Temperature- and detergent-dependent oligomeric structures of flavoprotein monohydroxybenzoate hydroxylases from Rhodococcus erythropolis
Author:
Publisher
Elsevier BV
Subject
Applied Microbiology and Biotechnology,Biotechnology
Reference12 articles.
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2. Purification and properties of three types of monohydroxybenzoate monooxygenase from Rhodococcus erythropolis S-1;Suemori;Biosci. Biotech. Biochem.,1993
3. Crystallization and properties of p-hydroxybenzoate hydroxylase from Pseudomonas putida;Hosokawa;J. Biol. Chem.,1966
4. Participation of iron and flavin adenine dinucleotide on the enzymatic hydroxylation of p-hydroxybenzoate;Yano;Agr. Biol. Chem.,1966
5. Purification and properties of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens;Howell;J. Biol. Chem.,1972
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1. Variability of enzyme system ofNocardioformbacteria as a basis of their metabolic activity;Journal of Environmental Science and Health, Part B;2008-03-28
2. Biodegradation of mixture containing monohydroxybenzoate isomers by Acinetobacter calcoaceticus;World Journal of Microbiology and Biotechnology;2007-09-09
3. Biocatalytic Potential ofp-Hydroxybenzoate Hydroxylase fromRhodococcus rhodnii 135 andRhodococcus opacus 557;Advanced Synthesis & Catalysis;2004-02
4. Purification and properties of p-hydroxybenzoate hydroxylases from Rhodococcus strains;Biochemistry (Moscow);2001
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