Literature DB >> 12876365

Crystallization and preliminary X-ray analysis of alginate lyase, a member of family PL-7, from Pseudomonas aeruginosa.

Masayuki Yamasaki1, Satoko Moriwaki, Wataru Hashimoto, Bunzo Mikami, Kousaku Murata.   

Abstract

Alginate lyase depolymerizes alginate, a heteropolysaccharide consisting of alpha-L-guluronate and beta-D-mannuronate, through a beta-elimination reaction. A protein PA1167 with a molecular mass of 25 kDa produced by Pseudomonas aeruginosa is an alginate lyase classified into polysaccharide lyase family PL-7. The enzyme was crystallized at 293 K in a drop solution comprising 1.4 M sodium chloride, 0.1 M potassium sodium phosphate and 0.1 M 2-morpholinoethanesulfonate-sodium hydroxide pH 6.5 by means of the vapor-diffusion method. The crystals were monoclinic and belonged to space group P2(1), with unit-cell parameters a = 43.4, b = 70.3, c = 67.4 A, beta = 94.5 degrees. Diffraction data were collected to 2.0 A from a single crystal.

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Year:  2003        PMID: 12876365     DOI: 10.1107/s0907444903012836

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


  2 in total

1.  Origin and diversity of alginate lyases of families PL-5 and -7 in Sphingomonas sp. strain A1.

Authors:  Osamu Miyake; Akihito Ochiai; Wataru Hashimoto; Kousaku Murata
Journal:  J Bacteriol       Date:  2004-05       Impact factor: 3.490

2.  Characterization of three new Azotobacter vinelandii alginate lyases, one of which is involved in cyst germination.

Authors:  Martin Gimmestad; Helga Ertesvåg; Tonje Marita Bjerkan Heggeset; Olav Aarstad; Britt Iren Glaerum Svanem; Svein Valla
Journal:  J Bacteriol       Date:  2009-05-29       Impact factor: 3.490

  2 in total

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