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

Erskine, Peter T., Senior, Natalie, Maignan, S., Cooper, J., Lambert, Richard, Lewis, Gareth, Spencer, Paul, Awan, Sarah, Warren, Martin J., Tickle, Ian J., and others. (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. (doi:10.1002/pro.5560060820) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:11092)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
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
DOI/Identification number: 10.1002/pro.5560060820
Uncontrolled keywords: Crystallography, X-Ray Escherichia coli/*enzymology Porphobilinogen Synthase/*chemistry Saccharomyces cerevisiae/*enzymology Species Specificity
Subjects: Q Science
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Martin Warren
Date Deposited: 16 Oct 2009 08:11 UTC
Last Modified: 23 Jan 2020 04:02 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/11092 (The current URI for this page, for reference purposes)
Warren, Martin J.: https://orcid.org/0000-0002-6028-6456
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