Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP binding View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1982-10

AUTHORS

Greg Winter, Alan R. Fersht, Anthony J. Wilkinson, Mark Zoller, Michael Smith

ABSTRACT

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 eventually lead to the engineering of new enzymatic activities. The gene encoding the enzyme is first cloned into a vector from which the enzyme is expressed and is then mutated in vitro to change a particular nucleotide and hence the amino acid sequence of the enzyme. We have cloned the gene for the tyrosyl tRNA synthetase of Bacillus stearothermophilus into a vector derived from the single-stranded bacteriophage M13 to facilitate mutagenesis with mismatched synthetic oligodeoxynucleotide primers. From the recombinant M13 clone we have obtained high levels of the enzyme (∼50% of soluble protein) expressed in the Escherichia coli host and have converted cysteine (Cys35) at the enzyme's active site to serine. This leads to a reduction in enzymatic activity that is largely attributable to a lower Km for ATP. More... »

PAGES

756-758

References to SciGraph publications

Journal

TITLE

Nature

ISSUE

5885

VOLUME

299

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/299756a0

DOI

http://dx.doi.org/10.1038/299756a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1052478826

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/6811955


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