Document Detail


Thematic review series: Glycerolipids. Acyltransferases in bacterial glycerophospholipid synthesis.
MedLine Citation:
PMID:  18369234     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Phospholipid biosynthesis is a vital facet of bacterial physiology that begins with the synthesis of the fatty acids by a soluble type II fatty acid synthase. The bacterial glycerol-phosphate acyltransferases utilize the completed fatty acid chains to form the first membrane phospholipid and thus play a critical role in the regulation of membrane biogenesis. The first bacterial acyltransferase described was PlsB, a glycerol-phosphate acyltransferase. PlsB is a key regulatory point that coordinates membrane phospholipid formation with cell growth and macromolecular synthesis. Phosphatidic acid is then produced by PlsC, a 1-acylglycerol-phosphate acyltransferase. These two acyltransferases use thioesters of either CoA or acyl carrier protein (ACP) as the acyl donors and have homologs that perform the same reactions in higher organisms. However, the most prevalent glycerol-phosphate acyltransferase in the bacterial world is PlsY, which uses a recently discovered acyl-phosphate fatty acid intermediate as an acyl donor. This unique activated fatty acid is formed from the acyl-ACP end products of the fatty acid biosynthetic pathway by PlsX, an acyl-ACP:phosphate transacylase.
Authors:
Yong-Mei Zhang; Charles O Rock
Related Documents :
6761144 - Evidence that the acyl-o-esters are intermediates in the catalysis. the mechanism of ra...
24493274 - The incorporation of amino acids into the protein of isolated soya bean mitochondria.
3778684 - Mitochondrial acetoacetyl-coa thiolase deficiency.
20809284 - Lipase-catalyzed synthesis of two new antioxidants: 4-o- and 3-o-palmitoyl chlorogenic ...
14608614 - Electrospray mass spectrometric investigation of the binding of cis-parinaric acid to b...
993074 - Histochemistry of some acid hydrolases in striated muscles of the rat.
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review     Date:  2008-03-27
Journal Detail:
Title:  Journal of lipid research     Volume:  49     ISSN:  0022-2275     ISO Abbreviation:  J. Lipid Res.     Publication Date:  2008 Sep 
Date Detail:
Created Date:  2008-08-18     Completed Date:  2008-10-06     Revised Date:  2013-06-05    
Medline Journal Info:
Nlm Unique ID:  0376606     Medline TA:  J Lipid Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1867-74     Citation Subset:  IM    
Affiliation:
Department of Infectious Diseases, St. Jude Children's Research Hospital, Memphis, TN 38105, USA. yongmei.zhang@stjude.org
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
1-Acylglycerol-3-Phosphate O-Acyltransferase / metabolism
Acetyltransferases / genetics,  metabolism
Acyl Carrier Protein / metabolism
Acyltransferases / physiology*
Bacteria / enzymology
Bacterial Proteins / genetics,  metabolism
Escherichia coli Proteins / metabolism
Fatty Acid Synthetase Complex, Type II / metabolism*
Glycerol-3-Phosphate O-Acyltransferase / metabolism
Glycerophospholipids / biosynthesis*
Phylogeny
Grant Support
ID/Acronym/Agency:
CA 21765/CA/NCI NIH HHS; GM 34496/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Acyl Carrier Protein; 0/Bacterial Proteins; 0/Escherichia coli Proteins; 0/Glycerophospholipids; 0/plsX protein, bacteria; EC 2.3.-/Acyltransferases; EC 2.3.1.-/Acetyltransferases; EC 2.3.1.-/PlsB protein, E coli; EC 2.3.1.15/Glycerol-3-Phosphate O-Acyltransferase; EC 2.3.1.51/1-Acylglycerol-3-Phosphate O-Acyltransferase; EC 2.3.1.51/plsC protein, E coli; EC 6.-/Fatty Acid Synthetase Complex, Type II
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Maternal and paternal contribution to intergenerational recurrence of breech delivery: population ba...
Next Document:  Control of cholesteryl ester transfer protein activity by sequestration of lipid transfer inhibitor ...