| Автор | Brown, C. Kent |
| Автор | Vetting, Matthew W. |
| Автор | Earhart, Cathleen A. |
| Автор | Ohlendorf, Douglas H. |
| Дата выпуска | 2004 |
| dc.description | ▪ 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. |
| Формат | application.pdf |
| Издатель | Annual Reviews |
| Копирайт | Annual Reviews |
| Название | BIOPHYSICAL ANALYSES OF DESIGNED AND SELECTED MUTANTS OF PROTOCATECHUATE 3,4-DIOXYGENASE <sup>1</sup> |
| DOI | 10.1146/annurev.micro.57.030502.090927 |
| Print ISSN | 0066-4227 |
| Журнал | Annual Review of Microbiology |
| Том | 58 |
| Первая страница | 555 |
| Последняя страница | 585 |
| Аффилиация | 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 |
