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

✍ Scribed by P.T. Erskine; J. Cooper; R. Lambert; G. Lewis; S.P. Wood; P.M. Shoolingin-Jordan; S. Maignan; P. Spencer; N. Senior; S. Awan; M. Warren; I.J. Tickle; P. Thomas

Publisher
Cold Spring Harbor Laboratory Press
Year
1997
Tongue
English
Weight
330 KB
Volume
6
Category
Article
ISSN
0961-8368

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✦ Synopsis

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 Zn^2+^ for catalytic activity and are potently inhibited by lead ions. The E. coli enzyme crystallized in space group 1422 (unit cell dimensions a = b= 130.7 Å, c = 142.4 Å). 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 (1422) but with a smaller unit cell volume (a = b = 103.7 Å, c = 167.7 Å). High resolution synchrotron data sets were obtained from both E. coli and yeast ALAD crystals by cryocooling to 100 K.

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