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MetaCyc Reaction: 2.3.1.51

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 2.3.1.51

Enzymes and Genes:

Escherichia coli K-12 substr. MG1655 : 1-acylglycerol-3-phosphate O-acyltransferase Inferred from experiment : plsC
Homo sapiens : 1-acyl-sn-glycerol-3-phosphate acyltransferase delta : AGPAT4
1-acyl-sn-glycerol-3-phosphate acyltransferase alpha : AGPAT1
1-acyl-sn-glycerol-3-phosphate acyltransferase beta : AGPAT2
1-acyl-sn-glycerol-3-phosphate acyltransferase gamma : AGPAT3
1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon : AGPAT5
Limnanthes douglasii : lysophosphatidate acyltransferase Inferred from experiment : LAT1
lysophosphatidate acyltransferase Inferred from experiment : LAT2
Pisum sativum : lysophosphatidate acyltransferase Inferred from experiment
Saccharomyces cerevisiae : 1-acyl-sn-gylcerol-3-phosphate acyl transferase : SLC1

In Pathway: CDP-diacylglycerol biosynthesis I , diacylglycerol and triacylglycerol biosynthesis

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, 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): 325.0658 Inferred 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 reaction of [a phosphatidylcholine + H2O → a 1-acyl 2-lyso-phosphatidylcholine + a long-chain fatty acid + H+] (3.1.1.4):
i7: 1,2-dipalmitoyl-phosphatidylcholine + H2O → 1-16:0-2-lysophosphatidylcholine + palmitate + H+ (3.1.1.4)

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):
i6: tributyrin + H2O → 1,2-dibutyrin + butanoate + H+ (3.1.1.3)

Instance reaction of [an L-1-phosphatidylethanolamine[periplasmic space] + H2O[periplasmic space] → a fatty acid[periplasmic space] + a 1-acyl 2-lyso-phosphatidylethanolamine[periplasmic space] + H+[periplasmic space]] (3.1.1.4):
i3: 1-18:1-2-18:1-phosphatidylethanolamine + H2O → 1-18:1-lysophosphatidylethanolamine + oleate + H+ (3.1.1.4)

Instance reactions of [a steryl-ester + H2O → a fatty acid + a sterol + H+] (3.1.1.13):
i4: ergosteryl oleate + H2O → ergosterol + oleate + H+ (3.1.1.13)

i5: lanosteryl oleate + H2O → lanosterol + oleate + H+ (3.1.1.13)

Unification Links: KEGG:R02241 , Rhea:19709

Relationship Links: BRENDA:EC:2.3.1.51 , ENZYME:EC:2.3.1.51 , IUBMB-ExplorEnz:EC:2.3.1.51


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


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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 SRI International Pathway Tools version 19.0 on Wed Aug 5, 2015, BIOCYC13A.