Crystallization of 5-aminolaevulinic acid dehydratase from Escherichia coli and Saccharomyces cerevisiae and preliminary X-ray characterization of the crystals

Erskine, P.T. and Senior, N. and Maignan, S. and Cooper, J. and Lambert, R. and Lewis, G. and Spencer, P. and Awan, S. and Warren, M.J. and Tickle, I.J. and Thomas, P. and Wood, S.P. and Shoolingin-Jordan, P.M. (1997) Crystallization of 5-aminolaevulinic acid dehydratase from Escherichia coli and Saccharomyces cerevisiae and preliminary X-ray characterization of the crystals. Protein Science, 6 (8). pp. 1774-6. ISSN 0961-8368 . (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1002/pro.5560060820

Abstract

5-Aminolaevulinic acid dehydratase (ALAD) catalyzes the formation of porphobilinogen from two molecules of 5-aminolaevulinic acid. Both Escherichia coli and Saccharomyces cerevisiae ALADs are homo-octameric enzymes which depend on Zn2+ for catalytic activity and are potently inhibited by lead ions. The E. coli enzyme crystallized in space group I422 (unit cell dimensions a = b = 130.7 A, c = 142.4 A). The best crystals were obtained in the presence of the covalently bound inhibitor laevulinic acid. The yeast enzyme (expressed in E. coli) crystallized in the same space group (I422) but with a smaller unit cell volume (a = b = 103.7 A, c = 167.7 A). High resolution synchrotron data sets were obtained from both E. coli and yeast ALAD crystals by cryocooling to 100 K.

Item Type: Article
Additional information:
Uncontrolled keywords: Crystallography, X-Ray Escherichia coli/*enzymology Porphobilinogen Synthase/*chemistry Saccharomyces cerevisiae/*enzymology Species Specificity
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Martin Warren
Date Deposited: 16 Oct 2009 08:11
Last Modified: 14 Jan 2010 14:42
Resource URI: http://kar.kent.ac.uk/id/eprint/11092 (The current URI for this page, for reference purposes)
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