Document Detail


Enzymatic bases for the fatty acid positioning in phospholipids of Brevibacterium ammoniagenes.
MedLine Citation:
PMID:  3511845     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Positional distribution of fatty acids in phospholipids from Brevibacterium ammoniagenes was analyzed to find that phosphatidylethanolamine consisted mainly of 1-saturated acyl 2-unsaturated acyl species while phosphatidylglycerol consisted mainly of 1-unsaturated acyl 2-saturated acyl species. Three acyltransferase systems were characterized in a membrane preparation--the acylations of glycerophosphate, 1-acyl-glycerophosphate, and 2-acyl-glycerophosphate--which appeared to be catalyzed by different enzymes. The distribution of fatty acids in the phosphatidylethanolamine molecule was not correlated simply with the specificities of these enzymes, but the relatively high specificity for palmitoyl-CoA of the glycerophosphate acyltransferase system to form 2-acyl-glycerophosphate, followed the relatively high specificity for oleoyl-CoA of the 2-acyl-glycerophosphate acyltransferase system, provided a basis for producing the major molecular species of phosphatidylglycerol.
Authors:
Y Oh-Hashi; M Inoue; S Murase; M Mizuno; A Kawaguchi; H Okuyama
Related Documents :
16042405 - Acyl-coenzyme a binding protein expression alters liver fatty acyl-coenzyme a metabolism.
8660675 - Fatty acid amide biosynthesis: a possible new role for peptidylglycine alpha-amidating ...
7548115 - Palmitoleate formation by soybean stearoyl-acyl carrier protein desaturase.
9096315 - A novel arachidonate-preferring acyl-coa synthetase is present in steroidogenic cells o...
16461735 - Diversity of microorganisms within rock varnish in the whipple mountains, california.
17419595 - Computational study of the reaction between biogenic stabilized criegee intermediates a...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Archives of biochemistry and biophysics     Volume:  244     ISSN:  0003-9861     ISO Abbreviation:  Arch. Biochem. Biophys.     Publication Date:  1986 Feb 
Date Detail:
Created Date:  1986-03-13     Completed Date:  1986-03-13     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0372430     Medline TA:  Arch Biochem Biophys     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  413-20     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
1-Acylglycerol-3-Phosphate O-Acyltransferase
Acylation
Acyltransferases / analysis
Brevibacterium / metabolism*
Chromatography, Thin Layer
Escherichia coli / metabolism
Escherichia coli Proteins
Fatty Acids / metabolism*
Glycerol-3-Phosphate O-Acyltransferase / analysis
Glycerophosphates / metabolism
Kinetics
Mycobacterium / metabolism
Phospholipids / analysis,  metabolism*
Chemical
Reg. No./Substance:
0/Escherichia coli Proteins; 0/Fatty Acids; 0/Glycerophosphates; 0/Phospholipids; EC 2.3.-/Acyltransferases; 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 2.3.1.52/2-acylglycerophosphate acyltransferase

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


Previous Document:  Carbonyl reductase of dog liver: purification, properties, and kinetic mechanism.
Next Document:  Deoxyribonucleotide biosynthesis in yeast: assay and properties of ribonucleotide reductase in perme...