PMID:10383414
| Citation |
Soutourina, J, Plateau, P, Delort, F, Peirotes, A and Blanquet, S (1999) Functional characterization of the D-Tyr-tRNATyr deacylase from Escherichia coli. J. Biol. Chem. 274:19109-14 |
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| Abstract |
The yihZ gene of Escherichia coli is shown to produce a deacylase activity capable of recycling misaminoacylated D-Tyr-tRNATyr. The reaction is specific and, under optimal in vitro conditions, proceeds at a rate of 6 s-1 with a Km value for the substrate equal to 1 microM. Cell growth is sensitive to interruption of the yihZ gene if D-tyrosine is added to minimal culture medium. Toxicity of exogenous D-tyrosine is exacerbated if, in addition to the disruption of yihZ, the gene of D-amino acid dehydrogenase (dadA) is also inactivated. Orthologs of the yihZ gene occur in many, but not all, bacteria. In support of the idea of a general role of the D-Tyr-tRNATyr deacylase function in the detoxification of cells, similar genes can be recognized in Saccharomyces cerevisiae, Caenorhabditis elegans, Arabidopsis thaliana, mouse, and man. |
| Links | |
| Keywords |
Aminoacyltransferases/genetics; Aminoacyltransferases/metabolism; Animals; Catalysis; Cloning, Molecular; DNA, Bacterial/chemistry; Escherichia coli/enzymology; Escherichia coli/genetics; Gene Library; Humans; Male; Mice; Open Reading Frames; Polymerase Chain Reaction; RNA, Transfer, Tyr/metabolism; Restriction Mapping |
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