EC Number |
General Information |
Reference |
---|
2.3.1.274 | malfunction |
depletion of PlsX does not affect cell division if phospholipid synthesis is maintained by an alternative enzyme |
-, 748665 |
2.3.1.274 | malfunction |
repression of slr1510 increases octadecanol productivity threefold over the base strain. Accumulation of fatty alcohols impairs growth, alters the membrane composition, and causes a build-up of reactive oxygen species |
748558 |
2.3.1.274 | metabolism |
cooverexpression of native phospholipid-biosynthetic genes plsX and plsC enhances lipid production in Synechocystis sp. PCC 6803 |
749362 |
2.3.1.274 | metabolism |
PlsX is a central enzyme of phospholipid synthesis in bacteria, converting acyl-ACP to acyl-phosphate on the pathway to phosphatidic acid formation. PlsX plays a key role in the coordination of fatty acid and phospholipid synthesis |
-, 748665 |
2.3.1.274 | metabolism |
the enzyme coordinates the production of fatty acids and membrane phospholipids |
-, 748508 |
2.3.1.274 | metabolism |
the enzyme is involved in phosphatidic acid synthesis |
748558 |
2.3.1.274 | metabolism |
the enzyme is involved in phospholipid biosynthesis |
-, 747421 |
2.3.1.274 | more |
substrate recognition and catalytic mechanism of phosphate acyltransferase PlsX, docking simulation, detailed overview. Conservation of potential active-site residues, sequence comparisons. The suspected ACP docking site is formed by Arg73 and Arg120 |
-, 756464 |