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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
|
pubmed:dateCreated |
1992-10-1
|
pubmed:abstractText |
In the past year, site-directed mutagenesis and other forms of protein engineering have been used to reverse the substrate specificity of several pairs of enzymes, including disulphide oxidoreductases, proteases, sugar-processing enzymes, and nucleases, as well as the specificity of hormones and their receptors. Mutations have been found that affect rate-determining steps, allowing normally transient intermediates to accumulate. Other mutations endow enzymes with totally new chemical reactions, and even novel biological functions. A combination of molecular genetics and chemical modification has been used for protein engineering.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
B
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0958-1669
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
3
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
370-7
|
pubmed:dateRevised |
2005-11-16
|
pubmed:meshHeading | |
pubmed:year |
1992
|
pubmed:articleTitle |
Alteration of enzyme specificity and catalysis.
|
pubmed:affiliation |
Department of Pharmacy, University of Manchester, UK.
|
pubmed:publicationType |
Journal Article,
Review
|