Probing the active site of homoserine trans-succinylase.

Content Provider	Semantic Scholar
Author	Rosen, Ran Becher, Dörte Büttner, Knut Biran, Dvora Hecker, Michael Ron, Eliora Z.
Copyright Year	2004
Abstract	Homoserine trans-succinylase is the first enzyme in methionine biosynthesis of Escherichia coli and catalyzes the activation of homoserine via a succinylation reaction. The in vivo activity of this enzyme is subject to tight regulation by several mechanisms, including repression and activation of gene expression, feedback inhibition, temperature regulation and proteolysis. This complex regulation reflects the key role of this enzyme in bacterial metabolism. Here, we demonstrate--using proteomics and high-resolution mass spectrometry--that succinyl is covalently bound to one of the two adjacent lysine residues at positions 45 and 46. Replacing these lysine residues by alanine abolished the enzymatic activity. These findings position the lysine residues, one of which is conserved, at the active site.
File Format	PDF HTM / HTML
DOI	10.1016/j.febslet.2004.10.037
PubMed reference number	15556615
Journal	Medline
Volume Number	577
Issue Number	3
Alternate Webpage(s)	https://www.tau.ac.il/~rrosen/HTSActiveSite.pdf
Alternate Webpage(s)	https://doi.org/10.1016/j.febslet.2004.10.037
Journal	FEBS letters
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article