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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
22
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pubmed:dateCreated |
2007-10-25
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pubmed:abstractText |
The antiarthritis drug D-penicillamine (D-PEN) catalyzes zinc(II) transfer from carboxypeptidase A to chelators such as thionein and EDTA at a rate constant up to 400-fold faster than the uncatalyzed release. Once D-PEN releases zinc(II) from enzyme stronger chelators can tightly bind zinc(II) leading to complete and essentially irreversible inhibition. D-PEN is the first drug to inhibit a zinc protease by catalyzing metal removal, and the name "catalytic chelation" is proposed for this mechanism.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0022-2623
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
50
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5524-7
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pubmed:meshHeading |
pubmed-meshheading:17918925-Animals,
pubmed-meshheading:17918925-Carboxypeptidases A,
pubmed-meshheading:17918925-Catalysis,
pubmed-meshheading:17918925-Cattle,
pubmed-meshheading:17918925-Chelating Agents,
pubmed-meshheading:17918925-Drug Synergism,
pubmed-meshheading:17918925-Edetic Acid,
pubmed-meshheading:17918925-Ergothioneine,
pubmed-meshheading:17918925-Kinetics,
pubmed-meshheading:17918925-Penicillamine,
pubmed-meshheading:17918925-Zinc
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pubmed:year |
2007
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pubmed:articleTitle |
Catalysis of zinc transfer by D-penicillamine to secondary chelators.
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pubmed:affiliation |
Department of Pharmacology and Molecular Sciences, Medical Scientist Training Program, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21287, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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