Enzymes
UniProtKB help_outline | 1 proteins |
Reaction participants Show >> << Hide
- Name help_outline L-lysine Identifier CHEBI:32551 Charge 1 Formula C6H15N2O2 InChIKeyhelp_outline KDXKERNSBIXSRK-YFKPBYRVSA-O SMILEShelp_outline [NH3+]CCCC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 65 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline D-lysine Identifier CHEBI:32557 Charge 1 Formula C6H15N2O2 InChIKeyhelp_outline KDXKERNSBIXSRK-RXMQYKEDSA-O SMILEShelp_outline [NH3+]CCCC[C@@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:22864 | RHEA:22865 | RHEA:22866 | RHEA:22867 | |
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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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Structural basis for the broad specificity of a new family of amino-acid racemases.
Espaillat A., Carrasco-Lopez C., Bernardo-Garcia N., Pietrosemoli N., Otero L.H., Alvarez L., de Pedro M.A., Pazos F., Davis B.M., Waldor M.K., Hermoso J.A., Cava F.
Broad-spectrum amino-acid racemases (Bsrs) enable bacteria to generate noncanonical D-amino acids, the roles of which in microbial physiology, including the modulation of cell-wall structure and the dissolution of biofilms, are just beginning to be appreciated. Here, extensive crystallographic, mu ... >> More
Broad-spectrum amino-acid racemases (Bsrs) enable bacteria to generate noncanonical D-amino acids, the roles of which in microbial physiology, including the modulation of cell-wall structure and the dissolution of biofilms, are just beginning to be appreciated. Here, extensive crystallographic, mutational, biochemical and bioinformatic studies were used to define the molecular features of the racemase BsrV that enable this enzyme to accommodate more diverse substrates than the related PLP-dependent alanine racemases. Conserved residues were identified that distinguish BsrV and a newly defined family of broad-spectrum racemases from alanine racemases, and these residues were found to be key mediators of the multispecificity of BrsV. Finally, the structural analysis of an additional Bsr that was identified in the bioinformatic analysis confirmed that the distinguishing features of BrsV are conserved among Bsr family members. << Less
Acta Crystallogr. D 70:79-90(2014) [PubMed] [EuropePMC]
This publication is cited by 12 other entries.
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A periplasmic, pyridoxal-5'-phosphate-dependent amino acid racemase in Pseudomonas taetrolens.
Matsui D., Oikawa T., Arakawa N., Osumi S., Lausberg F., Stabler N., Freudl R., Eggeling L.
The pyridoxal-5'-phosphate (PLP)-dependent amino acid racemases occur in almost every bacterium but may differ considerably with respect to substrate specificity. We here isolated the cloned broad substrate specificity racemase ArgR of Pseudomonas taetrolens from Escherichia coli by classical proc ... >> More
The pyridoxal-5'-phosphate (PLP)-dependent amino acid racemases occur in almost every bacterium but may differ considerably with respect to substrate specificity. We here isolated the cloned broad substrate specificity racemase ArgR of Pseudomonas taetrolens from Escherichia coli by classical procedures. The racemase was biochemically characterized and amongst other aspects it was confirmed that it is mostly active with lysine, arginine and ornithine, but merely weakly active with alanine, whereas the alanine racemase of the same organism studied in comparison acts on alanine only. Unexpectedly, sequencing the amino-terminal end of ArgR revealed processing of the protein, with a signal peptide cleaved off. Subsequent localization studies demonstrated that in both P. taetrolens and E. coli ArgR activity was almost exclusively present in the periplasm, a feature so far unknown for any amino acid racemase. An ArgR-derivative carrying a carboxy-terminal His-tag was made and this was demonstrated to localize even in an E. coli mutant devoid of the twin-arginine translocation (Tat) pathway in the periplasm. These data indicate that ArgR is synthesized as a prepeptide and translocated in a Tat-independent manner. We therefore propose that ArgR translocation depends on the Sec system and a post-translocational insertion of PLP occurs. As further experiments showed, ArgR is necessary for the catabolism of D: -arginine and D: -lysine by P. taetrolens. << Less
Appl. Microbiol. Biotechnol. 83:1045-1054(2009) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.