Enzymes
UniProtKB help_outline | 4 proteins |
Reaction participants Show >> << Hide
- Name help_outline L-tryptophan Identifier CHEBI:57912 Charge 0 Formula C11H12N2O2 InChIKeyhelp_outline QIVBCDIJIAJPQS-VIFPVBQESA-N SMILEShelp_outline [NH3+][C@@H](Cc1c[nH]c2ccccc12)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 56 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:70947 | RHEA:70948 | RHEA:70949 | RHEA:70950 | |
---|---|---|---|---|
Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
|
|||
MetaCyc help_outline | ||||
Reactome help_outline |
Publications
-
YddG from Escherichia coli promotes export of aromatic amino acids.
Doroshenko V., Airich L., Vitushkina M., Kolokolova A., Livshits V., Mashko S.
The inner membrane protein YddG of Escherichia coli is a homologue of the known amino acid exporters RhtA and YdeD. It was found that the yddG gene overexpression conferred resistance upon E. coli cells to the inhibiting concentrations of l-phenylalanine and aromatic amino acid analogues, dl-p-flu ... >> More
The inner membrane protein YddG of Escherichia coli is a homologue of the known amino acid exporters RhtA and YdeD. It was found that the yddG gene overexpression conferred resistance upon E. coli cells to the inhibiting concentrations of l-phenylalanine and aromatic amino acid analogues, dl-p-fluorophenylalanine, dl-o-fluorophenylalanine and dl-5-fluorotryptophan. In addition, yddG overexpression enhanced the production of l-phenylalanine, l-tyrosine or l-tryptophan by the respective E. coli-producing strains. On the other hand, the inactivation of yddG decreased the aromatic amino acid accumulation by these strains. The cells of the E. colil-phenylalanine-producing strain containing overexpressed yddG accumulated less l-phenylalanine inside and exported the amino acid at a higher rate than the cells of the isogenic strain containing wild-type yddG. Taken together, these results indicate that YddG functions as an aromatic amino acid exporter. << Less
FEMS Microbiol. Lett. 275:312-318(2007) [PubMed] [EuropePMC]