(Q37866109)

24 August 2017

title

Evidence that the fosfomycin target Cys115 in UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) is essential for product release (English)

1 reference

24 August 2017

Susanne Eschenburg

1

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24 August 2017

Melanie Priestman

series ordinal

2

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24 August 2017

Ernst Schönbrunn

series ordinal

3

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24 August 2017

language of work or name

English

0 references

publication date

5 November 2004

1 reference

Journal of Biological Chemistry

24 August 2017

number of pages

7

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based on heuristic

inferred from page(s)

published in

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24 August 2017

volume

280

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24 August 2017

issue

5

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24 August 2017

page(s)

3757-3763

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Recent advances in the formation of the bacterial peptidoglycan monomer unit

24 August 2017

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A new view of the mechanisms of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA) derived from X-ray structures of their tetrahedral reaction intermediate states

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Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA

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Characterization of a Cys115 to Asp substitution in the Escherichia coli cell wall biosynthetic enzyme UDP-GlcNAc enolpyruvyl transferase (MurA) that confers resistance to inactivation by the antibiotic fosfomycin.

21 January 2018

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Role of the loop containing residue 115 in the induced-fit mechanism of the bacterial cell wall biosynthetic enzyme MurA

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In vitro and in vivo functional activity of Chlamydia MurA, a UDP-N-acetylglucosamine enolpyruvyl transferase involved in peptidoglycan synthesis and fosfomycin resistance

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Nonenzymatic Breakdown of the Tetrahedral (α-Carboxyketal Phosphate) Intermediates of MurA and AroA, Two Carboxyvinyl Transferases. Protonation of Different Functional Groups Controls the Rate and Fate of Breakdown

21 January 2018

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Alteration of a single amino acid residue reverses fosfomycin resistance of recombinant MurA from Mycobacterium tuberculosis

21 January 2018

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Analysis of Fluoromethyl Group Chirality Establishes a Common Stereochemical Course for the Enolpyruvyl Transfers Catalyzed by EPSP Synthase and UDP-GlcNAc Enolpyruvyl Transferase†

21 January 2018

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20 May 2022

https://opencitations.net/index/coci/api/v1/citations/10.1107/S0907444998003254

Identifiers

DOI

10.1074/JBC.M411325200

1 reference

24 August 2017

1 reference