Linked Life Data

2456885

Source:http://linkedlifedata.com/resource/pubmed/id/2456885

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1988-9-12
pubmed:abstractText
A detailed study of the chemical behavior of modern catalysts (here, exemplified by dehydrogenases dependent on NAD+) allows us to construct models that distinguish between selected and drifting behaviors in biological macromolecules. These models enable us to manipulate rationally the properties of enzymes, here to design an "acetaldehyde reductase" dependent on NAD+ that is faster than any given us by nature. When applied to the origin of protein catalysis, models that explain the structures of ribo-cofactors (e.g., NAD+) must postulate a metabolically complex breakthrough organism. This means that: (1) The view from the present day back to the truly primeval organism is obscured; it is futile to try to deduce the detailed structure of the first life by examining the behaviors of modern organisms. (2) Riboorganisms dominated life on earth for a long time before translation evolved; indeed, fossils of riboorganisms might already be known. (3) Using organic synthesis, we have expanded the number of bases available for making RNA and making accessible RNA molecules that are likely to be intrinsically better catalysts.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0091-7451
pubmed:author
pubmed:issnType
Print
pubmed:volume
52
pubmed:owner
NLM
pubmed:authorsComplete
N
pubmed:pagination
53-63
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Natural selection, protein engineering, and the last riboorganism: rational model building in biochemistry.
pubmed:affiliation
Laboratory for Organic Chemistry, Swiss Federal Institute of Technology, Zurich.
pubmed:publicationType
Journal Article