Domains ofE. ColiGlutaminyl-tRNA Synthetase Disordered in the Crystal Structure Are Essential for Function or Stability

Autor:	Hans-Ulrich Thomann, Joyce M. Sherman, Dieter Söill, Jill Conley
Rok vydání:	1994
Předmět:	Specificity constant chemistry.chemical_classification Chemistry Stereochemistry Kinetics Aminoacylation Crystal structure medicine.disease_cause Biochemistry Glutamine—tRNA ligase Enzyme Genetics medicine Escherichia coli Function (biology)
Zdroj:	Nucleosides and Nucleotides. 13:1581-1595
ISSN:	0732-8311
DOI:	10.1080/15257779408012173
Popis:	Deletion analysis of E. coli glutaminyl-tRNA synthetase indicates that the N- and C-termini of the protein, which appear disordered in the crystal structure, are essential for function and stability in vivo. In vitro aminoacylation kinetics of a C-terminal deletion mutant exhibit a sharp reduction in the specificity constant. However, an N-terminal extension is catalytically, if not structurally equivalent to wild-type.
Databáze:	OpenAIRE
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