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Literature summary for 2.3.1.51 extracted from

  • Benghezal, M.; Roubaty, C.; Veepuri, V.; Knudsen, J.; Conzelmann, A.
    SLC1 and SLC4 encode partially redundant acyl-coenzyme A 1-acylglycerol-3-phosphate O-acyltransferases of budding yeast (2007), J. Biol. Chem., 282, 30845-30855.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain HB101, transformed into Saccharomyces cerevisiae, strains, plasmids and sources of parent vectors listed Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Saccharomyces cerevisiae 16020
-
microsome
-
Saccharomyces cerevisiae
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
61180
-
partially purified Slc1p, SDS-PAGE, Western Blot Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate Saccharomyces cerevisiae acyltranferase activity by Slc1p and Slc4p CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate Saccharomyces cerevisiae Slc1p and Slc4p both active as acyltransferases, involved in fatty acid exchange of mature glycerophospholipids CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P33333 16 strains, genotypes listed
-
Saccharomyces cerevisiae Q08548 16 strains, genotypes listed
-

Purification (Commentary)

Purification (Comment) Organism
partially purified, gel filtration Saccharomyces cerevisiae

Source Tissue

Source Tissue Comment Organism Textmining
cell culture
-
Saccharomyces cerevisiae
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
deletion of Slc1p alone not lethal, microsomal enzyme activity not completely lost, evidence for additional enzyme activity, comparison between Slc1p with Slc4p, single mutants of Slc1p and Slc4p generated, double mutant of Slc1p and Slc4p lethal, same glycerophospholipid profiles but different lipid profiles between Slc1p and Slc4p, both enzymes able to use endogenous lysoglycerophospholipids as substrates, substrate specificity between Slc1p and Slc4p different or access to different lysoglycerophospholipid substrates because of a different subcellular location, Slc1p and Slc4p are both active as acyltransferases and are also involved in fatty acid exchange at the sn-2-position of mature glycerophospholipids Saccharomyces cerevisiae
additional information
-
microsomal enzyme activity not completely lost by deletion of Slc1p, evidence for additional enzyme activity, SLC4 gene encodes second enzmye indicated by lethality of double mutants of Slc1p and Slc4p, same glycerophospholipid profile but different lipid profiles between Slc1p and Slc4p, different substrate specificity between Slc1p and Slc4p or access to different lysoglycerophospholipid substrates because of a different subcellular location Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate acyltranferase activity by Slc1p and Slc4p Saccharomyces cerevisiae CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate Slc1p and Slc4p both active as acyltransferases, involved in fatty acid exchange of mature glycerophospholipids Saccharomyces cerevisiae CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate glycerophospholipid profile similar between Slc1p and Slc4p Saccharomyces cerevisiae CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
?

Synonyms

Synonyms Comment Organism
1-acylglycerol 3-phosphate O-acyltransferase
-
Saccharomyces cerevisiae
Slc1p
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Saccharomyces cerevisiae
Slc4p
-
Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
activity assay at Saccharomyces cerevisiae