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Inhibition of Cobalamin-Dependent Methionine Synthase by Substituted Benzo-Fused Heterocycles
FEBS Journal, 2007 The cobalamin-dependent cytosolic enzyme, methionine synthase (EC.2.1.1.13), catalyzes the remethylation of homocysteine to methionine using 5-methyltetrahydrofolate as the methyl donor.
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The role of methionine synthases in fungal metabolism and virulence
Essays in Biochemistry, 2023Abstract Methionine synthases (MetH) catalyse the methylation of homocysteine (Hcy) with 5-methyl-tetrahydrofolate (5, methyl-THF) acting as methyl donor, to form methionine (Met) and tetrahydrofolate (THF). This function is performed by two unrelated classes of enzymes that differ significantly in both their structures and mechanisms of
Jennifer Scott, Jorge Amich
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Metabolic Derangement of Methionine and Folate Metabolism in Mice Deficient in Methionine Synthase Reductase [PDF]
Molecular Genetics and Metabolism, 2007 Hyperhomocyst(e)inemia is a metabolic derangement that is linked to the distribution of folate pools, which provide one-carbon units for biosynthesis of purines and thymidylate and for remethylation of homocysteine to form methionine. In humans, methionine synthase deficiency results in the accumulation of methyltetrahydrofolate at the expense of ...
Teodoro Bottiglieri +2 more
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Atherosclerosis, 2003
The metabolism of homocysteine requires contributions of several enzymes and vitamin cofactors. Earlier studies identified a common polymorphism of methylenetetrahydrofolate reductase that was associated with mild hyperhomocysteinemia. Common variants of two other enzymes involved in homocysteine metabolism, methionine synthase and methionine synthase ...
Paul F Jacques +2 more
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The metabolism of homocysteine requires contributions of several enzymes and vitamin cofactors. Earlier studies identified a common polymorphism of methylenetetrahydrofolate reductase that was associated with mild hyperhomocysteinemia. Common variants of two other enzymes involved in homocysteine metabolism, methionine synthase and methionine synthase ...
Paul F Jacques +2 more
exaly +3 more sources
Inactivation of Methionine Synthase by Nitrous Oxide
European Journal of Biochemistry, 1980Exposure of rats to a 50% N2O/oxygen mixture led to a rapid loss of methionine synthase activity in both liver and brain. This enzyme has vitamin B12 as a cofactor. There was impaired conversion of deoxyuridine to deoxythymidine by bone marrow cells and this defect followed loss of methionine synthase activity. There was no homocystinuria.
R, Deacon +6 more
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Biochemistry, 2007
Methionine synthase (MS) is a cobalamin-dependent enzyme. It transfers a methyl group from methyltetrahydrofolate to homocysteine forming methionine and tetrahydrofolate. On the basis of sequence similarity with Escherichia coli cobalamin-dependent MS (MetH), human MS comprises four discrete functional modules that bind from the N- to C-terminus ...
Wolthers, Kirsten R., Scrutton, Nigel S.
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Methionine synthase (MS) is a cobalamin-dependent enzyme. It transfers a methyl group from methyltetrahydrofolate to homocysteine forming methionine and tetrahydrofolate. On the basis of sequence similarity with Escherichia coli cobalamin-dependent MS (MetH), human MS comprises four discrete functional modules that bind from the N- to C-terminus ...
Wolthers, Kirsten R., Scrutton, Nigel S.
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Methionine synthase from pig liver
1997Publisher Summary This chapter discusses methionine synthase from pig liver. Several methods are available for assaying methionine synthase. Mammalian methionine synthase serves two major metabolic functions. It recycles homocysteine—a toxic catabolite of S-adenosylmethionine (AdoMet)—and converts the circulating form of folic acid—5-CH 3 -H 4 folate—
R, Banerjee, Z, Chen, S, Gulati
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Interaction of Flavodoxin with Cobalamin-Dependent Methionine Synthase
Biochemistry, 2000Cobalamin-dependent methionine synthase catalyzes the transfer of a methyl group from methyltetrahydrofolate to homocysteine, forming tetrahydrofolate and methionine. The Escherichia coli enzyme, like its mammalian homologue, is occasionally inactivated by oxidation of the cofactor to cob(II)alamin.
D A, Hall +4 more
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Synthetic Models for the Zinc Sites in the Methionine Synthases
Inorganic Chemistry, 2000The syntheses and molecular structures of a series of tetrahedral zinc complexes designed to model the active sites in Escherichia coli methionine synthases are reported. [PhTttBu]ZnBr (PhTttBu = phenyltris((tert-butylthio)-methyl)borate) was prepared and characterized crystallographically to provide entry into [S3]ZnX complexes.
S J, Chiou +5 more
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JBIC Journal of Biological Inorganic Chemistry, 2012
Density functional theory has been applied to investigate the methyl transfer from methylcobalamin (MeCbl) cofactor to homocysteine (Hcy) as catalyzed by methionine synthase (MetH). Specifically, the S(N)2 and the reductive elimination pathways have been probed as the possible mechanistic pathways for the methyl transfer reaction.
Pawel M, Kozlowski +3 more
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Density functional theory has been applied to investigate the methyl transfer from methylcobalamin (MeCbl) cofactor to homocysteine (Hcy) as catalyzed by methionine synthase (MetH). Specifically, the S(N)2 and the reductive elimination pathways have been probed as the possible mechanistic pathways for the methyl transfer reaction.
Pawel M, Kozlowski +3 more
openaire +2 more sources