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Probing the active site of homoserine trans-succinylase
Year:
2004
Source of publication :
FEBS Letters
Authors :
Rosen, Ran
;
.
Volume :
577
Co-Authors:
Rosen, R., Dept. Molec. Microbiol. and Biotech., Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv 69978, Israel, Inst. F. Mikrobiol. M., Ernst-Moritz-Arndt-Univ. Greifswald, 17487 Greifswald, Germany
Becher, D., Inst. F. Mikrobiol. M., Ernst-Moritz-Arndt-Univ. Greifswald, 17487 Greifswald, Germany
Büttner, K., Inst. F. Mikrobiol. M., Ernst-Moritz-Arndt-Univ. Greifswald, 17487 Greifswald, Germany
Biran, D., Dept. Molec. Microbiol. and Biotech., Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv 69978, Israel
Hecker, M., Inst. F. Mikrobiol. M., Ernst-Moritz-Arndt-Univ. Greifswald, 17487 Greifswald, Germany
Ron, E.Z., Dept. Molec. Microbiol. and Biotech., Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv 69978, Israel
Facilitators :
From page:
386
To page:
392
(
Total pages:
7
)
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. © 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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More details
DOI :
10.1016/j.febslet.2004.10.037
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
19992
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:33
Scientific Publication
Probing the active site of homoserine trans-succinylase
577
Rosen, R., Dept. Molec. Microbiol. and Biotech., Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv 69978, Israel, Inst. F. Mikrobiol. M., Ernst-Moritz-Arndt-Univ. Greifswald, 17487 Greifswald, Germany
Becher, D., Inst. F. Mikrobiol. M., Ernst-Moritz-Arndt-Univ. Greifswald, 17487 Greifswald, Germany
Büttner, K., Inst. F. Mikrobiol. M., Ernst-Moritz-Arndt-Univ. Greifswald, 17487 Greifswald, Germany
Biran, D., Dept. Molec. Microbiol. and Biotech., Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv 69978, Israel
Hecker, M., Inst. F. Mikrobiol. M., Ernst-Moritz-Arndt-Univ. Greifswald, 17487 Greifswald, Germany
Ron, E.Z., Dept. Molec. Microbiol. and Biotech., Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv 69978, Israel
Probing the active site of homoserine trans-succinylase
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. © 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
Scientific Publication
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