HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Zieske, L. R. Articles by Davis, L. Search for Related Content PubMed PubMed Citation Articles by Zieske, L. R. Articles by Davis, L. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 258, Issue 17, 10355-10359, Sep, 1983

Decarboxylation of glycine by serine hydroxymethyltransferase in the presence of lipoic acid

LR Zieske and L Davis

Serine hydroxymethyltransferase and the glycine cleavage system are both present in liver mitochondria and both bind glycine to form a pyridoxal 5'-phosphate carbanionic quinoid species. Lipoic acid has been shown to have the ability to intercept the carbanionic intermediate formed from the binary complex of serine hydroxymethyltransferase and glycine and form an intermediate adduct which is ultimately processed to yield CO2 and a methylamine adduct. Kinetic studies have shown that the lipoic acid-dependent decarboxylation of glycine catalyzed by serine hydroxymethyltransferase proceeds through a sequential mechanism. This lipoic acid-dependent decarboxylation catalyzed by serine hydroxymethyltransferase is similar to the initial reaction of the glycine cleavage system and to the lipoic acid-dependent decarboxylation of glycine by the P-protein alone suggesting that both enzymes could serve in lieu of each other.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?