Enzymes
| UniProtKB help_outline | 5 proteins |
Reaction participants Show >> << Hide
- Name help_outline L-leucine Identifier CHEBI:57427 Charge 0 Formula C6H13NO2 InChIKeyhelp_outline ROHFNLRQFUQHCH-YFKPBYRVSA-N SMILEShelp_outline CC(C)C[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 45 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline D-leucine Identifier CHEBI:143079 Charge 0 Formula C6H13NO2 InChIKeyhelp_outline ROHFNLRQFUQHCH-RXMQYKEDSA-N SMILEShelp_outline [O-]C([C@@H](CC(C)C)[NH3+])=O 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:59396 | RHEA:59397 | RHEA:59398 | RHEA:59399 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
Related reactions help_outline
More general form(s) of this reaction
Publications
-
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.