Enzymes
| UniProtKB help_outline | 105 proteins |
| Enzyme class help_outline |
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Reaction participants Show >> << Hide
- Name help_outline lipid IIA Identifier CHEBI:86226 Charge -2 Formula C73H137N3O26P2 InChIKeyhelp_outline TYGQMXOPLFWYPM-ISFHUDAKSA-L SMILEShelp_outline CCCCCCCCCCC[C@@H](O)CC(=O)N[C@H]1[C@@H](OP([O-])(=O)O[C@H]2OC[C@H]([NH3+])[C@H](O)[C@H]2O)O[C@H](CO[C@@H]2O[C@H](CO)[C@@H](OP([O-])([O-])=O)[C@H](OC(=O)C[C@H](O)CCCCCCCCCCC)[C@H]2NC(=O)C[C@H](O)CCCCCCCCCCC)[C@@H](O)[C@@H]1OC(=O)C[C@H](O)CCCCCCCCCCC 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine Identifier CHEBI:77369 Charge 0 Formula C25H49NO8PR SMILEShelp_outline CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 14 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline lipid IIB Identifier CHEBI:87058 Charge -2 Formula C89H167N3O27P2 InChIKeyhelp_outline KQPSNVBCBKBYRA-MVRMDACESA-L SMILEShelp_outline CCCCCCCCCCCCCCCC(=O)O[C@H](CCCCCCCCCCC)CC(=O)N[C@H]1[C@@H](OP([O-])(=O)O[C@H]2OC[C@H]([NH3+])[C@H](O)[C@H]2O)O[C@H](CO[C@@H]2O[C@H](CO)[C@@H](OP([O-])([O-])=O)[C@H](OC(=O)C[C@H](O)CCCCCCCCCCC)[C@H]2NC(=O)C[C@H](O)CCCCCCCCCCC)[C@@H](O)[C@@H]1OC(=O)C[C@H](O)CCCCCCCCCCC 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 2-acyl-sn-glycero-3-phosphocholine Identifier CHEBI:57875 Charge 0 Formula C9H19NO7PR SMILEShelp_outline C[N+](C)(C)CCOP([O-])(=O)OC[C@@H](CO)OC([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 99 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:46872 | RHEA:46873 | RHEA:46874 | RHEA:46875 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Transfer of palmitate from phospholipids to lipid A in outer membranes of gram-negative bacteria.
Bishop R.E., Gibbons H.S., Guina T., Trent M.S., Miller S.I., Raetz C.R.
Regulated covalent modifications of lipid A are implicated in virulence of pathogenic Gram-negative bacteria. The Salmonella typhimurium PhoP/PhoQ-activated gene pagP is required both for biosynthesis of hepta-acylated lipid A species containing palmitate and for resistance to cationic anti-microb ... >> More
Regulated covalent modifications of lipid A are implicated in virulence of pathogenic Gram-negative bacteria. The Salmonella typhimurium PhoP/PhoQ-activated gene pagP is required both for biosynthesis of hepta-acylated lipid A species containing palmitate and for resistance to cationic anti-microbial peptides. Palmitoylated lipid A can also function as an endotoxin antagonist. We now show that pagP and its Escherichia coli homolog (crcA) encode an unusual enzyme of lipid A biosynthesis localized in the outer membrane. PagP transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A (or its precursors). PagP bearing a C-terminal His(6)-tag accumulated in outer membranes during overproduction, was purified with full activity and was shown by cross-linking to behave as a homodimer. PagP is the first example of an outer membrane enzyme involved in lipid A biosynthesis. Additional pagP homologs are encoded in the genomes of Yersinia and Bordetella species. PagP may provide an adaptive response toward both Mg(2+) limitation and host innate immune defenses. << Less
EMBO J. 19:5071-5080(2000) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.
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PagP crystallized from SDS/cosolvent reveals the route for phospholipid access to the hydrocarbon ruler.
Cuesta-Seijo J.A., Neale C., Khan M.A., Moktar J., Tran C.D., Bishop R.E., Pomes R., Prive G.G.
Enzymatic reactions involving bilayer lipids occur in an environment with strict physical and topological constraints. The integral membrane enzyme PagP transfers a palmitoyl group from a phospholipid to lipid A in order to assist Escherichia coli in evading host immune defenses during infection. ... >> More
Enzymatic reactions involving bilayer lipids occur in an environment with strict physical and topological constraints. The integral membrane enzyme PagP transfers a palmitoyl group from a phospholipid to lipid A in order to assist Escherichia coli in evading host immune defenses during infection. PagP measures the palmitoyl group with an internal hydrocarbon ruler that is formed in the interior of the eight-stranded antiparallel β barrel. The access and egress of the palmitoyl group is thought to take a lateral route from the bilayer phase to the barrel interior. Molecular dynamics, mutagenesis, and a 1.4 A crystal structure of PagP in an SDS / 2-methyl-2,4-pentanediol (MPD) cosolvent system reveal that phospholipid access occurs at the crenel present between strands F and G of PagP. In this way, the phospholipid head group can remain exposed to the cell exterior while the lipid acyl chain remains in a predominantly hydrophobic environment as it translocates to the protein interior. << Less
Structure 18:1210-1219(2010) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.