2.7.8.43 1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + lipid A low activity, addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A Neisseria meningitidis 1,2-dihexanoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate) - ? 433068 2.7.8.43 1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + lipid A low activity, addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A Neisseria meningitidis 1,2-dihexanoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 433069 2.7.8.43 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine + monoolein - Neisseria meningitidis serogroup B 1,2-dioleoyl-sn-glycerol + 2-oleoyl-sn-glycero-1-phosphoethanolamine - ? 458811 2.7.8.43 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine + monoolein - Neisseria meningitidis serogroup B MC58 1,2-dioleoyl-sn-glycerol + 2-oleoyl-sn-glycero-1-phosphoethanolamine - ? 458811 2.7.8.43 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A Neisseria meningitidis 1,2-dipalmitoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate) - ? 432558 2.7.8.43 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A Neisseria meningitidis 1,2-dipalmitoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432559 2.7.8.43 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + monoolein - Neisseria meningitidis serogroup B 1,2-dipalmitoyl-sn-glycerol + 2-oleoyl-sn-glycero-1-phosphoethanolamine - ? 458816 2.7.8.43 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + monoolein - Neisseria meningitidis serogroup B MC58 1,2-dipalmitoyl-sn-glycerol + 2-oleoyl-sn-glycero-1-phosphoethanolamine - ? 458816 2.7.8.43 1-acyl-2-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]dodecanoyl]-sn-glycero-3-phosphoethanolamine + alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A - Neisseria meningitidis serogroup B 1-acyl-2-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]dodecanoyl]-sn-glycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A - ? 458834 2.7.8.43 1-acyl-2-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]dodecanoyl]-sn-glycero-3-phosphoethanolamine + alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A - Neisseria meningitidis serogroup B MC58 1-acyl-2-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]dodecanoyl]-sn-glycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A - ? 458834 2.7.8.43 diacylphosphatidylethanolamine + alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A - Cronobacter sakazakii diacylglycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A - ? 433631 2.7.8.43 diacylphosphatidylethanolamine + alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A - Cronobacter sakazakii BAA894 diacylglycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A - ? 433631 2.7.8.43 diacylphosphatidylethanolamine + arbutin arbutin is a substrate for the phosphoethanolamine transferase Escherichia coli diacylglycerol + ? - ? 439491 2.7.8.43 diacylphosphatidylethanolamine + flagellar rod protein FlgG - Campylobacter jejuni ? - ? 432761 2.7.8.43 diacylphosphatidylethanolamine + flagellar rod protein FlgG FlgG is modified at a single site Thr75, EptC is unable to modify other amino acids (e.g. serine and tyrosine), mass spectroscopic analysis, overview Campylobacter jejuni ? - ? 432761 2.7.8.43 diacylphosphatidylethanolamine + flagellar rod protein FlgG usage of recombinant C-terminally His6-tagged substrate protein Campylobacter jejuni ? - ? 432761 2.7.8.43 diacylphosphatidylethanolamine + flagellar rod protein FlgG EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto Thr75 of FlgG proteins Campylobacter jejuni ? - ? 432761 2.7.8.43 diacylphosphatidylethanolamine + flagellar rod protein FlgG - Campylobacter jejuni 81-176 ? - ? 432761 2.7.8.43 diacylphosphatidylethanolamine + flagellar rod protein FlgG FlgG is modified at a single site Thr75, EptC is unable to modify other amino acids (e.g. serine and tyrosine), mass spectroscopic analysis, overview Campylobacter jejuni 81-176 ? - ? 432761 2.7.8.43 diacylphosphatidylethanolamine + flagellar rod protein FlgG EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto Thr75 of FlgG proteins Campylobacter jejuni 81-176 ? - ? 432761 2.7.8.43 diacylphosphatidylethanolamine + lipid A a phosphoethanolamine unit is directly linked to the 1-position of the disaccharide backbone of lipid A Helicobacter pylori ? - ? 432762 2.7.8.43 diacylphosphatidylethanolamine + lipid A - Helicobacter pylori diacylglycerol + lipid A 1-(2-aminoethyl diphosphate) - ? 432763 2.7.8.43 diacylphosphatidylethanolamine + lipid A - Campylobacter jejuni diacylglycerol + lipid A 1-(2-aminoethyl diphosphate) - ? 432763 2.7.8.43 diacylphosphatidylethanolamine + lipid A - [Haemophilus] ducreyi diacylglycerol + lipid A 1-(2-aminoethyl diphosphate) - ? 432763 2.7.8.43 diacylphosphatidylethanolamine + lipid A - Escherichia coli diacylglycerol + lipid A 1-(2-aminoethyl diphosphate) - ? 432763 2.7.8.43 diacylphosphatidylethanolamine + lipid A addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A Neisseria gonorrhoeae diacylglycerol + lipid A 1-(2-aminoethyl diphosphate) - ? 432763 2.7.8.43 diacylphosphatidylethanolamine + lipid A addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A Salmonella enterica diacylglycerol + lipid A 1-(2-aminoethyl diphosphate) - ? 432763 2.7.8.43 diacylphosphatidylethanolamine + lipid A EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto the LOS core and phosphates of lipid A Campylobacter jejuni diacylglycerol + lipid A 1-(2-aminoethyl diphosphate) - ? 432763 2.7.8.43 diacylphosphatidylethanolamine + lipid A addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A Neisseria gonorrhoeae FA19 diacylglycerol + lipid A 1-(2-aminoethyl diphosphate) - ? 432763 2.7.8.43 diacylphosphatidylethanolamine + lipid A addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A Salmonella enterica LT2 diacylglycerol + lipid A 1-(2-aminoethyl diphosphate) - ? 432763 2.7.8.43 diacylphosphatidylethanolamine + lipid A - Campylobacter jejuni 81-176 diacylglycerol + lipid A 1-(2-aminoethyl diphosphate) - ? 432763 2.7.8.43 diacylphosphatidylethanolamine + lipid A EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto the LOS core and phosphates of lipid A Campylobacter jejuni 81-176 diacylglycerol + lipid A 1-(2-aminoethyl diphosphate) - ? 432763 2.7.8.43 diacylphosphatidylethanolamine + lipid A - [Haemophilus] ducreyi ATCC 700724 diacylglycerol + lipid A 1-(2-aminoethyl diphosphate) - ? 432763 2.7.8.43 diacylphosphatidylethanolamine + lipid A - Neisseria gonorrhoeae diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A - Neisseria meningitidis diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A - Campylobacter jejuni diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A - Pseudomonas aeruginosa diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A - [Haemophilus] ducreyi diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A - Escherichia coli diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A Neisseria gonorrhoeae diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A Salmonella enterica diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A Neisseria meningitidis diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A the phosphoethanolamine transferase is specific for the 4'-phosphate residue of Cronobacter sakazakii lipid A Cronobacter sakazakii diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A Pseudomonas aeruginosa lipid A, enzyme EptAPa-dependent addition of pEtN to the 4' phosphate group of BN2 and PA14 lipid A Pseudomonas aeruginosa diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto the LOS core and phosphates of lipid A Campylobacter jejuni diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A - Neisseria meningitidis NMB diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A Neisseria gonorrhoeae FA19 diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A Salmonella enterica LT2 diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A the phosphoethanolamine transferase is specific for the 4'-phosphate residue of Cronobacter sakazakii lipid A Cronobacter sakazakii BAA894 diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A - Neisseria gonorrhoeae FA 1090 diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A Neisseria gonorrhoeae FA 1090 diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A - Campylobacter jejuni 81-176 diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A - [Haemophilus] ducreyi ATCC 700724 diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate) - ? 432764 2.7.8.43 diacylphosphatidylethanolamine + lipid A - Neisseria meningitidis diacylglycerol + lipid A (2-aminoethyl diphosphate) - ? 438315 2.7.8.43 diacylphosphatidylethanolamine + lipid A - Shewanella algae diacylglycerol + lipid A (2-aminoethyl diphosphate) - ? 438315 2.7.8.43 diacylphosphatidylethanolamine + lipid A - Shewanella algae MARS 14 diacylglycerol + lipid A (2-aminoethyl diphosphate) - ? 438315 2.7.8.43 diacylphosphatidylethanolamine + lipid A - Neisseria meningitidis NMB diacylglycerol + lipid A (2-aminoethyl diphosphate) - ? 438315 2.7.8.43 diacylphosphatidylethanolamine + O-antigen serotype 4av - Shigella flexneri diacylglycerol + O-antigen serotype 4av (2-aminoethyl diphosphate) the serotype 4av O-antigen has the phosphoethanolamine at position 3 of RhaIII (major) or both RhaII and RhaIII (minor) ? 438316 2.7.8.43 diacylphosphatidylethanolamine + O-antigen serotype Xv - Shigella flexneri diacylglycerol + O-antigen serotype Xv (2-aminoethyl diphosphate) the serotype Xv O-antigen has the phosphoethanolamine on RhaII ? 438317 2.7.8.43 diacylphosphatidylethanolamine + O-antigen serotype Xv - Shigella flexneri diacylglycerol + O-antigen serotype Xv (2-aminoethyl diphosphate) in serotype Yv, mono- and bisphosphorylated O-units generate a block-copolymeric structure, the former being partially O-acetylated at position 6 of GlcNAc and the latter lacking O-acetylation. The serotype Xv O-antigen has the phosphoethanolamine on RhaII ? 438317 2.7.8.43 diacylphosphatidylethanolamine + O-antigen serotype Yv - Shigella flexneri diacylglycerol + O-antigen serotype Yv 3-(2-aminoethyl diphosphate) the serotype Yv O-antigen has the same basic carbohydrate backbone structure as that of the classical serotype Y, but differs in the presence of phosphoethanolamine at position 3 of RhaIII (major) or both RhaII and RhaIII (minor) ? 438318 2.7.8.43 additional information enzyme EptC catalyzes the addition of phosphoethanolamine to the first heptose sugar (Hep I) of the inner core oligosaccharide of Campylobacter jejuni lipooligosaccharide Campylobacter jejuni ? - ? 89 2.7.8.43 additional information enzyme LptA modifies lipid A with phosphoethanolamine, mass spectrometric analysis. Haemophilus ducreyi lipopolysaccharide contains one phosphoethanolamine on its lipid A and one phosphoethanolamine on its core oligosaccharide [Haemophilus] ducreyi ? - ? 89 2.7.8.43 additional information in all meningococcal strains examined, each lipid A species contains the basal diphosphorylated species, wherein a phosphate group is attached to each glucosamine residue. Also elaborated within the population of lipopolysacchride molecules are a variety of phosphoforms that contain either an additional phosphate residue, an additional phosphoethanolamine residue, additional phosphate and phosphoethanolamine residues, or an additional phosphate and two phosphoethanolamine residues in the lipid A, mass spectroscopic analyses, overview Neisseria meningitidis ? - ? 89 2.7.8.43 additional information lipid A of Helicobacter pylori lacks a 4'-phosphate group and is tri- or tetra-acylated with either (R)-3-hydroxystearate (C18) or (R)-3-hydroxypalmitate (C16), the C-1 hydroxyl group of the proximal glucosamine is derivatized with a phosphoethanolamine residue. This is in contrast with the phoshoethanolamine units of Escherichia coli, Salmonella typhimurium, and Neisseria meningitidis, which are attached to the lipid A phosphate group to form a pyrophosphate linkage. A minor lipid A species found in Helicobacter pylori is both bisphosphorylated and hexa-acylated resembling enterobacterial lipid As Helicobacter pylori ? - ? 89 2.7.8.43 additional information the enzyme modifies lipid A with one or two phosphoethanolamine moieties. Six lipid A substrate subtypes, St1 to St6, from wild type Salmonella typhimurium are covalently modified with one or two 4-amino-4-deoxy-L-arabinose moieties. Each lipid A species with a defined set of polar modifications can be further derivatized with a palmitoyl moiety and/or a 2-hydroxymyristoyl residue in place of the secondary myristoyl chain at position 3', high resolution NMR spectroscopy and mass spectrometry analysis of lipid A profiles from wild-type strain 14028 and mutant strains, overview Salmonella enterica subsp. enterica serovar Typhimurium ? - ? 89 2.7.8.43 additional information the lipid A of Campylobacter jejuni is characterized by longer secondary acyl chains attached to the 2' and 3' positions of the molecule and by the addition of phosphoethanolamine to the phosphate groups attached at the 1 and 4' positions of the disaccharide backbone. The disaccharide backbone of Campylobacter jejuni lipid A is not composed solely of glucosamine residues, but can be replaced with the analogue 2,3-diamino-2,3-dideoxy-D-glucopyranose Campylobacter jejuni ? - ? 89 2.7.8.43 additional information addition of phosphoethanolamine to hepta-acylated lipid A Acinetobacter baumannii ? - ? 89 2.7.8.43 additional information enzyme EptA catalyses the periplasmic addition of the positively charged substituent phosphoethanolamine to lipid A controlled by the PmrA transcriptional regulator and conferring resistance to cationic antimicrobial peptides, including polymyxin Salmonella enterica ? - ? 89 2.7.8.43 additional information enzyme EptA or PmrC catalyses the periplasmic addition of the positively charged substituent phosphoethanolamine to lipid A controlled by the PmrA transcriptional regulator and conferring resistance to cationic antimicrobial peptides, including polymyxin Escherichia coli ? - ? 89 2.7.8.43 additional information in Neisseria meningitidis, phosphatidylethanolamine typically has acyl chains of C12 and C14 with the first position being occupied with a saturated chain and the second being unsaturated. The recombinant soluble periplasmic domain of the enzyme is active in an aqueous assay but unable to add phoshoethanolamine to lipid A in Escherichia coli strains, lipid A profiles, overview Neisseria meningitidis ? - ? 89 2.7.8.43 additional information phosphoethanolamine substitution at both the 1 and 4' positions of lipid A, component of lipooligosaccharide. Lipooligosaccharide structure analysis by MALDI-TOF mass spectrometry, overview Neisseria gonorrhoeae ? - ? 89 2.7.8.43 additional information pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins Campylobacter jejuni ? - ? 89 2.7.8.43 additional information the phosphoethanolamine cycle, overview Escherichia coli ? - ? 89 2.7.8.43 additional information enzyme activity assays on the membrane-deleted LptA are performed using 4-nitrophenyl phosphoethanolamine, p-NPPE, as the substrate analogue, the enzyme is capable of cleaving the phosphoethanolamine portion from the p-NPPE chromogenic substrate Neisseria meningitidis ? - ? 89 2.7.8.43 additional information lipid A substrate and product analysis by MALDI-TOF/MS. The lipidA preparations from transgenic Escherichia coli strains carrying EptA show additional ions due to the addition of phosphoethanolamine to the bis-phosphorylatedstructure and the hepta-acylated structure Shewanella algae ? - ? 89 2.7.8.43 additional information NMR spectroscopic analysis of O-antigen substrates and products, detailed overview Shigella flexneri ? - ? 89 2.7.8.43 additional information quantitative analysis of binding of LPS by LptA, 1:1 ratio for the LPS:LptA complex, and structure analysis of the LPS binding pocket. The entire LptA protein is affected by LPS binding, the N-terminus unfolds in the presence of LPS Escherichia coli ? - ? 89 2.7.8.43 additional information specific LPS interactions with LptA and LptC Escherichia coli ? - ? 89 2.7.8.43 additional information transfer may occur both to the 4'- and 1-phospho groups of lipid A Escherichia coli ? - - 89 2.7.8.43 additional information the enzyme modifies lipid A with one or two phosphoethanolamine moieties. Six lipid A substrate subtypes, St1 to St6, from wild type Salmonella typhimurium are covalently modified with one or two 4-amino-4-deoxy-L-arabinose moieties. Each lipid A species with a defined set of polar modifications can be further derivatized with a palmitoyl moiety and/or a 2-hydroxymyristoyl residue in place of the secondary myristoyl chain at position 3', high resolution NMR spectroscopy and mass spectrometry analysis of lipid A profiles from wild-type strain 14028 and mutant strains, overview Salmonella enterica subsp. enterica serovar Typhimurium ATCC 14028 ? - ? 89 2.7.8.43 additional information lipid A substrate and product analysis by MALDI-TOF/MS. The lipidA preparations from transgenic Escherichia coli strains carrying EptA show additional ions due to the addition of phosphoethanolamine to the bis-phosphorylatedstructure and the hepta-acylated structure Shewanella algae MARS 14 ? - ? 89 2.7.8.43 additional information enzyme activity assays on the membrane-deleted LptA are performed using 4-nitrophenyl phosphoethanolamine, p-NPPE, as the substrate analogue, the enzyme is capable of cleaving the phosphoethanolamine portion from the p-NPPE chromogenic substrate Neisseria meningitidis NMB ? - ? 89 2.7.8.43 additional information phosphoethanolamine substitution at both the 1 and 4' positions of lipid A, component of lipooligosaccharide. Lipooligosaccharide structure analysis by MALDI-TOF mass spectrometry, overview Neisseria gonorrhoeae FA19 ? - ? 89 2.7.8.43 additional information enzyme EptA catalyses the periplasmic addition of the positively charged substituent phosphoethanolamine to lipid A controlled by the PmrA transcriptional regulator and conferring resistance to cationic antimicrobial peptides, including polymyxin Salmonella enterica LT2 ? - ? 89 2.7.8.43 additional information enzyme EptC catalyzes the addition of phosphoethanolamine to the first heptose sugar (Hep I) of the inner core oligosaccharide of Campylobacter jejuni lipooligosaccharide Campylobacter jejuni 81-176 ? - ? 89 2.7.8.43 additional information pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins Campylobacter jejuni 81-176 ? - ? 89