The role of complementary hydrogen bonding as a determinant of biological specificity has
been examined by protein engineering of the tyrosyl-tRNA synthetase. Deletion of a side …

The AAA + superfamily of ATPases, which contain a homologous ATPase module, are found
in all kingdoms of living organisms where they participate in diverse cellular processes …

Bacteria adapt to environmental stimuli by adjusting their transcriptomes in a complex manner,
the full potential of which has yet to be established for any individual bacterial species. …

In a previous study, a mutant of tyrosyl-tRNA synthetase in which a threonine residue (Thr51)
was converted to proline dramatically improved the aff inity of the enzyme for its ATP …

We describe here a general method for systematically replacing amino acids in an enzyme.
This allows analysis of their molecular roles in substrate binding or catalysis and could …

Adaptation of cells to environmental changes requires dynamic interactions between
metabolic and regulatory networks, but studies typically address only one or a few layers of …

Arginines are a recurrent feature of the active sites and subunit interfaces of the ATPase
domains of AAA and AAA + proteins. In particular family members these residues occupy two or …

African sleeping sickness or human African trypanosomiasis, caused by Trypanosoma brucei
spp., is responsible for ∼30,000 deaths each year. Available treatments for this disease …

Anthony J. Wilkinson, Alan R. Fersht,* David M. Blow, and Greg Winter* abstract:
Oligodeoxynucleotide-directed mutagenesis has been used on the gene of tyrosyl-tRNA synthetase …

It is 20 years since site-directed mutagenesis was first used to modify the active site of an
enzyme of known structure and mechanism. Since then, this method has contributed far-…