B12-Dependent Methionine Synthase: A Structure That Adapts to Catalyze Multiple Methyl Transfer Reactions

2002 ◽  
pp. 186-201 ◽  
Author(s):  
Martha L. Ludwig ◽  
Rowena G. Matthews
Keyword(s):  
Methionine Synthase ◽  
Transfer Reactions ◽  
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.

Corrinoid-Dependent Methyl Transfer Reactions inSporomusa ovata

2007 ◽  
pp. 179-187 ◽  
Author(s):  
Erhard Stupperich ◽  
Ralph Konle ◽  
Michaela Lehle
Keyword(s):  
Transfer Reactions ◽  
Methyl Transfer

Methyl-transfer reactions. 7. Systems with MeOSO+ intermediate

1983 ◽  
Vol 48 (15) ◽  
pp. 2531-2534 ◽  
Author(s):  
J. Joseph Christie ◽  
Edward S. Lewis ◽  
Edward F. Casserly
Keyword(s):  
Transfer Reactions ◽  
Methyl Transfer

scholarly journals Application of a BOSS-Gaussian interface for QM/MM simulations of Henry and methyl transfer reactions

2015 ◽  
Vol 36 (27) ◽  
pp. 2064-2074 ◽  
Author(s):  
Jonah Z. Vilseck ◽  
Jakub Kostal ◽  
Julian Tirado-Rives ◽  
William L. Jorgensen
Keyword(s):  
Transfer Reactions ◽  
Methyl Transfer

A High-Level Theoretical Study on the Gas-Phase Identity Methyl Transfer Reactions

2002 ◽  
Vol 106 (6) ◽  
pp. 1081-1087 ◽  
Author(s):  
Ikchoon Lee ◽  
Chang Kon Kim ◽  
Chang Kook Sohn ◽  
Hong Guang Li ◽  
Hai Whang Lee
Keyword(s):  
Gas Phase ◽  
Theoretical Study ◽  
Transfer Reactions ◽  
Methyl Transfer ◽  
High Level

Reactivity in methyl transfer reactions. 5. Relation between rates and equilibriums

1980 ◽  
Vol 102 (5) ◽  
pp. 1619-1623 ◽  
Author(s):  
Edward S. Lewis ◽  
Semyon Kukes ◽  
Carl D. Slater
Keyword(s):  
Transfer Reactions ◽  
Methyl Transfer
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