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Protein Science, Vol 3, Issue 10 1644-1650, Copyright © 1994 by Cold Spring Harbor Laboratory Press

INVITED PAPER, SPECIAL SECTION IN HONOR OF MAX PERUTZ

The three-dimensional structures of mutants of porphobilinogen deaminase: Toward an understanding of the structural basis of acute intermittent porphyria

P. D. BROWNLIE, R. LAMBERT, G. V. LOUIE, P. M. JORDAN, T. L. BLUNDELL, M. J. WARREN, J. B. COOPER and S. P. WOOD
Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, University of London, Malet St., London WC1E7HX, United Kingdom Present address: European Molecular Biology Laboratory, Postfach 1022.40, DW-6900 Heidelberg, Germany.

Mutations in the human gene for the enzyme porphobilinogen deaminase give rise to an inherited disease of heme biosynthesis, acute intermittent porphyria. Knowledge of the 3-dimensional structure of human porphobilinogen deaminase, based on the structure of the bacterial enzyme, allows correlation of structure with gene organization and leads to an understanding of the relationship between mutations in the gene, structural and functional changes of the enzyme, and the symptoms of the disease. Most mutations occur in exons 10 and 12, often changing amino acids in the active site. Several of these are shown to be involved in binding the primer or substrate; none modifies Asp 84, which is essential for catalytic activity.
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