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1975 1
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1982 3
1983 1
1986 1
1987 1
1988 4
1989 2
1990 5
1991 1
1992 3
1993 4
1994 5
1995 6
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1997 8
1998 4
1999 4
2000 4
2001 8
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Page 1
Insights into the reactivation of cobalamin-dependent methionine synthase.
Koutmos M, Datta S, Pattridge KA, Smith JL, Matthews RG. Koutmos M, et al. Among authors: matthews rg. Proc Natl Acad Sci U S A. 2009 Nov 3;106(44):18527-32. doi: 10.1073/pnas.0906132106. Epub 2009 Oct 21. Proc Natl Acad Sci U S A. 2009. PMID: 19846791 Free PMC article.
Cobalamin-dependent methionine synthase (MetH) is a modular protein that catalyzes the transfer of a methyl group from methyltetrahydrofolate to homocysteine to produce methionine and tetrahydrofolate. The cobalamin cofactor, which serves as both acceptor and donor of the …
Cobalamin-dependent methionine synthase (MetH) is a modular protein that catalyzes the transfer of a methyl group from methyltetrahyd …
A love affair with vitamins.
Matthews RG. Matthews RG. J Biol Chem. 2009 Sep 25;284(39):26217-28. doi: 10.1074/jbc.X109.041178. Epub 2009 Jul 13. J Biol Chem. 2009. PMID: 19596855 Free PMC article. No abstract available.
Cobalamin- and corrinoid-dependent enzymes.
Matthews RG. Matthews RG. Met Ions Life Sci. 2009;6:53-114. doi: 10.1039/BK9781847559159-00053. Epub 2009 Jan 30. Met Ions Life Sci. 2009. PMID: 20877792 Free PMC article.
These enzymes fall into two broad classes, those using methylcobalamin or related methylcorrinoids as prosthetic groups and catalyzing methyl transfer reactions, and those using adenosylcobalamin as the prosthetic group and catalyzing the generation of substrate radicals t …
These enzymes fall into two broad classes, those using methylcobalamin or related methylcorrinoids as prosthetic groups and catalyzing me …
Cobalamin-dependent and cobamide-dependent methyltransferases.
Matthews RG, Koutmos M, Datta S. Matthews RG, et al. Curr Opin Struct Biol. 2008 Dec;18(6):658-66. doi: 10.1016/j.sbi.2008.11.005. Curr Opin Struct Biol. 2008. PMID: 19059104 Free PMC article. Review.
Methyltransferases that employ cobalamin cofactors, or their analogs the cobamides, as intermediates in catalysis of methyl transfer play vital roles in energy generation in anaerobic unicellular organisms. In a broader range of organisms they are involved in the conversio …
Methyltransferases that employ cobalamin cofactors, or their analogs the cobamides, as intermediates in catalysis of methyl transfer …
Spectroscopic study of the cobalamin-dependent methionine synthase in the activation conformation: effects of the Y1139 residue and S-adenosylmethionine on the B12 cofactor.
Liptak MD, Datta S, Matthews RG, Brunold TC. Liptak MD, et al. Among authors: matthews rg. J Am Chem Soc. 2008 Dec 3;130(48):16374-81. doi: 10.1021/ja8038129. J Am Chem Soc. 2008. PMID: 19006389 Free PMC article.
The cobalamin-dependent methionine synthase (MetH) from Escherichia coli is a modular enzyme that catalyzes a methyl group transfer from methyltetrahydrofolate to homocysteine via a methylcob(III)alamin (MeCbl) intermediate, generating tetrahydrofolate and methionine (Met) …
The cobalamin-dependent methionine synthase (MetH) from Escherichia coli is a modular enzyme that catalyzes a methyl group transfer f …
A disulfide-stabilized conformer of methionine synthase reveals an unexpected role for the histidine ligand of the cobalamin cofactor.
Datta S, Koutmos M, Pattridge KA, Ludwig ML, Matthews RG. Datta S, et al. Among authors: matthews rg. Proc Natl Acad Sci U S A. 2008 Mar 18;105(11):4115-20. doi: 10.1073/pnas.0800329105. Epub 2008 Mar 10. Proc Natl Acad Sci U S A. 2008. PMID: 18332423 Free PMC article.
B(12)-dependent methionine synthase (MetH) from Escherichia coli is a large modular protein that is alternately methylated by methyltetrahydrofolate to form methylcobalamin and demethylated by homocysteine to form cob(I)alamin. ...Here, we describe an x-ray structure of th …
B(12)-dependent methionine synthase (MetH) from Escherichia coli is a large modular protein that is alternately methylated by methylt …
Metal active site elasticity linked to activation of homocysteine in methionine synthases.
Koutmos M, Pejchal R, Bomer TM, Matthews RG, Smith JL, Ludwig ML. Koutmos M, et al. Among authors: matthews rg. Proc Natl Acad Sci U S A. 2008 Mar 4;105(9):3286-91. doi: 10.1073/pnas.0709960105. Epub 2008 Feb 22. Proc Natl Acad Sci U S A. 2008. PMID: 18296644 Free PMC article.
Enzymes possessing catalytic zinc centers perform a variety of fundamental processes in nature, including methyl transfer to thiols. Cobalamin-independent (MetE) and cobalamin-dependent (MetH) methionine synthases are two such enzyme families. ...Specifically, zinc is mobi …
Enzymes possessing catalytic zinc centers perform a variety of fundamental processes in nature, including methyl transfer to thiols. …
Ligand trans influence governs conformation in cobalamin-dependent methionine synthase.
Fleischhacker AS, Matthews RG. Fleischhacker AS, et al. Among authors: matthews rg. Biochemistry. 2007 Oct 30;46(43):12382-92. doi: 10.1021/bi701367c. Epub 2007 Oct 9. Biochemistry. 2007. PMID: 17924667 Free PMC article.
Cobalamin-dependent methionine synthase (MetH) of Escherichia coli is a large, modular enzyme that uses a cobalamin prosthetic group as a donor or acceptor in three separate methyl transfer reactions. The prosthetic group alternates between methylcobalamin and cob(I)alamin …
Cobalamin-dependent methionine synthase (MetH) of Escherichia coli is a large, modular enzyme that uses a cobalamin prosthetic group as a do …
114 results