Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase1.

C Kent Brown, Matthew W Vetting, Cathleen A Earhart, Douglas H Ohlendorf

Journal: Annual review of microbiology 2004;58():555-85

PMID: 15487948

Abstract

The catechol dioxygenases allow a wide variety of bacteria to use aromatic compounds as carbon sources by catalyzing the key ring-opening step. These enzymes use specifically either catechol or protocatechuate (2,3-dihydroxybenozate) as their substrates; they use a bare metal ion as the sole cofactor. To learn how this family of metalloenzymes functions, a structural analysis of designed and selected mutants of these enzymes has been undertaken. Here we review the results of this analysis on the nonheme ferric iron intradiol dioxygenase protocatechuate 3,4-dioxygenase.

Address: Center for Metals in Biocatalysis and Department of Biochemistry, Molecular Biology, and Biophysics , Minneapolis, Minnesota 55455, USA. [email protected]

DOI: 10.1146/annurev.micro.57.030502.090927

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MeSH Terms: Acinetobacter, Amino Acid Sequence, Catechols, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Point Mutation, Protein Conformation, Protocatechuate-3,4-Dioxygenase, Pseudomonas, Sequence Alignment