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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
|
pubmed:dateCreated |
1995-7-12
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pubmed:abstractText |
The efficiency of cobalt(III)-ligated peptides as acceptor nucleophiles in acyl transfer reactions catalyzed by alpha-chymotrypsin was examined. A series of metallopeptides with the general formula [H-(Gly)n-OCo(NH3)5]2+ (1 < or = n < or = 4) was tested. The aminolysis rate of acyl-chymotrypsin was measured spectrophotometrically by monitoring the concentration of unreacted nucleophile. The rate of the competing hydrolysis of acyl-chymotrypsin was obtained by automatic titration with base, using a pH-stat. The main result was that the positively charged metallopeptides, in general, were more efficient nucleophiles than the corresponding amides and free peptides that were examined for comparison. A binding model that rationalizes the findings is given.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
|
pubmed:issn |
0162-0134
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
57
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
271-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7775980-Amino Acid Sequence,
pubmed-meshheading:7775980-Catalysis,
pubmed-meshheading:7775980-Chymotrypsin,
pubmed-meshheading:7775980-Cobalt,
pubmed-meshheading:7775980-Kinetics,
pubmed-meshheading:7775980-Molecular Sequence Data,
pubmed-meshheading:7775980-Peptide Synthases,
pubmed-meshheading:7775980-Peptides,
pubmed-meshheading:7775980-Spectrophotometry,
pubmed-meshheading:7775980-Thermodynamics
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pubmed:year |
1995
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pubmed:articleTitle |
Cobalt(III)-ligated peptides as acyl acceptors in peptide synthesis catalyzed by chymotrypsin.
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pubmed:affiliation |
Chemistry Department A, Technical University of Denmark, Lyngby.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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