(Q30432739)

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High expression and steady-state kinetic characterization of methionine site-directed mutants of Escherichia coli methionyl- and selenomethionyl-dihydrofolate reductase

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scholarly article

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Europe PubMed Central

PubMed publication ID

21 June 2017

High expression and steady-state kinetic characterization of methionine site-directed mutants of Escherichia coli methionyl- and selenomethionyl-dihydrofolate reductase (English)

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Europe PubMed Central

PubMed publication ID

21 June 2017

Escherichia coli

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author name string

D Shaw

1

1 reference

Europe PubMed Central

PubMed publication ID

21 June 2017

J D Odom

2

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21 June 2017

R B Dunlap

3

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21 June 2017

language of work or name

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publication date

1 January 1999

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21 June 2017

Biochimica et Biophysica Acta

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21 June 2017

1429

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Europe PubMed Central

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21 June 2017

2

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Europe PubMed Central

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21 June 2017

401-410

1 reference

Europe PubMed Central

PubMed publication ID

21 June 2017

Direct phase determination based on anomalous scattering.

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Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation

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Bis-methionine ligation to heme iron in mutants of cytochrome b562. 1. Spectroscopic and electrochemical characterization of the electronic properties.

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Structure of a methionine-rich segment of Escherichia coli Ffh protein

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Isolation and refolding of a mutant methionine-free interleukin-2-receptor alpha chain synthesized as a fusion protein in Escherichia coli

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A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme

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Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state

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Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding

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Partial 1H NMR assignments of the Escherichia coli dihydrofolate reductase complex with folate: evidence for a unique conformation of bound folate.

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Evidence for two interconverting protein isomers in the methotrexate complex of dihydrofolate reductase from Escherichia coli

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Determination by Raman spectroscopy of the pKa of N5 of dihydrofolate bound to dihydrofolate reductase: mechanistic implications

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Directed mutagenesis of dihydrofolate reductase

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Functional role of aspartic acid-27 in dihydrofolate reductase revealed by mutagenesis

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Hydrophobic interactions via mutants of Escherichia coli dihydrofolate reductase: separation of binding and catalysis.

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Kinetics of substrate, coenzyme, and inhibitor binding to Escherichia coli dihydrofolate reductase.

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Kinetic mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli.

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Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli

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Implications for enzymic catalysis from free-energy reaction coordinate profiles

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The independent distribution of amino acid near neighbor pairs into polypeptides

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Preparation and storage of competent Escherichia coli cells

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Methotrexate-resistant variants of human dihydrofolate reductase with substitutions of leucine 22. Kinetics, crystallography, and potential as selectable markers

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Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence

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Engineering specificity for folate into dihydrofolate reductase from Escherichia coli

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Identifiers

10.1016/S0167-4838(98)00250-7

1 reference

Europe PubMed Central

PubMed publication ID

21 June 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

21 June 2017

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