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Literature summary extracted from

  • Robertson, R.M.; Yao, J.; Gajewski, S.; Kumar, G.; Martin, E.W.; Rock, C.O.; White, S.W.
    A two-helix motif positions the active site of lysophosphatidic acid acyltransferase for catalysis within the membrane bilayer (2017), Nat. Struct. Mol. Biol., 24, 666-671 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.51 gene plsC, functional recombinant expression in and complementation of the Escherichia coli temperature-sensitive mutant strain SM2-1 (plsC(Ts)), growth at 30°C. Chlamydia trachomatis PlsC also complements growth at 42°C. TmPlsC expression in strain SM2-1 results in predominately 16:0/16:0 and 18:1/16:0 phospholipids, indicating a TmPlsC substrate selectivity for 16:0. Overexpression of C- or N-terminally His6-tagged wild-type and selenomethionine-substituted enzymes in Escherichia coli Thermotoga maritima

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.51 purified recombinant His-tagged selenomethionine-substituted enzyme TmPlsC, X-ray diffraction structure determination and analysis at 2.8-4.0 A resolution, method overview Thermotoga maritima

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.51 membrane the N-terminal two-helix motif associates with the membrane. Full-length TmPlsC is membrane-bound and not removed by a 0.5 M NaCl wash Thermotoga maritima 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.51 acyl-CoA + 1-acyl-sn-glycerol 3-phosphate Thermotoga maritima
-
 CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.51 acyl-CoA + 1-acyl-sn-glycerol 3-phosphate Thermotoga maritima DSM 3109
-
 CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.51 acyl-CoA + 1-acyl-sn-glycerol 3-phosphate Thermotoga maritima ATCC 43589
-
 CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.51 acyl-CoA + 1-acyl-sn-glycerol 3-phosphate Thermotoga maritima JCM 10099
-
 CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.51 Thermotoga maritima Q9X219
-
-
2.3.1.51 Thermotoga maritima ATCC 43589 Q9X219
-
-
2.3.1.51 Thermotoga maritima DSM 3109 Q9X219
-
-
2.3.1.51 Thermotoga maritima JCM 10099 Q9X219
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.51 recombinant C- or N-terminally His6-tagged enzyme from Escherichia coli from the detergent solubilized membrane fraction by nickel affinity chromatography and gel filtration in presence of n-dodecyl-beta-D-maltoside Thermotoga maritima

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.51 acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
-
 Thermotoga maritima CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.51 acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
-
 Thermotoga maritima DSM 3109 CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.51 acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
-
 Thermotoga maritima ATCC 43589 CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.51 acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
-
 Thermotoga maritima JCM 10099 CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.51 additional information TmPlsC expression in Escherichia coli strain SM2-1 results in predominately 16:0/16:0 and 18:1/16:0 phospholipids, indicating a TmPlsC substrate selectivity for 16:0, analysis of acyl chain specificity, overview. Substrate tight association with the alphabeta catalytic domain is crucial to the function of the enzyme, an active site tunnel includes residues Tyr20, Ile21, Gly25, Ile49 and Phe52 from the N-terminal two-helix motif Thermotoga maritima ?
-
-
2.3.1.51 additional information TmPlsC expression in Escherichia coli strain SM2-1 results in predominately 16:0/16:0 and 18:1/16:0 phospholipids, indicating a TmPlsC substrate selectivity for 16:0, analysis of acyl chain specificity, overview. Substrate tight association with the alphabeta catalytic domain is crucial to the function of the enzyme, an active site tunnel includes residues Tyr20, Ile21, Gly25, Ile49 and Phe52 from the N-terminal two-helix motif Thermotoga maritima DSM 3109 ?
-
-
2.3.1.51 additional information TmPlsC expression in Escherichia coli strain SM2-1 results in predominately 16:0/16:0 and 18:1/16:0 phospholipids, indicating a TmPlsC substrate selectivity for 16:0, analysis of acyl chain specificity, overview. Substrate tight association with the alphabeta catalytic domain is crucial to the function of the enzyme, an active site tunnel includes residues Tyr20, Ile21, Gly25, Ile49 and Phe52 from the N-terminal two-helix motif Thermotoga maritima ATCC 43589 ?
-
-
2.3.1.51 additional information TmPlsC expression in Escherichia coli strain SM2-1 results in predominately 16:0/16:0 and 18:1/16:0 phospholipids, indicating a TmPlsC substrate selectivity for 16:0, analysis of acyl chain specificity, overview. Substrate tight association with the alphabeta catalytic domain is crucial to the function of the enzyme, an active site tunnel includes residues Tyr20, Ile21, Gly25, Ile49 and Phe52 from the N-terminal two-helix motif Thermotoga maritima JCM 10099 ?
-
-
2.3.1.51 palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
-
 Thermotoga maritima CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.51 palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
-
 Thermotoga maritima DSM 3109 CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.51 palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
-
 Thermotoga maritima ATCC 43589 CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.51 palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
-
 Thermotoga maritima JCM 10099 CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.51 palmitoyl-[acyl carrier protein] + 1-acyl-sn-glycerol 3-phosphate
-
 Thermotoga maritima acyl carrier protein + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.51 palmitoyl-[acyl carrier protein] + 1-acyl-sn-glycerol 3-phosphate
-
 Thermotoga maritima DSM 3109 acyl carrier protein + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.51 palmitoyl-[acyl carrier protein] + 1-acyl-sn-glycerol 3-phosphate
-
 Thermotoga maritima ATCC 43589 acyl carrier protein + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.51 palmitoyl-[acyl carrier protein] + 1-acyl-sn-glycerol 3-phosphate
-
 Thermotoga maritima JCM 10099 acyl carrier protein + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.51 More TmPlsC comprises two domains: residues 1-61 create a distinctive N-terminal two-helix motif, and the C-terminal residues 62-247 form an alphabeta domain comprising a seven stranded beta-sheet core surrounded by five alpha-helices and four 310 helices. All four conserved motifs within the AGPAT family are within the alphabeta domain. The N-terminal two-helix motif comprises an anti-parallel two-helix bundle (alpga1 and alpha2). The HX4D catalytic motif is positioned in a deep cleft that is the dominant surface feature of TmPlsC Thermotoga maritima

Synonyms

EC Number Synonyms Comment Organism
2.3.1.51 1-acyl-sn-glycero-3-phosphate acyltransferase
-
 Thermotoga maritima
2.3.1.51 LPAAT
-
 Thermotoga maritima
2.3.1.51 lysophosphatidic acid acyltransferase
-
 Thermotoga maritima
2.3.1.51 PlsC
-
 Thermotoga maritima
2.3.1.51 TmPlsC
-
 Thermotoga maritima
2.3.1.51 TM_1693
-
 Thermotoga maritima

General Information

EC Number General Information Comment Organism
2.3.1.51 evolution the LPAAT/PlsC enzymes belong to the evolutionarily conserved lysophospholipid acyltransferase (AGPAT) family of intrinsic membrane proteins. TmPlsC comprises two domains: residues 1-61 create a distinctive N-terminal two-helix motif, and the C-terminal residues 62-247 form an alphabeta domain comprising a seven stranded beta-sheet core surrounded by five alpha-helices and four 310 helices. All four conserved motifs within the AGPAT family are within the alphabeta domain. The N-terminal two-helix motif comprises an anti-parallel two-helix bundle (alpga1 and alpha2), structure comparisons, e.g. with soluble plant GPATs (EC 2.3.1.15), overview Thermotoga maritima
2.3.1.51 metabolism phosphatidic acid is the central intermediate in membrane phospholipid synthesis and is generated by two acyltransferases in a pathway conserved in all life forms. The second step in this pathway is catalyzed by 1-acyl-sn-glycero-3-phosphate acyltransferase, called PlsC in bacteria Thermotoga maritima
2.3.1.51 additional information a two-helix motif positions the active site of lysophosphatidic acid acyltransferase is required for catalysis within the membrane bilayer. The structure of PlsC shows an unusual hydrophobic/aromatic N-terminal two-helix motif linked to an acyltransferase alphabeta domain that contains the catalytic HX4D motif. Molecular dynamics simulations reveal that the two-helix motif represents a substructure that firmly anchors the protein to one leaflet of the membrane. This binding mode allows the PlsC active site to acylate lysophospholipids within the membrane bilayer using soluble acyl donors. Catalytic mechanism and substrate binding sites, overview Thermotoga maritima
2.3.1.51 physiological function enzyme PlsC dictates the acyl chain composition of the 2-position of phospholipids, and the acyl chain selectivity ruler is an appropriately placed and closed hydrophobic tunnel Thermotoga maritima