Enzymes
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Reaction participants Show >> << Hide
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Namehelp_outline
L-alanyl-tRNAAla
Identifier
RHEA-COMP:9923
Reactive part
help_outline
- Name help_outline 3'-(L-alanyl)adenylyl group Identifier CHEBI:78497 Charge 0 Formula C13H18N6O7P SMILEShelp_outline C[C@H]([NH3+])C(=O)O[C@@H]1[C@@H](COP([O-])(-*)=O)O[C@H]([C@@H]1O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 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 46 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 1,2-diacyl-sn-glycero-3-phospho-1ʼ-(3ʼ-O-L-alanyl)-sn-glycerol Identifier CHEBI:75793 Charge 0 Formula C11H18NO11PR2 SMILEShelp_outline C[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
tRNAAla
Identifier
RHEA-COMP:9657
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 79 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:20489 | RHEA:20490 | RHEA:20491 | RHEA:20492 | |
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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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Participation of aminoacyl transfer ribonucleic acid in aminoacyl phosphatidylglycerol synthesis. II. Specificity of alanyl phosphatidylglycerol synthetase.
Gould R.M., Thornton M.P., Liepkalns V., Lennarz W.J.
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Broad range amino acid specificity of RNA-dependent lipid remodeling by multiple peptide resistance factors.
Roy H., Ibba M.
Aminoacylphosphatidylglycerol synthases (aaPGSs) are multiple peptide resistance factors that transfer amino acids from aminoacyl-tRNAs to phosphatidylglycerol (PG) in the cytoplasmic membrane. Aminoacylation of PG is used by bacteria to decrease the net negative charge of the cell envelope, dimin ... >> More
Aminoacylphosphatidylglycerol synthases (aaPGSs) are multiple peptide resistance factors that transfer amino acids from aminoacyl-tRNAs to phosphatidylglycerol (PG) in the cytoplasmic membrane. Aminoacylation of PG is used by bacteria to decrease the net negative charge of the cell envelope, diminishing affinity for charged molecules and allowing for adaptation to environmental changes. Lys-PGS, which transfers lysine to PG, is essential for the virulence of certain pathogens, providing resistance to both host cationic antimicrobial peptides and therapeutic antibiotics. Ala-PGS was also recently described, but little is known about the possible activities of other members of the highly diverse aaPGS family of proteins. Systematic deletion of the predicted membrane-inserted domains of several aaPGSs revealed that the carboxyl-terminal hydrophilic domain alone is sufficient for aminoacylphosphatidylglycerol transferase catalytic activity. In contrast to previously characterized aaPGSs, the Enterococcus faecium enzyme used an expanded repertoire of amino acids to modify PG with Ala, Arg, or Lys. Reexamination of previously characterized aaPGSs also revealed broader than anticipated substrate specificity, for example Bacillus subtilis Lys-PGS was shown to also catalyze Ala-PG synthesis. The relaxed substrate specificities of these aaPGSs allows for more elaborate remodeling of membrane lipids than previously thought, potentially providing bacteria that harbor these enzymes resistance to a broad spectrum of antibiotics and environmental stresses. << Less
J Biol Chem 284:29677-29683(2009) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.