BIOPHYSICAL ANALYSES OF DESIGNED AND SELECTED MUTANTS OF PROTOCATECHUATE 3,4-DIOXYGENASE <sup>1</sup>
Brown, C. Kent; Vetting, Matthew W.; Earhart, Cathleen A.; Ohlendorf, Douglas H.; Brown, C. Kent; 1 Center for Metals in Biocatalysis and Department of Biochemistry, Molecular Biology, and Biophysics , Minneapolis, Minnesota 55455 ; email: brow0927@umn.edu ; earhart@umn.edu ; ohlen@umn.edu
Журнал:
Annual Review of Microbiology
Дата:
2004
Аннотация:
▪ 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.
817.1Кб