Mechanistic Investigations of Anaerobic Sulfatase-Maturating Enzyme: Direct Cβ H-Atom Abstraction Catalyzed by a Radical AdoMet Enzyme

被引:36
作者
Benjdia, Alhosna [1 ]
Leprince, Jerome [2 ]
Sandstrom, Corine [3 ]
Vaudry, Hubert [2 ]
Berteau, Olivier [1 ]
机构
[1] UEPSD, INRA, UPR 910, F-78352 Jouy En Josas, France
[2] Univ Rouen, INSERM, U413,IFRMP23, UA CNRS, F-76821 Mont St Aignan, France
[3] Swedish Univ Agr Sci, Dept Chem, SE-75007 Uppsala, Sweden
关键词
CRYSTAL-STRUCTURE; PSEUDOMONAS-AERUGINOSA; S-ADENOSYLMETHIONINE; ALKYLSULFATASE; ARYLSULFATASE; SUPERFAMILY; PROKARYOTES;
D O I
10.1021/ja901571p
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Sulfatases are unique in requiring an essential post-translational modification of a critical active-site cysteinyt or seryl residue to 3-oxoalanine usually called C alpha-formylglycine (FGly). This post-translational modification is catalyzed anaerobically by anaerobic Sulfatase Maturating Enzyme (anSME), a member of the radical AdoMet superfamily. Using a new labeled substrate, we demonstrate that anSME uses a 5'-deoxyadenosyl radical to catalyze direct H-atom abstraction from the substrate. We thus established that anSMEs are the first radical AdoMet enzymes catalyzing a post-translational modification involving C, H-atom abstraction from an active site cysteinyl or seryl residue. This mechanistic study allowed us to decipher the first steps of the mechanism of this new radical AdoMet enzyme family.
引用
收藏
页码:8348 / +
页数:4
相关论文
共 16 条
[1]   Anaerobic sulfatase-maturating enzymes, first dual substrate radical S-adenosylmethionine enzymes [J].
Benjdia, Alhosna ;
Subramanian, Sowmya ;
Leprince, Jerome ;
Vaudry, Hubert ;
Johnson, Michael K. ;
Berteau, Olivier .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (26) :17815-17826
[2]   Anaerobic sulfatase-maturating enzymes: Radical SAM enzymes able to catalyze in vitro sulfatase post-translational modification [J].
Benjdia, Alhosna ;
Leprince, Jerome ;
Guillot, Alain ;
Vaudry, Hubert ;
Rabot, Sylvie ;
Berteau, Olivier .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2007, 129 (12) :3462-+
[3]   First evidences for a third sulfatase maturation system in prokaryotes from E-coli aslB and ydeM deletion mutants [J].
Benjdia, Alhosna ;
Deho, Gianni ;
Rabot, Sylvie ;
Berteau, Olivier .
FEBS LETTERS, 2007, 581 (05) :1009-1014
[4]   A new type of bacterial sulfatase reveals a novel maturation pathway in prokaryotes [J].
Berteau, Olivier ;
Guillot, Alain ;
Benjdia, Alhosna ;
Rabot, Sylvie .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (32) :22464-22470
[5]   Enzymatic C-H activation by metal-superoxo intermediates [J].
Bollinger, J. Martin, Jr. ;
Krebs, Carsten .
CURRENT OPINION IN CHEMICAL BIOLOGY, 2007, 11 (02) :151-158
[6]   1.3 Å structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family [J].
Boltes, I ;
Czapinska, H ;
Kahnert, A ;
von Bülow, R ;
Dierks, T ;
Schmidt, B ;
von Figura, K ;
Kertesz, MA ;
Usón, I .
STRUCTURE, 2001, 9 (06) :483-491
[7]   Function and structure of a prokaryotic formylglycine-generating enzyme [J].
Carlson, Brian L. ;
Ballister, Edward R. ;
Skordalakes, Emmanuel ;
King, David S. ;
Breidenbach, Mark A. ;
Gilmore, Sarah A. ;
Berger, James M. ;
Bertozzi, Carolyn R. .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (29) :20117-20125
[8]   S-adenosylmethionine:: nothing goes to waste [J].
Fontecave, M ;
Atta, M ;
Mulliez, E .
TRENDS IN BIOCHEMICAL SCIENCES, 2004, 29 (05) :243-249
[9]  
Frey PA, 2008, CRIT REV BIOCHEM MOL, V43, P63, DOI [10.1080/10409230701829169, 10.1080/10409230701829169 ]
[10]   The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, defines a third class of sulfatases [J].
Hagelueken, Gregor ;
Adams, Thorsten M. ;
Wiehlmann, Lutz ;
Widow, Lite ;
Kolmar, Harald ;
Tummler, Burkhard ;
Heinz, Dirk W. ;
Schubert, Wolf-Dieter .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (20) :7631-7636