Journal article
Aromatic metabolism in Rhizobium trifolii - protocatechuate 3,4-dioxygenase
Archives of Microbiology, Vol.138(3), pp.187-190
1984
Abstract
Protocatechuate 3,4-dioxygenase (EC 1.13.11.3) has been purified 42-fold from 4-hydroxybenzoate-grown cells of Rhizobium trifolii TA1, where it constitutes about 2% of the cell protein. The dioxygenase has a molecular weight of 220,000, with two dissimilar sub-units of molecular weights 29,000 and 26,500, corresponding to an α4β4 composition. The enzyme is specific for protocatechuate, with a Km of 1.75×10-5 M and maximum activity at pH 9.2. Metal removal and replacement studies indicate that the enzyme contains complexed Fe3+ which is required for activity. Direct atomic absorption analysis gave 1.3–1.5 g atoms Fe3+ per mole of isolated enzyme, but correction for metal-deficient proteins suggests that the value is close to 2.
Details
- Title
- Aromatic metabolism in Rhizobium trifolii - protocatechuate 3,4-dioxygenase
- Authors/Creators
- Y.P. Chen (Author/Creator)M.J. Dilworth (Author/Creator)A.R. Glenn (Author/Creator)
- Publication Details
- Archives of Microbiology, Vol.138(3), pp.187-190
- Publisher
- Springer Verlag
- Identifiers
- 991005542977407891
- Murdoch Affiliation
- School of Environmental and Life Sciences
- Language
- English
- Resource Type
- Journal article
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- Citation topics
- 3 Agriculture, Environment & Ecology
- 3.83 Bioengineering
- 3.83.323 Bioremediation
- Web Of Science research areas
- Microbiology
- ESI research areas
- Microbiology