Proteomics

Results change the paradigm for vitamin K-dependent protein carboxylation

Published in Medical Letter on the CDC and FDA, December 19th, 2004

A recent report describes a new model for vitamin K-dependent carboxylation: The catalytic base that deprotonates vitamin K hydroquinone is not Cys but an activated amine.

According to published research from the United States, "Vitamin K-dependent (VKD) proteins require carboxylation for diverse functions that include hemostasis, apoptosis, and Ca²⁺ homeostasis, yet the mechanism of carboxylation is not well understood. Combined biochemical and chemical studies have led to a long-standing model in which a carboxylase Cys catalytic base deprotonates vitamin K hydroquinone (KH2) leading to KH2 oxygenation and Glu carboxylation."

M.A....

Want to see the full article?

Purchase this article for only $3.00

We're a pay-per-view site for premium content. If you'd like to purchase this article, it's only $3.00.

Welcome to NewsRx!

Learn more about a six-week, no-risk free trial of Medical Letter on the CDC and FDA

Source: Medical Letter on the CDC and FDA (2004-12-19)

NewsRx is Social

Top Medical Newsletters

Awards

Best Health/Healthcare Content, 2012
Best Health/Healthcare Content, 2011
Best e-Business Site, 2010
Best e-Business Site, 2009
Best e-Business Site, 2008
Best e-Business Site, 2007
Best e-Business Site, 2006
Best Healthcare Content, 2005
Best Overall Internet Site, 2005
Best Interactive Site, 2005

Facts & Stats

NewsRx also is available at LexisNexis, Gale, ProQuest, Factiva, Dialog, Thomson Reuters, NewsEdge, and Dow Jones.

Google 2010 PageRank: #2 Among Top Health News and Media Publications
Google 2010 PageRank: #2 Among Top Science Publications in Biology/Physiology
Google 2010 PageRank: #2 Among Top News and Media for the Business of Pharmaceuticals
Amazon's Alexa 2010 PageRank: #2 News and Media Site for the Pharmaceutical Industry