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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
36
|
| pubmed:dateCreated |
1998-3-31
|
| pubmed:abstractText |
Aminoacyl-tRNAs are either synthesized directly by aminoacyl-tRNA synthetases or indirectly by tRNA-dependent transformation of mischarged tRNAs. The enzymes which participate in the indirect routes may be interesting targets in the development of novel therapeutic compounds. We have purified one such enzyme, Glu-tRNA(Gln) amidotransferase from Bacillus subtilis, to homogeneity and present the initial biochemical characterization data.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0261-3166
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
2-4
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1997
|
| pubmed:articleTitle |
tRNA-dependent amino acid transformations.
|
| pubmed:affiliation |
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA.
|
| pubmed:publicationType |
Journal Article,
Review
|