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rdf:type |
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|
lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2006-3-24
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pubmed:abstractText |
The irreversible inhibition of 8-amino-7-oxononanoate synthase by trifluoroalanine involves decarboxylative defluorination of the inhibitor-PLP aldimine followed by attack of the conjugated imine by the amino group of the active site lysine to afford a covalently bound difluorinated intermediate which can subsequently undergo further HF losses and hydrolysis to afford a 2-(pyridoximine phosphate) acetoyl protein adduct.
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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 |
Apr
|
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pubmed:issn |
1477-0520
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pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1209-12
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pubmed:meshHeading |
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pubmed:year |
2006
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pubmed:articleTitle |
Suicide inhibition of alpha-oxamine synthases: structures of the covalent adducts of 8-amino-7-oxononanoate synthase with trifluoroalanine.
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|
pubmed:affiliation |
School of Biology, Swann Building, University of Edinburgh, Mayfield Road, Edinburgh, UKEH9 3JR.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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