Mechanistic Insights for Formation of an Organometallic Co–C Bond in the Methyl Transfer Reaction Catalyzed by Methionine Synthase

2013 ◽  
Vol 117 (50) ◽  
pp. 16044-16057 ◽  
Author(s):  
Neeraj Kumar ◽  
Pawel M. Kozlowski
Keyword(s):  
Transfer Reaction ◽  
Methionine Synthase ◽  
Methyl Transfer

scholarly journals The thiostrepton A tryptophan methyltransferase TsrM catalyses a cob(II)alamin-dependent methyl transfer reaction

2015 ◽  
Vol 6 (1) ◽  
Author(s):  
Alhosna Benjdia ◽  
Stéphane Pierre ◽  
Carmen Gherasim ◽  
Alain Guillot ◽  
Manon Carmona ◽  
...  
Keyword(s):  
Transfer Reaction ◽  
Methyl Transfer

scholarly journals The folate-binding module ofThermus thermophiluscobalamin-dependent methionine synthase displays a distinct variation of the classical TIM barrel: a TIM barrel with a `twist'

2018 ◽  
Vol 74 (1) ◽  
pp. 41-51
Author(s):  
Kazuhiro Yamada ◽  
Markos Koutmos
Keyword(s):  
Tertiary Amine ◽  
Thermus Thermophilus ◽  
Methionine Synthase ◽  
Structural Studies ◽  
Binding Domains ◽  
Methyl Transfer ◽  
Structural Differences ◽  
Tim Barrel ◽  
Eukaryotic Organisms

Methyl transfer between methyltetrahydrofolate and corrinoid molecules is a key reaction in biology that is catalyzed by a number of enzymes in many prokaryotic and eukaryotic organisms. One classic example of such an enzyme is cobalamin-dependent methionine synthase (MS). MS is a large modular protein that utilizes an SN2-type mechanism to catalyze the chemically challenging methyl transfer from the tertiary amine (N5) of methyltetrahydrofolate to homocysteine in order to form methionine. Despite over half a century of study, many questions remain about how folate-dependent methyltransferases, and MS in particular, function. Here, the structure of the folate-binding (Fol) domain of MS fromThermus thermophilusis reported in the presence and absence of methyltetrahydrofolate. It is found that the methyltetrahydrofolate-binding environment is similar to those of previously described methyltransferases, highlighting the conserved role of this domain in binding, and perhaps activating, the methyltetrahydrofolate substrate. These structural studies further reveal a new distinct and uncharacterized topology in the C-terminal region of MS Fol domains. Furthermore, it is found that in contrast to the canonical TIM-barrel β8α8fold found in all other folate-binding domains, MS Fol domains exhibit a unique β8α7fold. It is posited that these structural differences are important for MS function.

Methyl-transfer reaction to alkylthiol catalyzed by a simple vitamin B12 model complex using zinc powder

2011 ◽  
Vol 368 (1) ◽  
pp. 194-199 ◽  
Author(s):  
Ling Pan ◽  
Keishiro Tahara ◽  
Takahiro Masuko ◽  
Yoshio Hisaeda
Keyword(s):  
Vitamin B12 ◽  
Transfer Reaction ◽  
Zinc Powder ◽  
Methyl Transfer ◽  
Model Complex

Electrochemical Methyl-transfer Reaction to Alkylthiol Catalyzed by Hydrophobic Vitamin B12

2009 ◽  
Vol 38 (1) ◽  
pp. 26-27 ◽  
Author(s):  
Ling Pan ◽  
Hisashi Shimakoshi ◽  
Yoshio Hisaeda
Keyword(s):  
Vitamin B12 ◽  
Transfer Reaction ◽  
Methyl Transfer

scholarly journals Flagellin lysine methyltransferase FliB catalyzes a [4Fe-4S] mediated methyl transfer reaction

2021 ◽  
Vol 17 (11) ◽  
pp. e1010052
Author(s):  
Chu Wang ◽  
Christian Nehls ◽  
Dirk Baabe ◽  
Olaf Burghaus ◽  
Robert Hurwitz ◽  
...  
Keyword(s):  
Transfer Reaction ◽  
Radical Mechanism ◽  
Zero Field ◽  
Paramagnetic Resonance ◽  
Methyl Transfer ◽  
Lysine Residues ◽  
Oxygen Sensitive ◽  
Flagellar Filament

The methyltransferase FliB posttranslationally modifies surface-exposed ɛ-N-lysine residues of flagellin, the protomer of the flagellar filament in Salmonella enterica (S. enterica). Flagellin methylation, reported originally in 1959, was recently shown to enhance host cell adhesion and invasion by increasing the flagellar hydrophobicity. The role of FliB in this process, however, remained enigmatic. In this study, we investigated the properties and mechanisms of FliB from S. enterica in vivo and in vitro. We show that FliB is an S-adenosylmethionine (SAM) dependent methyltransferase, forming a membrane associated oligomer that modifies flagellin in the bacterial cytosol. Using X-band electron paramagnetic resonance (EPR) spectroscopy, zero-field 57Fe Mössbauer spectroscopy, methylation assays and chromatography coupled mass spectrometry (MS) analysis, we further found that FliB contains an oxygen sensitive [4Fe-4S] cluster that is essential for the methyl transfer reaction and might mediate a radical mechanism. Our data indicate that the [4Fe-4S] cluster is coordinated by a cysteine rich motif in FliB that is highly conserved among multiple genera of the Enterobacteriaceae family.

Methyl Transfer Reaction from Monomethyltin Reagent under Palladium(0) Catalysis: A Versatile Method for Labeling with Carbon-11.

ChemInform ◽  
2006 ◽  
Vol 37 (17) ◽  
Author(s):  
Mickael Huiban ◽  
Aline Huet ◽  
Louisa Barre ◽  
Franck Sobrio ◽  
Eric Fouquet ◽  
...  
Keyword(s):  
Transfer Reaction ◽  
Methyl Transfer
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