Discovery and characterization of a putrescine oxidase from Rhodococcus erythropolis NCIMB 11540
نویسندگان
چکیده
منابع مشابه
Extracellular Cholesterol Oxidase from Rhodococcus sp.: Isolation and Molecular Characterization
Background: Cholesterol oxidase (CHO) has various clinical and industrial applications. Recently, microbial CHO have received a great attention for their wide usage in medicine. Here, taxonomic characterizations of isolated strain from soil, optimization of the conditions for CHO production and biochemical characterizations of produced CHO enzyme were described. Finally, CHO gene was cloned int...
متن کاملCharacterization of catechol catabolic genes from Rhodococcus erythropolis 1CP.
The biochemical characterization of the muconate and the chloromuconate cycloisomerases of the chlorophenol-utilizing Rhodococcus erythropolis strain 1CP previously indicated that efficient chloromuconate conversion among the gram-positive bacteria might have evolved independently of that among gram-negative bacteria. Based on sequences of the N terminus and of tryptic peptides of the muconate ...
متن کاملextracellular cholesterol oxidase from rhodococcus sp.: isolation and molecular characterization
background: cholesterol oxidase (cho) has various clinical and industrial applications. recently, microbial cho have received a great attention for their wide usage in medicine. here, taxonomic characterizations of isolated strain from soil, optimization of the conditions for cho production and biochemical characterizations of produced cho enzyme were described. finally, cho gene was cloned int...
متن کاملIsolation and Characterization of Carbendazim-degrading Rhodococcus erythropolis djl-11
Carbendazim (methyl 1H-benzimidazol-2-yl carbamate) is one of the most widely used fungicides in agriculture worldwide, but has been reported to have adverse effects on animal health and ecosystem function. A highly efficient carbendazim-degrading bacterium (strain dj1-11) was isolated from carbendazim-contaminated soil samples via enrichment culture. Strain dj1-11 was identified as Rhodococcus...
متن کاملADP competes with FAD binding in putrescine oxidase.
Putrescine oxidase from Rhodococcus erythropolis NCIMB 11540 (PuO(Rh)) is a soluble homodimeric flavoprotein of 100 kDa, which catalyzes the oxidative deamination of putrescine and some other aliphatic amines. The initial characterization of PuO(Rh) uncovered an intriguing feature: the enzyme appeared to contain only one noncovalently bound FAD cofactor per dimer. Here we show that this low FAD...
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ژورنال
عنوان ژورنال: Applied Microbiology and Biotechnology
سال: 2008
ISSN: 0175-7598,1432-0614
DOI: 10.1007/s00253-007-1310-4