Complete inactivation of Escherichia coli uridine phosphorylase by modification of Asp5 with Woodward's reagent K. (Q54613646)

1 June 2018

title

Complete inactivation of Escherichia coli uridine phosphorylase by modification of Asp5 with Woodward's reagent K. (English)

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Komissarov AA

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Romanova DV

series ordinal

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Debabov VG

series ordinal

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language of work or name

English

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publication date

1 April 1995

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Journal of Biological Chemistry

published in

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volume

270

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issue

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page(s)

10050-10055

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Modification of uridine phosphorylase from Escherichia coli by diethyl pyrocarbonate. Evidence for a histidine residue in the active site of the enzyme

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Tissue sulfhydryl groups

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Selective modification of putative uridine-binding site of uridine phosphorylase from E. coli with fluorescein 5'-isothiocyanate.

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37 Uridine nucleosidase from yeast

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Modification of carboxyl groups in bovine carboxypeptidase A. I. Inactivation of the enzyme by N-ethyl-5-phenylisoxazolium-3'-sulfonate (Woodward's reagent K).

21 January 2018

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A spectrophotometric method for quantitation of carboxyl group modification of proteins using Woodward's Reagent K.

21 January 2018

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Nucleotide sequence of the Escherichia coli uridine phosphorylase (udp) gene.

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Uridine phosphorylase, molecular properties, and mechanism of catalysis

21 January 2018

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Differential effects of 2,2'-anhydro-5-ethyluridine, a uridine phosphorylase inhibitor, on the antitumor activity of 5-fluorouridine and 5-fluoro-2'-deoxyuridine

21 January 2018

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New analogues of benzylacyclouridines, specific and potent inhibitors of uridine phosphorylase from human and mouse livers

21 January 2018

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Role of uridine phosphorylase in the anabolism of 5-fluorouracil

21 January 2018

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Inhibition of uridine phosphorylase by pyrimidine nucleoside analogs and consideration of substrate binding to the enzyme based on solution conformation as seen by NMR spectroscopy

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.270.17.10050

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1 June 2018

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1 June 2018