Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
twitter

MetaCyc Reaction: 2.3.1.51

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsProtein-Modification Reactions
Reactions Classified By SubstrateMacromolecule ReactionsProtein-ReactionsProtein-Modification Reactions

EC Number: 2.3.1.51

Enzymes and Genes:

Arabidopsis thaliana col: lysophosphatidate acyltransferaseInferred from experiment: ATS2
Escherichia coli K-12 substr. MG1655: 1-acylglycerol-3-phosphate O-acyltransferaseInferred from experiment: plsC
Saccharomyces cerevisiae: 1-acyl-sn-gylcerol-3-phosphate acyl transferase: SLC1
Streptococcus pneumoniae R6: 1-acylglycerol-3-phosphate acyltransferaseInferred from experiment: plsC

In Pathway: CDP-diacylglycerol biosynthesis III, CDP-diacylglycerol biosynthesis II

Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name: 1-acylglycerol-3-phosphate O-acyltransferase

Enzyme Commission Synonyms: 1-acyl-sn-glycero-3-phosphate acyltransferase, 1-acyl-sn-glycerol 3-phosphate acyltransferase, 1-acylglycero-3-phosphate acyltransferase, 1-acylglycerolphosphate acyltransferase, 1-acylglycerophosphate acyltransferase, lysophosphatidic acid-acyltransferase

Standard Gibbs Free Energy (ΔrG in kcal/mol): -3.6099854Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Acyl-[acyl-carrier protein] can also act as an acyl donor. The animal enzyme is specific for the transfer of unsaturated fatty acyl groups.

Citations: [Frentzen83, Hill68, Yamashita73]

Gene-Reaction Schematic

Gene-Reaction Schematic

Instance reactions of [a steryl-ester + H2O → a fatty acid + a sterol + H+] (3.1.1.13):
i3: ergosteryl oleate + H2O → ergosterol + oleate + H+ (3.1.1.13)

i4: lanosteryl oleate + H2O → lanosterol + oleate + H+ (3.1.1.13)

Instance reaction of [an acyl-CoA + a 1-acyl 2-lyso-phosphatidylcholine ↔ a phosphatidylcholine + coenzyme A] (2.3.1.23):
i1: palmitoyl-CoA + 1-16:0-2-lysophosphatidylcholine ↔ 1,2-dipalmitoyl-phosphatidylcholine + coenzyme A (2.3.1.23)

Instance reaction of [a triglyceride + H2O → a 1,2-diglyceride + a fatty acid + H+] (3.1.1.3):
i5: tributyrin + H2O → 1,2-dibutyrin + butanoate + H+ (3.1.1.3)

Instance reactions of [a long-chain acyl-CoA + a 1-acyl-sn-glycerol 3-phosphate → a 1,2-diacyl-sn-glycerol 3-phosphate + coenzyme A] (2.3.1.51):
i8: cis-vaccenoyl-CoA + 1-cis-vaccenoylglycerol-3-phosphate → 1,2-dicis-vaccenoyl-phosphatidate + coenzyme A (2.3.1.51)

i9: cis-vaccenoyl-CoA + 1-palmitoylglycerol 3-phosphate → 1-palmitoyl-2-cis-vaccenoyl phosphatidate + coenzyme A (2.3.1.51)

i10: palmitoleoyl-CoA + 1-myristoylglycerol 3-phosphate → 1-myristoyl-2-palmitoleoyl phosphatidate + coenzyme A (2.3.1.51)

i11: palmitoleoyl-CoA + 1-cis-vaccenoylglycerol-3-phosphate → 1-cis-vaccenoyl-2-palmitoleoyl phosphatidate + coenzyme A (2.3.1.51)

i12: palmitoleoyl-CoA + 1-palmitoylglycerol 3-phosphate → 1-palmitoyl-2-palmitoleoyl phosphatidate + coenzyme A (2.3.1.51)

i13: 1-palmitoylglycerol 3-phosphate + myristoyl-CoA → 1-palmitoyl-2-myristoyl phosphatidate + coenzyme A (2.3.1.51)

i14: myristoyl-CoA + 1-myristoylglycerol 3-phosphate → dimyristoyl phosphatidate + coenzyme A (2.3.1.51)

Unification Links: KEGG:R09381

Relationship Links: BRENDA:EC:2.3.1.51, ENZYME:EC:2.3.1.51, IUBMB-ExplorEnz:EC:2.3.1.51, UniProt:RELATED-TO:O07584, UniProt:RELATED-TO:O07807, UniProt:RELATED-TO:O07808, UniProt:RELATED-TO:O07809, UniProt:RELATED-TO:O25903, UniProt:RELATED-TO:O35083, UniProt:RELATED-TO:O53516, UniProt:RELATED-TO:O84459, UniProt:RELATED-TO:P0A257, UniProt:RELATED-TO:P26647, UniProt:RELATED-TO:P44848, UniProt:RELATED-TO:P74498, UniProt:RELATED-TO:P75479, UniProt:RELATED-TO:Q9JU41, UniProt:RELATED-TO:Q9KP63, UniProt:RELATED-TO:Q9PHZ5, UniProt:RELATED-TO:Q9RRA7, UniProt:RELATED-TO:Q9S2M2, UniProt:RELATED-TO:Q9US20, UniProt:RELATED-TO:Q9XDL6, UniProt:RELATED-TO:Q9Z7Y4, UniProt:RELATED-TO:Q9ZBS1, UniProt:RELATED-TO:Q9ZD75, UniProt:RELATED-TO:Q9ZJN8, UniProt:RELATED-TO:Q22267, UniProt:RELATED-TO:Q42870, UniProt:RELATED-TO:Q49402, UniProt:RELATED-TO:Q59188, UniProt:RELATED-TO:Q59601, UniProt:RELATED-TO:Q59618, UniProt:RELATED-TO:Q93841


References

Frentzen83: Frentzen M, Heinz E, McKeon TA, Stumpf PK (1983). "Specificities and selectivities of glycerol-3-phosphate acyltransferase and monoacylglycerol-3-phosphate acyltransferase from pea and spinach chloroplasts." Eur J Biochem 129(3);629-36. PMID: 6825679

Hill68: Hill EE, Lands WE (1968). "Incorporation of long-chain and polyunsaturated acids into phosphatidate and phosphatidylcholine." Biochim Biophys Acta 152(3);645-8. PMID: 5661029

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Yamashita73: Yamashita S, Hosaka K, Numa S (1973). "Acyl-donor specificities of partially purified 1-acylglycerophosphate acyltransferase, 2-acylglycerophosphate acyltransferase and 1-acylglycerophosphorylcholine acyltransferase from rat-liver microsomes." Eur J Biochem 38(1);25-31. PMID: 4774123


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Sun Feb 7, 2016, biocyc11.