Enzymes
UniProtKB help_outline | 7,762 proteins |
Enzyme class help_outline |
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GO Molecular Function help_outline |
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Reaction participants Show >> << Hide
- Name help_outline 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) Identifier CHEBI:64716 Charge -1 Formula C8H12O10PR2 SMILEShelp_outline OC[C@H](O)COP([O-])(=O)OC[C@@H](COC([*])=O)OC([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 43 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
L-lysyl-tRNALys
Identifier
RHEA-COMP:9696
Reactive part
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- Name help_outline 3'-(L-lysyl)adenylyl group Identifier CHEBI:78529 Charge 1 Formula C16H26N7O7P SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(-*)=O)[C@@H](OC(=O)[C@@H]([NH3+])CCCC[NH3+])[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 1,2-diacyl-sn-glycero-3-phospho-1ʼ-(3ʼ-O-L-lysyl)-sn-glycerol Identifier CHEBI:75792 Charge 1 Formula C14H26N2O11PR2 SMILEShelp_outline [NH3+]CCCC[C@H]([NH3+])C(=O)OC[C@H](O)COP([O-])(=O)OC[C@@H](COC([*])=O)OC([*])=O 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
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Namehelp_outline
tRNALys
Identifier
RHEA-COMP:9697
Reactive part
help_outline
- Name help_outline AMP 3'-end residue Identifier CHEBI:78442 Charge -1 Formula C10H12N5O6P SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(-*)=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 67 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:10668 | RHEA:10669 | RHEA:10670 | RHEA:10671 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Substrate specificity of O-L-lysylphosphatidylglycerol synthetase. Enzymatic studies on the structure of O-L-lysylphosphatidylglycerol.
Lennarz W.J., Bonsen P.P., van Deenen L.L.
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MprF-mediated biosynthesis of lysylphosphatidylglycerol, an important determinant in staphylococcal defensin resistance.
Staubitz P., Neumann H., Schneider T., Wiedemann I., Peschel A.
Frequently bacteria are exposed to membrane-damaging cationic antimicrobial molecules (CAMs) produced by the host's immune system (defensins, cathelicidins) or by competing microorganisms (bacteriocins). Staphylococcus aureus achieves CAM resistance by modifying anionic phosphatidylglycerol with p ... >> More
Frequently bacteria are exposed to membrane-damaging cationic antimicrobial molecules (CAMs) produced by the host's immune system (defensins, cathelicidins) or by competing microorganisms (bacteriocins). Staphylococcus aureus achieves CAM resistance by modifying anionic phosphatidylglycerol with positively charged L-lysine, resulting in repulsion of the peptides. Inactivation of the novel S. aureus gene, mprF, which is found in many bacterial pathogens, has resulted in the loss of lysylphosphatidylglycerol (L-PG), increased inactivation by CAM-containing neutrophils, and attenuated virulence. We demonstrate here that expression of mprF is sufficient to confer L-PG production in Escherichia coli, which indicates that MprF represents the L-PG synthase. L-PG biosynthesis was studied in vitro and found to be dependent on phosphatidylglycerol and lysyl-tRNA, two putative substrate molecules. Further addition of cadaverin, a competitive inhibitor of the lysyl-tRNA synthetases, or of RNase A abolished L-PG biosynthesis, thereby confirming the involvement of lysyl-tRNA. This study forms the basis for further detailed analyses of L-PG biosynthesis and its role in bacterial infections. << Less