EC Number   |
General Information |
Reference |
|---|
    2.3.1.51 | evolution |
PrLPAAT1 may be a member of AGPAT family, and may have acyltransferase activity, comparisons of sequences, genetic structures, and conserved structure motifs, overview. Phylogenetic analysis |
755824 |
| 2.3.1.51 | evolution |
the enzyme belongs to the acyl-CoA:1-acylglycerol-sn-3-phosphate acyltranferases (AGPAT) family, PrLPAAT4 possesses a 1-acyl-sn-glycerol-3-phosphate acyltransferase-related domain, it is subordinated to cluster III. Comparative analysis of gene structure and conserved domain in the LPAAT4 proteins |
757715 |
| 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 |
-, 757793 |
| 2.3.1.51 | malfunction |
deletion of the SlPlsC1 gene causes a marked decrease in the amounts of eicosapentaenoic acid (EPA)-containing phospholipids, without significantly altering the composition of other phospholipids. The EPA-containing phospholipids play an important role in survival of the bacterium in a cold environment |
-, 748130 |
| 2.3.1.51 | malfunction |
enzyme knockdown inhibits proliferation and anchorage-independent growth of pancreatic cancer cells |
737122 |
| 2.3.1.51 | malfunction |
enzyme-deficient mice develop widespread disturbances of metabolism, sperm development, and neurologic function resulting from disrupted phospholipid homeostasis. Enzyme-deficient mice have reduced body weight, total body fat, and plasma leptin level and show features of epilepsy. Neonatal enzyme-deficient mice have minor alterations in lipid synthesis and reduced plasma glucose levels. Enzyme-deficient males and females mice have reproductive abnormalities |
756599 |
| 2.3.1.51 | malfunction |
in a plsC4-disrupted mutant, phospholipids (PLs) containing 13:0 found in the parental strain are almost completely absent. The loss of these PLs is suppressed by introduction of a plsC4-expression plasmid. PLs containing 15:0 are also drastically decreased by plsC4 disruption |
-, 755967 |
| 2.3.1.51 | malfunction |
in cultured adipocytes, knockdown of AGPAT2 reduces TG synthesis and increased lyso-PA channeling into phospholipids |
756108 |
| 2.3.1.51 | malfunction |
in enzyme AGPAT2 defiecient mice, reduces TG synthesis and increased lyso-PA channeling into phospholipids is observed. In Agpat2-/- mouse liver, hepatic steatosis is driven by increased fatty acid synthesis and diversion of lyso-PA to TG and phospholipids by a mechanism independent of monoacylglycerol acyltransferase 1 (MGAT1) activity. The increase in phospholipid synthesis might be due to an alternate AGPAT-dependent pathway |
756108 |
| 2.3.1.51 | malfunction |
mutations in human CGI-58/ABHD5 cause Chanarin-Dorfman syndrome, characterized by excessive storage of triacylglycerol in tissues |
705011 |
