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Phosphatidylcholine biosynthesis and function in bacteria.
Geiger, Otto; López-Lara, Isabel M; Sohlenkamp, Christian.
Affiliation
  • Geiger O; Centro de Ciencias Genómicas, Universidad Nacional Autónoma de México, Av. Universidad s/n, Apdo. Postal 565-A, Cuernavaca, Morelos, CP62210, Mexico. otto@ccg.unam.mx
Biochim Biophys Acta ; 1831(3): 503-13, 2013 Mar.
Article in En | MEDLINE | ID: mdl-22922101
ABSTRACT
Phosphatidylcholine (PC) is the major membrane-forming phospholipid in eukaryotes and is estimated to be present in about 15% of the domain Bacteria. Usually, PC can be synthesized in bacteria by either of two pathways, the phospholipid N-methylation (Pmt) pathway or the phosphatidylcholine synthase (Pcs) pathway. The three subsequent enzymatic methylations of phosphatidylethanolamine are performed by a single phospholipid N-methyltransferase in some bacteria whereas other bacteria possess multiple phospholipid N-methyltransferases each one performing one or several distinct methylation steps. Phosphatidylcholine synthase condenses choline directly with CDP-diacylglycerol to form CMP and PC. Like in eukaryotes, bacterial PC also functions as a biosynthetic intermediate during the formation of other biomolecules such as choline, diacylglycerol, or diacylglycerol-based phosphorus-free membrane lipids. Bacterial PC may serve as a specific recognition molecule but it affects the physicochemical properties of bacterial membranes as well. This article is part of a Special Issue entitled Phospholipids and Phospholipid Metabolism.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Phosphatidylcholines / Bacterial Proteins / Sinorhizobium meliloti / Agrobacterium tumefaciens Limits: Animals / Humans Language: En Journal: Biochim Biophys Acta Year: 2013 Document type: Article Affiliation country: Mexico

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Phosphatidylcholines / Bacterial Proteins / Sinorhizobium meliloti / Agrobacterium tumefaciens Limits: Animals / Humans Language: En Journal: Biochim Biophys Acta Year: 2013 Document type: Article Affiliation country: Mexico
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