Enzyme-catalyzed methyl transfers to thiols: the role of zinc. (Q47830031)

6 February 2018

review article

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title

Enzyme-catalyzed methyl transfers to thiols: the role of zinc. (English)

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6 February 2018

author name string

Matthews RG

series ordinal

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6 February 2018

Goulding CW

series ordinal

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6 February 2018

publication date

1 October 1997

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6 February 2018

Current Opinion in Chemical Biology

published in

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6 February 2018

volume

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6 February 2018

issue

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6 February 2018

page(s)

332-339

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6 February 2018

Repair of DNA methylphosphotriesters through a metalloactivated cysteine nucleophile

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Positive and negative regulation of transcription by a cleavage product of Ada protein

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Zinc binding by the methylation signaling domain of the Escherichia coli Ada protein

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Solution structure of the DNA methyl phosphotriester repair domain of Escherichia coli Ada

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Backbone dynamics, amide hydrogen exchange, and resonance assignments of the DNA methylphosphotriester repair domain of Escherichia coli Ada using NMR.

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Metal-coordination sphere in the methylated Ada protein-DNA co-complex

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Alkyl Transfer to Metal Thiolates: Kinetics, Active Species Identification, and Relevance to the DNA Methyl Phosphotriester Repair Center of Escherichia coli Ada.

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Mechanistic Studies of the Methyltransferase from Clostridium thermoaceticum: Origin of the pH Dependence of the Methyl Group Transfer from Methyl Tetrahydrofolate to the Corrinoid/Iron-Sulfur Protein

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Comparison of cobalamin-independent and cobalamin-dependent methionine synthases from Escherichia coli: two solutions to the same chemical problem

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Cobalamin-independent methionine synthase from Escherichia coli: a zinc metalloenzyme

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Structure-based perspectives on B12-dependent enzymes

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Assignment of enzymatic function to specific protein regions of cobalamin-dependent methionine synthase from Escherichia coli.

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Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin, and adenosylmethionine.

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Purification, kinetic properties, and cDNA cloning of mammalian betaine-homocysteine methyltransferase

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The reductive acetyl coenzyme A pathway: sequence and heterologous expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum

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How a protein binds B12: A 3.0 A X-ray structure of B12-binding domains of methionine synthase

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The structure of the C-terminal domain of methionine synthase: presenting S-adenosylmethionine for reductive methylation of B12

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Cloning, sequencing and immunological characterization of the corrinoid-containing subunit of the N5-methyltetrahydromethanopterin: coenzyme-M methyltransferase from Methanobacterium thermoautotrophicum

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The energy conserving N5-methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum is composed of eight different subunits

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The corrinoid-containing 23-kDa subunit MtrA of the energy-conserving N5-methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum. EPR spectroscopic evidence for a histidine residue as a cobalt lig

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Sequence and transcript analysis of a novel Methanosarcina barkeri methyltransferase II homolog and its associated corrinoid protein homologous to methionine synthase

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Reconstitution of Monomethylamine:Coenzyme M methyl transfer with a corrinoid protein and two methyltransferases purified from Methanosarcina barkeri

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Methyltransferases involved in methanol conversion by Methanosarcina barkeri

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Activation mechanism of methanol:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri

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Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression

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Methylcobalamin: coenzyme M methyltransferase isoenzymes MtaA and MtbA from Methanosarcina barkeri. Cloning, sequencing and differential transcription of the encoding genes, and functional overexpression of the mtaA gene in Escherichia coli

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Substitution of cadmium for zinc in farnesyl:protein transferase alters its substrate specificity

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Identification of a cysteine residue essential for activity of protein farnesyltransferase. Cys299 is exposed only upon removal of zinc from the enzyme.

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Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution

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7 January 2021

Evidence for a catalytic role of zinc in protein farnesyltransferase. Spectroscopy of Co2+-farnesyltransferase indicates metal coordination of the substrate thiolate

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Influence of metal ions on substrate binding and catalytic activity of mammalian protein geranylgeranyltransferase type-I

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Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases

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7 January 2021

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Identifiers

DOI

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6 February 2018

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6 February 2018