Disease relevance of plsB

• The DNA sequences encoding plsB and dgk loci of Escherichia coli [1].

High impact information on plsB

• In Escherichia coli, acylation of the 1-position of G3P is carried out by PlsB; however, the majority of bacteria lack a plsB gene and in others it is not essential [2].
• In view of a possible association of germin with cellular membranes, the most interesting relatedness of the germin sequence to the sequences of other proteins is an 80% homology between a decapeptide sequence in mature germin and a decapeptide sequence in Escherichia coli glycerol-3-phosphate acyltransferase [3].
• The gene encoding the Escherichia coli sn-glycerol-3-phosphate acyltransferase, plsB, was inserted into hybrid plasmids under transcriptional control of the lambda PL and tac promoters [4].
• The reacylation aspect of the turnover cycle was demonstrated by the incorporation of fatty acids into the 1-position of pre-existing phosphatidylethanolamine when de novo phospholipid biosynthesis was inhibited using the plsB acyltransferase mutant [5].
• The partial sequence analysis of the homogeneous sn-glycerol-3-phosphate acyltransferase is fully in accord with the primary structure inferred from the DNA sequence [6].

Chemical compound and disease context of plsB

• Partial NH2- and COOH-terminal sequence and cyanogen bromide peptide analysis of Escherichia coli sn-glycerol-3-phosphate acyltransferase [6].
• We found that the histidine and aspartate in block I, the glycine in block III, and the proline in block IV all play a role in E. coli GPAT catalysis [7].

Biological context of plsB

• The 806-amino acid sequence encoded within the longest open reading frame is in agreement with NH2-terminal sequences of the sn-glycerol-3-phosphate acyltransferase (Green, P., Vanaman, T. C., Modrich, P., and Bell, R. M. (1983) J. Biol. Chem. 258, 10862-10866), indicating that this is the structural gene for this protein [1].
• Analysis of amino acid motifs diagnostic for the sn-glycerol-3-phosphate acyltransferase reaction [7].
• A missense mutation accounts for the defect in the glycerol-3-phosphate acyltransferase expressed in the plsB26 mutant [8].
• The mrACBP was functionally active as shown by binding of cis-parinaroyl-CoA with high affinity, K(d) = 12 +/- 2 nM, at a single binding site, stimulating oleoyl-CoA utilization by microsomal glycerol-3-phosphate acyltransferase 3.2-fold and protecting oleoyl-CoA from microsomal acyl-CoA hydrolase [9].

Anatomical context of plsB

• This method also allowed measurement of the specific activities of the glycerol-P acyltransferase in membranes from a wild type E. coli strain and from plasmid-containing strains which express the plsB gene product to different extents [10].

Associations of plsB with chemical compounds

• Fatty acid metabolism in sn-glycerol-3-phosphate acyltransferase (plsB) mutants [11].
• Processing of the sn-glycerol-3-phosphate acyltransferase is apparently limited to the removal of the NH2-terminal formylmethionine [6].
• The advantages of these critical modifications are demonstrated with the membrane enzymes glycerol 3-phosphate acyltransferase and cytidine 5'-diphosphate-diglyceride hydrolase [12].
• There was no significant difference in the activities of glycerol-3-phosphate acyltransferase and phosphatidate phosphohydrolase between control and septic rats.(ABSTRACT TRUNCATED AT 250 WORDS)[13]

Analytical, diagnostic and therapeutic context of plsB

• Using Escherichia coli GPAT (PlsB) as a model acyltransferase, we examined the role of the highly conserved amino acid residues in blocks I-IV in GPAT activity through chemical modification and site-directed mutagenesis experiments [7].

References