Kristina }} machine readable pathway collection.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1IUQ}} and {{PDB link|1K30}}. Currently 4 different proteins are assigned to this reaction, [https://www.uniprot.org/uniprot/Q9HCL2 GPAT1], [https://www.uniprot.org/uniprot/Q6NUI2 GPAT2], [https://www.uniprot.org/uniprot/Q53EU6 GPAT3] and GPAT4. GPAT1 and 2 are considered mitochondrial proteins.{{Cite web|url=https://www.uniprot.org/uniprot/Q9HCL2|title=Uniprot|date=2019-11-01|website=UniProt}}{{Cite web|url=https://www.uniprot.org/uniprot/Q6NUI2|title=Uniprot|date=2019-11-01|website=UniProt}}

References

{{cite journal |author1 = Bertrams M |author2 =Heinz E | year = 1981 | title = Positional Specificity and Fatty Acid Selectivity of Purified sn-Glycerol 3-Phosphate Acyltransferases from Chloroplasts | journal = Plant Physiol. | volume = 68 | pages = 653–657 | doi = 10.1104/pp.68.3.653 | pmid=16661974 | issue = 3 | pmc = 425956}}
{{cite journal | doi = 10.1111/j.1432-1033.1983.tb07096.x | vauthors = Frentzen M, Heinz E, McKeon TA, Stumpf PK | year = 1983 | title = Specificities and selectivities of glycerol-3-phosphate acyltransferase and monoacylglycerol-3-phosphate acyltransferase from pea and spinach chloroplasts | journal = Eur. J. Biochem. | volume = 129 | pages = 629–36 | pmid = 6825679 | issue = 3 | doi-access = free }}
{{cite journal | vauthors = Green PR, Vanaman TC, Modrich P, Bell RM | year = 1983 | title = Partial NH2- and COOH-terminal sequence and cyanogen bromide peptide analysis of Escherichia coli sn-glycerol-3-phosphate acyltransferase | journal = J. Biol. Chem. | volume = 258 | pages = 10862–6 | pmid = 6350296 | issue = 18 | doi = 10.1016/S0021-9258(17)44355-9 | doi-access = free }}
{{cite journal | vauthors = Yamashita S, Numa S | year = 1972 | title = Partial purification and properties of glycerophosphate acyltransferase from rat liver. Formation of 1-acylglycerol 3-phosphate from sn-glycerol 3-phosphate and palmityl coenzyme A | journal = Eur. J. Biochem. | volume = 31 | pages = 565–73 | pmid = 4650158 | doi = 10.1111/j.1432-1033.1972.tb02566.x | issue = 3 | doi-access = free }}

Category:EC 2.3.1

Category:Enzymes of known structure