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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
13
|
| pubmed:dateCreated |
1983-8-17
|
| pubmed:abstractText |
Two pentapeptides Phe-Leu-X-Glu-Val where X is either the L-threo-gamma-fluoroglutamic acid or the L-erythro-isomer have been synthesized and tested as substrates in the vitamin K-dependent carboxylation. Both peptides are carboxylated, but the reaction occurs exclusively on the glutamic acid of the L-threo-gamma-fluoroglutamate-containing peptide, whereas both glutamic and fluoroglutamic residues of the L-erythro-gamma-fluoroglutamate-containing peptide are carboxylated. These results reveal that the enzymatic hydrogen abstraction step is stereospecific and corresponds, in the gamma-fluoroglutamate case, to the elimination of the hydrogen equivalent to the pro-S hydrogen of glutamic acid.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
10
|
| pubmed:volume |
258
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
7897-9
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading | |
| pubmed:year |
1983
|
| pubmed:articleTitle |
Vitamin K-dependent carboxylation. Study of the hydrogen abstraction stereochemistry with gamma-fluoroglutamic acid-containing peptides.
|
| pubmed:publicationType |
Journal Article
|