Linked Life Data

8779715

Source:http://linkedlifedata.com/resource/pubmed/id/8779715

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6595
pubmed:dateCreated
1996-10-17
pubmed:abstractText
Mimicking the efficiency of enzyme catalysis is a daunting challenge. An enzyme selectively binds and stabilizes the transition state (s) for a particular reaction. Artificial host systems can bind ground states just as efficiently, and rate enhancements comparable to those in enzymatic reactions can be achieved by bringing catalytic and substrate groups together in intramolecular reactions. But the combination of selective binding and efficient catalysis remains elusive. The best enzyme mimics currently known are catalytic antibodies. They bind transition-state analogues with high affinity, but their catalytic efficiency generally falls far short of that of enzymes. Thorn et al. recently described an antibody that catalyses the eliminative ring-opening of a benziosoxazole "exceptionally efficiently" using carboxylate as the general base, raising the intriguing possibility that this high efficiency derives from precise positioning of catalytic and substrate groups. Here we show that familiar 'off-the-shelf' proteins--serum albumins--catalyse the same reaction at similar rates, using a lysine side-chain amino group as the catalytic general base. Comparisons suggest that formal general base catalysis is of only modest efficiency in both systems, and that the antibody catalysis is boosted by a non-specific medium effect.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
383
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
60-2
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Off-the-shelf proteins that rival tailor-made antibodies as catalysts.
pubmed:affiliation
University Chemical Laboratory, Cambridge, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't