Literature DB >> 10771446

Crystallization and preliminary crystallographic analysis of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli.

F M Ferreira1, G Mendoza-Hernández, M L Calcagno, F Minauro, L F Delboni, G Oliva.   

Abstract

N-Acetylglucosamine 6-phosphate deacetylase (E.C. 3.5.1.25), an enzyme from Escherichia coli involved in aminosugar catabolism, has been crystallized by the vapour-diffusion technique using phosphate as precipitant. X-ray diffraction experiments show the crystals to belong to the orthorhombic crystal system, with space group P2(1)2(1)2. The unit-cell parameters are a = 82.09 (2), b = 114.50 (1), c = 80.17 (1) A. The crystals diffract to a maximum resolution of 1.8 A and an initial data set was collected to 2.0 A.

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Year:  2000        PMID: 10771446     DOI: 10.1107/s0907444900003668

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  2 in total

1.  N-acetylglucosamine 6-phosphate deacetylase (nagA) is required for N-acetyl glucosamine assimilation in Gluconacetobacter xylinus.

Authors:  Vikas Yadav; Bruce Panilaitis; Hai Shi; Keiji Numuta; Kyongbum Lee; David L Kaplan
Journal:  PLoS One       Date:  2011-06-02       Impact factor: 3.240

2.  Structural and functional determination of homologs of the Mycobacterium tuberculosis N-acetylglucosamine-6-phosphate deacetylase (NagA).

Authors:  Mohd Syed Ahangar; Christopher M Furze; Collette S Guy; Charlotte Cooper; Kathryn S Maskew; Ben Graham; Alexander D Cameron; Elizabeth Fullam
Journal:  J Biol Chem       Date:  2018-05-04       Impact factor: 5.157

  2 in total

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