Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.51 extracted from

  • Huang, L.; Yu, L.; Li, Z.; Li, Y.; Yoon, K.; Hu, Q.; Yuan, L.; Han, D.
    Microalgal plastidial lysophosphatidic acid acyltransferase interacts with upstream glycerol-3-phosphate acyltransferase and defines its substrate selectivity via the two transmembrane domains (2020), Algal Res., 45, 101758-101768 .
No PubMed abstract available
Search for more literature for 2.3.1.51

Cloned(Commentary)

Cloned (Comment) Organism
gene CHLREDRAFT_174358, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Chlamydomonas reinhardtii

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
 Chlamydomonas reinhardtii 9507
-
membrane CrLPAAT1 is an integral membrane protein with two potential transmembrane domains (TM), namely TM1 (residues 94-116) and TM2 (residues 188-205), along with a chloroplast transit peptide (cTP) of 46 amino acid residues at the N-terminus. The segment between cTP and TM1 is enriched with serine (Ser) and proline (Pro) residues, the Ser/Pro-rich domain together with a transmembrane alpha-helix might be a sorting/insertion signal for the post-import sorting pathway Chlamydomonas reinhardtii 16020
-
additional information putative topology models of CrLPAAT1, overview Chlamydomonas reinhardtii
-
-
plastid
-
 Chlamydomonas reinhardtii 9536
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, activates best at 5 mM Chlamydomonas reinhardtii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate Chlamydomonas reinhardtii
-
 CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Chlamydomonas reinhardtii A8J0J0 i.e. Chlamydomonas smithii
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration Chlamydomonas reinhardtii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the purified soluble recombinant CrLPAAT1 prefers C16:0-CoA over other acyl donors, whereas it shows broader substrate selectivity than the membrane-bound enzyme. Comparison of the wild-type CrLPAAT1 and the transmembrane domain-truncated enzyme revelas that the two transmembrane domains of CrLPAAT1 are involved in shaping its substrate preference for C16:0-CoA. The wild-type CrLPAAT1 can utilize C18:1 (n9)-LPA and C16:0- CoA to produce phosphatidic acid in a dosage-dependent manner. The transmembrane domains affect substrate selectivity, mechanism, detailed overview. The effect of two transmembrane domains of CrLPAAT1 is more dramatic on the selectivity on C16:0 than that on the other acyl-CoA substrates Chlamydomonas reinhardtii ?
-
-
palmitoyl-CoA + 1-(9Z)-octa-9-decenyl-lysophosphatidic acid
-
 Chlamydomonas reinhardtii CoA + 1-(9Z)-octa-9-decenyl-2-palmitoyl-lysophosphatidic acid
-
 ?
palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
-
 Chlamydomonas reinhardtii CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
-
 ?
palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate preferred acyl donor substrate Chlamydomonas reinhardtii CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
-
 ?

Subunits

Subunits Comment Organism
? x * 36200, about, sequence calculation Chlamydomonas reinhardtii

Synonyms

Synonyms Comment Organism
CHLREDRAFT_174358
-
 Chlamydomonas reinhardtii
CrLPAAT1
-
 Chlamydomonas reinhardtii
LPAAT
-
 Chlamydomonas reinhardtii
lysophosphatidic acid acyltransferase
-
 Chlamydomonas reinhardtii
plastidial LPAAT
-
 Chlamydomonas reinhardtii
plastidial lysophosphatidic acid acyltransferase
-
 Chlamydomonas reinhardtii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 recombinant enzyme Chlamydomonas reinhardtii

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 40 over 50% of maximal activity within this range, profilw overview Chlamydomonas reinhardtii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 7.5 recombinant enzyme, broad optimum Chlamydomonas reinhardtii

pH Range

pH Minimum pH Maximum Comment Organism
6.5 9 recombinant enzyme, over 90% of maximal activity at pH 6.5-7.5, 50% at pH 8.0, below 10% at pH 9.0 Chlamydomonas reinhardtii

General Information

General Information Comment Organism
metabolism the plastidial lysophosphatidic acid acyltransferase of the unicellular green alga Chlamydomonas reinhardtii (CrLPAAT1) is a key enzyme in triacylglycerol biosynthesis. In microalgae, de novo biosynthesis of triacylglycerol (TAG) via the Kennedy pathway involves successive acylation of glycerol-3-phosphate (G-3-P) by glycerol-3-phosphate acyltransferase (GPAT, EC 2.3.1.15), lysophosphatidic acid acyltransferase (LPAAT, EC 2.3.1.51), and diacylglycerol acyltransferase (DGAT, EC 2.3.1.20). Analysis of the affinity between CrLPAAT1 and CrGPATcl, binding kinetics. The strength of CrLPAAT1-CrGPATcl interaction varied with the pH values, which peaks in the neutral environment and is gradually diminished in both acidic and alkaline buffers. CrLPAAT1-CrGPATcl tend to be dissociated with the increased concentration of C18:1(n9)-LPA, whereas G-3-P has no effect on the interaction between these two proteins. Besides, the stability of CrLPAAT1-CrGPATcl complex is inversely proportional to the concentrations of acyl donors used in the assays, and it is found to be the most sensitive to the high-concentration of C18:1(n9)-CoA among various acyl donors Chlamydomonas reinhardtii
physiological function the plastidial lysophosphatidic acid acyltransferase of the unicellular green alga Chlamydomonas reinhardtii (CrLPAAT1) is a key enzyme involved in triacylglycerol biosynthesis Chlamydomonas reinhardtii