Source:http://linkedlifedata.com/resource/pubmed/id/11543272
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
|
pubmed:dateCreated |
2000-8-27
|
pubmed:abstractText |
In vitro selection techniques were applied to the development of a DNA enzyme that contains three catalytically essential imidazole groups and catalyzes the cleavage of RNA substrates. Nucleic acid libraries for selection were constructed by polymerase-catalyzed incorporation of C5-imidazole-functionalized deoxyuridine in place of thymidine. Chemical synthesis was used to define a minimized catalytic domain composed of only 12 residues. The catalytic domain forms a compact hairpin structure that displays the three imidazole-containing residues. The enzyme can be made to cleave RNAs of almost any sequence by simple alteration of the two substrate-recognition domains that surround the catalytic domain. The enzyme operates with multiple turnover in the presence of micromolar concentrations of Zn2+, exhibiting saturation kinetics and a catalytic rate of >1 min-1. The imidazole-containing DNA enzyme, one of the smallest known nucleic acid enzymes, combines the substrate-recognition properties of nucleic acid enzymes and the chemical functionality of protein enzymes in a molecule that is small, yet versatile and catalytically efficient.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
S
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyuridine,
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Imidazoles,
http://linkedlifedata.com/resource/pubmed/chemical/Metals,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Catalytic,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0002-7863
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
22
|
pubmed:volume |
122
|
pubmed:owner |
NASA
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2433-9
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:11543272-Base Composition,
pubmed-meshheading:11543272-Base Sequence,
pubmed-meshheading:11543272-Catalysis,
pubmed-meshheading:11543272-Cations, Divalent,
pubmed-meshheading:11543272-DNA,
pubmed-meshheading:11543272-Deoxyuridine,
pubmed-meshheading:11543272-Endoribonucleases,
pubmed-meshheading:11543272-Hydrogen-Ion Concentration,
pubmed-meshheading:11543272-Imidazoles,
pubmed-meshheading:11543272-Kinetics,
pubmed-meshheading:11543272-Metals,
pubmed-meshheading:11543272-RNA,
pubmed-meshheading:11543272-RNA, Catalytic,
pubmed-meshheading:11543272-Substrate Specificity,
pubmed-meshheading:11543272-Zinc
|
pubmed:year |
2000
|
pubmed:articleTitle |
RNA cleavage by a DNA enzyme with extended chemical functionality.
|
pubmed:affiliation |
Department of Chemistry, The Scripps Research Institute, La Jolla, California 92037, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|