EC Number   |
General Information |
Reference |
|---|
    2.7.8.5 | malfunction |
an isolated pgp1/pgp2 double mutant pgp1-2 of Arabidopsis thaliana shows delayed embryo development, the majority of seeds from the mutant do not germinate, mutant thylakoid membranes do not develop in plastids, mitochondrial membrane structures are abnormal in the mutant embryos, and radiolabeling of phospholipids shows that radioactivity is not significantly incorporated into phosphatidylglycerol. Structures of chloroplasts and mitochondria in embryonic cells of pgp1-2 and pgp1-2pgp2, and phenotypes, detailed overview |
738231 |
| 2.7.8.5 | malfunction |
gene knockdown results in loss of phosphatidylglycerol and a reduction of another mitochondria-specific phospholipid, cardiolipin. Reduced enzyme expression in Trypanosoma brucei procyclic forms leads to alterations in mitochondrial morphology, reduction in the amounts of respiratory complexes III and IV and, ultimately, parasite death |
-, 723221 |
| 2.7.8.5 | malfunction |
overexpression of phosphatidylglycerophosphate synthase 1, PGS1, increases the cellular contents of phosphatidylglycerol, cardiolipin, and phosphatidylcholine, and reduces that of phosphatidic acid. PGS1 overexpression also elevates the mitochondrial contents of cardiolipin and phosphatidylcholine, but has no effect on the number of mitochondria per cell |
739659 |
| 2.7.8.5 | malfunction |
the Synechocystis sp.PCC 6803 pgsA mutant isdefective in PGPS activity |
-, 738290 |
| 2.7.8.5 | metabolism |
in mammalian cells, phosphatidylglycerol is produced from CDP-diacylglycerol (CDP-DAG) through two steps catalyzed by phosphatidylglycerophosphate (PGP) synthase and PGP phosphatase. CDP-DAG is formed from phosphatidic acid (PA) by the enzymes CDP-DAG synthase 1 and 2, which are integral membrane proteins located to mitochondria and endoplasmic reticulum. CDP-DAG is converted to PGP by the action of the mitochondrial enzyme PGP synthase 1 (PGS1) through the exchange of glycerol-3-phosphate (G3P) with CMP moiety of CDP-DAG. Phosphatidylglycerophosphate is rapidly dephosphorylated to generate phosphatidylglycerol |
739659 |
| 2.7.8.5 | metabolism |
phosphatidylglycerophosphate synthase catalyzes a committed step in the biosynthesis of phosphatidylglycerol |
738231 |
| 2.7.8.5 | metabolism |
phosphatidylglycerophosphate synthase, PGPS, is the rate-limiting enzyme in phosphatidylglycerophosphate biosynthesis in Chlamydomonas reinhardtii |
-, 738290 |
| 2.7.8.5 | physiological function |
CLS1 is not able to complement the growth phenotype of a phosphatidylglycerophosphate synthase mutant of Synechocystis sp. PCC6803, it rescues the temperature-sensitive growth phenotype, growth profile with different carbon sources, phospholipid composition and enzyme activity ofx02crd1, a CLS mutant of Saccharomyces cerevisiae |
761150 |
| 2.7.8.5 | physiological function |
distinct and overlapping function of PGPS in cyanobacteria and eukaryotic algae. Heterologous complementation of Synechocystis sp. PCC6803 gene pgsA mutant individually by CrPGP1 and CrPGP2 rescues the phosphatidylglycerophosphate-dependent growth phenotype, but the phosphatidylglycerophosphate level and its fatty acid composition are not fully rescued in the complemented strains. As well, oxygen evolution activity is not fully recovered, although electron transport activity of photosystem II is restored to the wild-type level, differential response of CrPGP1 and CrPGP2 expression to phosphorus and nitrogen deficiency. LipidCompositionof pgsA/CrPGP1 and pgsA/CrPGP2, the rescued mutant content is reduced compared to the wild-type, overview |
-, 738290 |
| 2.7.8.5 | physiological function |
in a PgsA deletion mutant, phosphatidylglycerol levels remain at about 0.1% of wild-type. When the growth medium is supplemented with glycerol, the expression of ClsB, a phospholipase D-type cardiolipin synthase, significantly increases phosphatidylglycerol and cardiolipin levels, with the growth deficiency of PgsA null strain also being complemented under such conditions |
761454 |
