Purification of arogenate dehydrogenase from Phenylobacterium immobile
Abstract
Phenylobacterium immobile, a bacterium which is able to degrade the herbicide chloridazon, utilizes for L-tyrosine synthesis arogenate as an obligatory intermediate which is converted in the final biosynthetic step by a dehydrogenase to tyrosine. This enzyme, the arogenate dehydrogenase, has been purified for the first time in a 5-step procedure to homogeneity as confirmed by electrophoresis. The M r of the enzyme that consists of two identical subunits amounts to 69000 as established by gel electrophoresis after cross-linking the enzyme with dimethylsuberimidate. The K m values were 0.09 mM for arogenate and 0.02mM for NAD +. The enzyme has a high specificity with respect to its substrate arogenate.
- Publication:
-
FEBS Letters
- Pub Date:
- January 1985
- DOI:
- 10.1016/0014-5793(85)80519-6
- Bibcode:
- 1985FEBSL.179..208M
- Keywords:
-
- L-Tyrosine biosynthesis;
- Arogenate;
- Arogenate dehydrogenase;
- Phenylobacterium immobile