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Article: Cobalamin- and corrinoid-dependent enzymes.

Matthews, Rowena G

Metal ions in life sciences

2009 Volume 6, Page(s) 53–114

Abstract: This chapter reviews the literature on cobalamin- and corrinoid-containing enzymes. These enzymes fall into two broad classes, those using methylcobalamin or related methylcorrinoids as prosthetic groups and catalyzing methyl transfer reactions, and ... ...

Abstract	This chapter reviews the literature on cobalamin- and corrinoid-containing enzymes. 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 that in turn undergo rearrangements and/or eliminations.
Language	English
Publishing date	2009-01-30
Publishing country	Germany
Document type	Journal Article
ISSN	1559-0836
ISSN	1559-0836
DOI	10.1039/BK9781847559159-00053
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Article ; Online: A love affair with vitamins.

Matthews, Rowena G

The Journal of biological chemistry

2009 Volume 284, Issue 39, Page(s) 26217–26228

MeSH term(s)	5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase/chemistry ; 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase/metabolism ; Crystallography, X-Ray ; Dihydrolipoamide Dehydrogenase/chemistry ; Dihydrolipoamide Dehydrogenase/metabolism ; Disulfides/chemistry ; Disulfides/metabolism ; Folic Acid/chemistry ; Folic Acid/metabolism ; Humans ; Methylenetetrahydrofolate Reductase (NADPH2)/chemistry ; Methylenetetrahydrofolate Reductase (NADPH2)/metabolism ; Molecular Structure ; Oxidation-Reduction ; Protein Conformation ; Tetrahydrofolates/chemistry ; Tetrahydrofolates/metabolism ; Thioctic Acid/analogs & derivatives ; Thioctic Acid/chemistry ; Thioctic Acid/metabolism ; Vitamins/chemistry ; Vitamins/metabolism
Chemical Substances	Disulfides ; Tetrahydrofolates ; Vitamins ; 5,10-methylenetetrahydrofolic acid (0SXY5ET48B) ; dihydrolipoamide (3884-47-7) ; 5,6,7,8-tetrahydrofolic acid (43ZWB253H4) ; Thioctic Acid (73Y7P0K73Y) ; Folic Acid (935E97BOY8) ; Methylenetetrahydrofolate Reductase (NADPH2) (EC 1.5.1.20) ; Dihydrolipoamide Dehydrogenase (EC 1.8.1.4) ; 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase (EC 2.1.1.13)
Language	English
Publishing date	2009-07-13
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.X109.041178
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Article: A Love Affair with Vitamins

Matthews, Rowena G

Journal of biological chemistry. 2009 Sept. 25, v. 284, no. 39

2009

Language	English
Dates of publication	2009-0925
Size	p. 26217-26228.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
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Article: Methylenetetrahydrofolate reductase: a common human polymorphism and its biochemical implications.

Matthews, Rowena G

Chemical record (New York, N.Y.)

2002 Volume 2, Issue 1, Page(s) 4–12

Abstract: Methlenetetrahydrofolate (CH2-H4folate) is required for the conversion of homocysteine to methionine and of dUMP to dTMP in support of DNA synthesis, and also serves as a major source of one carbon unit for purine biosynthesis. This review presents ... ...

Abstract	Methlenetetrahydrofolate (CH2-H4folate) is required for the conversion of homocysteine to methionine and of dUMP to dTMP in support of DNA synthesis, and also serves as a major source of one carbon unit for purine biosynthesis. This review presents biochemical studies of a human polymorphism in methylenetetrahydrofolate reductase, which catalyzes the reaction shown below. The mutation decreases the flux of CH2-H4folate into CH3-H4folate, and is associated with both beneficial and deleterious effects that can be traced to the molecular effect of the substitution of alanine 222 by valine.
MeSH term(s)	Amino Acid Substitution ; Animals ; Catalysis ; Folic Acid/metabolism ; Humans ; Kinetics ; Methylation ; Methylenetetrahydrofolate Reductase (NADPH2) ; Mutation ; Oxidoreductases Acting on CH-NH Group Donors/genetics ; Oxidoreductases Acting on CH-NH Group Donors/metabolism ; Oxidoreductases Acting on CH-NH Group Donors/physiology ; Polymorphism, Genetic
Chemical Substances	Folic Acid (935E97BOY8) ; Oxidoreductases Acting on CH-NH Group Donors (EC 1.5.-) ; Methylenetetrahydrofolate Reductase (NADPH2) (EC 1.5.1.20)
Language	English
Publishing date	2002
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2044646-9
ISSN	1528-0691 ; 1527-8999
ISSN (online)	1528-0691
ISSN	1527-8999
DOI	10.1002/tcr.10006
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Article ; Online: Oxidation of cysteine 645 of cobalamin-independent methionine synthase causes a methionine limitation in Escherichia coli.

Hondorp, Elise R / Matthews, Rowena G

Journal of bacteriology

2009 Volume 191, Issue 10, Page(s) 3407–3410

Abstract: Cobalamin-independent methionine synthase (MetE) catalyzes the final step in Escherichia coli methionine biosynthesis but is inactivated under oxidative conditions, triggering a methionine deficiency. This study demonstrates that the mutation of MetE ... ...

Abstract	Cobalamin-independent methionine synthase (MetE) catalyzes the final step in Escherichia coli methionine biosynthesis but is inactivated under oxidative conditions, triggering a methionine deficiency. This study demonstrates that the mutation of MetE cysteine 645 to alanine completely eliminates the methionine auxotrophy imposed by diamide treatment, suggesting that modulation of MetE activity via cysteine 645 oxidation has significant physiological consequences for oxidatively stressed cells.
MeSH term(s)	Alanine/genetics ; Alanine/physiology ; Cysteine/genetics ; Cysteine/physiology ; Diamide/pharmacology ; Escherichia coli/drug effects ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Methionine/metabolism ; Methyltransferases/drug effects ; Methyltransferases/genetics ; Methyltransferases/metabolism ; Mutation ; Oxidation-Reduction/drug effects ; Structure-Activity Relationship
Chemical Substances	Diamide (10465-78-8) ; Methionine (AE28F7PNPL) ; Methyltransferases (EC 2.1.1.-) ; 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase (EC 2.1.1.14) ; Cysteine (K848JZ4886) ; Alanine (OF5P57N2ZX)
Language	English
Publishing date	2009-03-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.01722-08
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Article: Defects in homocysteine metabolism: diversity among hyperhomocyst(e)inemias.

Matthews, Rowena G / Elmore, C Lee

Clinical chemistry and laboratory medicine

2007 Volume 45, Issue 12, Page(s) 1700–1703

Abstract: There are now four genetic mouse models that induce hyperhomocyst(e)inemia by decreasing the activity of an enzyme involved in homocysteine metabolism: cystathionine beta-synthase, methylenetetrahydrofolate reductase, methionine synthase and methionine ... ...

Abstract	There are now four genetic mouse models that induce hyperhomocyst(e)inemia by decreasing the activity of an enzyme involved in homocysteine metabolism: cystathionine beta-synthase, methylenetetrahydrofolate reductase, methionine synthase and methionine synthase reductase. While each enzyme deficiency leads to murine hyperhomocyst(e)inemia, the accompanying metabolic profiles are significantly and often unexpectedly, different. Deficiencies in cystathionine beta-synthase lead to elevated plasma methionine, while deficiencies of the remaining three enzymes lead to hypomethioninemia. The liver [S-adenosylmethionine]/[S-adenosylhomocysteine] ratio is decreased in mice lacking methylenetetrahydrofolate reductase or cystathionine beta-synthase, but unexpectedly increased in mice with deficiencies in methionine synthase or methionine synthase reductase. Folate pool imbalances are observed in complete methylenetetrahydrofolate reductase deficiency, where methyltetra-hydrofolate is a minor component, and in methionine synthase reductase deficiency, where methyltetrahydrofolate is increased relative to wild-type mice. These differences illustrate the potential diversity among human patients with hyperhomocyst(e)inemia, and strengthen the argument that the pathologies associated with the dissimilar forms of the condition will require different treatments.
MeSH term(s)	Animals ; Homocysteine/blood ; Humans ; Hyperhomocysteinemia/blood ; Mice ; Models, Animal
Chemical Substances	Homocysteine (0LVT1QZ0BA)
Language	English
Publishing date	2007-08-30
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	1418007-8
ISSN	1437-4331 ; 1434-6621 ; 1437-8523
ISSN (online)	1437-4331
ISSN	1434-6621 ; 1437-8523
DOI	10.1515/CCLM.2007.324
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Article: Catalysis and regulation - from structure to function.

Dijkstra, Bauke W / Matthews, Rowena G

Current opinion in structural biology

2004 Volume 13, Issue 6, Page(s) 706–708

MeSH term(s)	Catalysis ; Enzyme Activation ; Enzymes/chemistry ; Enzymes/metabolism ; Homeostasis/physiology ; Protein Conformation ; Structure-Activity Relationship
Chemical Substances	Enzymes
Language	English
Publishing date	2004-03-01
Publishing country	England
Document type	Editorial ; Review
ZDB-ID	1068353-7
ISSN	0959-440X
ISSN	0959-440X
DOI	10.1016/j.sbi.2003.10.014
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Article: Ligand trans influence governs conformation in cobalamin-dependent methionine synthase.

Fleischhacker, Angela S / Matthews, Rowena G

Biochemistry

2007 Volume 46, Issue 43, Page(s) 12382–12392

Abstract: 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 ... ...

Abstract	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 during catalysis as homocysteine is converted to methionine using a methyl group derived from methyltetrahydrofolate. Occasional oxidation of cob(I)alamin to cob(II)alamin inactivates the enzyme. Reductive methylation with flavodoxin and adenosylmethionine returns the enzyme to an active methylcobalamin state. At different points during the reaction cycle, the coordination state of the cobalt of the cobalamin changes. The imidazole side chain of His759 coordinates to cobalamin in a "His-on" state and dissociates to produce a "His-off" state. The His-off state has been associated with a conformation of MetH that is poised for reactivation of cobalamin by reductive methylation rather than catalysis. Our studies on cob(III)alamins bound to MetH, specifically aqua-, methyl-, and n-propylcobalamin, show a correlation between the accessibility of the reactivation conformation and the order of the established ligand trans influence. The trans influence also controls the affinity of MetH in the cob(III)alamin form for flavodoxin. Flavodoxin, which acts to shift the conformational equilibrium toward the reactivation conformation, binds less tightly to MetH when the cob(III)alamin has a strong trans ligand and therefore has less positive charge on cobalt. These results are compared to those for cob(II)alamin MetH, illustrating that access to the reactivation conformation is governed by the net charge on the cobalt as well as the trans influence in cob(III)alamins.
MeSH term(s)	5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase/chemistry ; 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase/metabolism ; Ligands ; Protein Conformation ; Spectrophotometry/methods ; Vitamin B 12/metabolism
Chemical Substances	Ligands ; 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase (EC 2.1.1.13) ; Vitamin B 12 (P6YC3EG204)
Language	English
Publishing date	2007-10-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi701367c
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Article: Folate Biosynthesis, Reduction, and Polyglutamylation and the Interconversion of Folate Derivatives.

Green, Jacalyn M / Matthews, Rowena G

EcoSal Plus

2007 Volume 2, Issue 2

Abstract: Many microorganisms and plants possess the ability to synthesize folic acid derivatives de novo, initially forming dihydrofolate. All the folic acid derivatives that serve as recipients and donors of one-carbon units are derivatives of tetrahydrofolate, ... ...

Abstract	Many microorganisms and plants possess the ability to synthesize folic acid derivatives de novo, initially forming dihydrofolate. All the folic acid derivatives that serve as recipients and donors of one-carbon units are derivatives of tetrahydrofolate, which is formed from dihydrofolate by an NADPH-dependent reduction catalyzed by dihydrofolate reductase (FolA). This review discusses the biosynthesis of dihydrofolate monoglutamate, its reduction to tetrahydrofolate monoglutamate, and the addition of glutamyl residues to form folylpolyglutamates. Escherichia coli and Salmonella, like many microorganisms that can synthesize folate de novo, appear to lack the ability to transport folate into the cell and are thus highly susceptible to inhibitors of folate biosynthesis. The review includes a brief discussion of the inhibition of folate biosynthesis by sulfa drugs. The folate biosynthetic pathway can be divided into two sections. First, the aromatic precursor chorismate is converted to paminobenzoic acid (PABA) by the action of three proteins. Second, the pteridine portion of folate is made from GTP and coupled to PABA to generate dihydropteroate, and the bifunctional protein specified by folC, dihydrofolate synthetase, or folylpolyglutamate synthetase, adds the initial glutamate molecule to form dihydrofolate (H2PteGlu1, or dihydropteroylmonoglutamate). Bacteriophage T4 infection of E. coli has been shown to cause alterations in the metabolism of folate derivatives. Infection is associated with an increase in the chain lengths in folylpolyglutamates and particularly the accumulation of hexaglutamate derivatives.
Language	English
Publishing date	2007-04
Publishing country	United States
Document type	Journal Article
ISSN	2324-6200
ISSN	2324-6200
DOI	10.1128/ecosalplus.3.6.3.6
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Article: The many flavors of hyperhomocyst(e)inemia: insights from transgenic and inhibitor-based mouse models of disrupted one-carbon metabolism.

Elmore, C Lee / Matthews, Rowena G

Antioxidants & redox signaling

2007 Volume 9, Issue 11, Page(s) 1911–1921

Abstract: Mouse models that perturb homocysteine metabolism, including genetic mouse models that result in deficiencies of methylenetetrahydrofolate reductase, methionine synthase, methionine synthase reductase, and cystathionine beta-synthase, and a ... ...

Abstract	Mouse models that perturb homocysteine metabolism, including genetic mouse models that result in deficiencies of methylenetetrahydrofolate reductase, methionine synthase, methionine synthase reductase, and cystathionine beta-synthase, and a pharmaceutically induced mouse model with a transient deficiency in betainehomocysteine methyl transferase, have now been characterized and can be compared. Although each of these enzyme deficiencies is associated with moderate to severe hyperhomocyst(e)inemia, the broader metabolic profiles are profoundly different. In particular, the various models differ in the degree to which tissue ratios of S-adenosylmethionine to S-adenosylhomocysteine are reduced in the face of elevated plasma homocyst(e)ine, and in the distribution of the tissue folate pools. These different metabolic profiles illustrate the potential complexities of hyperhomocyst(e)inemia in humans and suggest that comparison of the disease phenotypes of the various mouse models may be extremely useful in dissecting the underlying risk factors associated with human hyperhomocyst(e)inemia.
MeSH term(s)	5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase/blood ; 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase/chemistry ; 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase/metabolism ; Animals ; Cystathionine beta-Synthase/blood ; Cystathionine beta-Synthase/chemistry ; Cystathionine beta-Synthase/metabolism ; Disease Models, Animal ; Ferredoxin-NADP Reductase/blood ; Ferredoxin-NADP Reductase/chemistry ; Ferredoxin-NADP Reductase/metabolism ; Hyperhomocysteinemia/enzymology ; Hyperhomocysteinemia/metabolism ; Methylenetetrahydrofolate Reductase (NADPH2)/blood ; Methylenetetrahydrofolate Reductase (NADPH2)/chemistry ; Methylenetetrahydrofolate Reductase (NADPH2)/metabolism ; Mice ; Mice, Transgenic ; Models, Biological ; Molecular Structure ; S-Adenosylhomocysteine/metabolism ; S-Adenosylmethionine/metabolism
Chemical Substances	S-Adenosylmethionine (7LP2MPO46S) ; S-Adenosylhomocysteine (979-92-0) ; methionine synthase reductase (EC 1.18.1.-) ; Ferredoxin-NADP Reductase (EC 1.18.1.2) ; Methylenetetrahydrofolate Reductase (NADPH2) (EC 1.5.1.20) ; 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase (EC 2.1.1.13) ; Cystathionine beta-Synthase (EC 4.2.1.22)
Language	English
Publishing date	2007-11
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1483836-9
ISSN	1557-7716 ; 1523-0864
ISSN (online)	1557-7716
ISSN	1523-0864
DOI	10.1089/ars.2007.1795
Database	MEDical Literature Analysis and Retrieval System OnLINE

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