Degradation of 2-Nitrobenzoate byBurkholderia terraeStrain KU-15
نویسندگان
چکیده
منابع مشابه
New metabolic pathway for degradation of 2-nitrobenzoate by Arthrobacter sp. SPG
Arthrobacter sp. SPG utilized 2-nitrobenzoate as its sole source of carbon and energy and degraded it with accumulation of stoichiometric amounts of nitrite ions. Salicylate and catechol were detected as metabolites of the 2-nitrobenzoate degradation using high performance liquid chromatography and gas chromatography-mass spectrometry. Enzyme activities for 2-nitrobenzoate-2-monooxygenase, sali...
متن کاملCrystal Structure of L-Histidinium 2-Nitrobenzoate
A new nonlinear optical organic compound, namely, L-histidinium 2-nitrobenzoate (abbreviated as LH2NB (I); ([C(6)H(10)N(3)O(2)](+) [C(7)H(4)NO(4)](-))), was synthesized. The molecular structure of LH2NB (I) was elucidated using single crystal X-ray diffraction technique. The second harmonic generation (SHG) efficiency of this compound is about two times that of the standard potassium dihydrogen...
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Pseudomonas fluorescens strain KU-7 is a prototype microorganism that metabolizes 2-nitrobenzoate (2-NBA) via the formation of 3-hydroxyanthranilate (3-HAA), a known antioxidant and reductant. The initial two steps leading to the sequential formation of 2-hydroxy/aminobenzoate and 3-HAA are catalyzed by a NADPH-dependent 2-NBA nitroreductase (NbaA) and 2-hydroxylaminobenzoate mutase (NbaB), res...
متن کاملCloning and characterization of the genes for p-nitrobenzoate degradation from Pseudomonas pickettii YH105.
Pseudomonas pickettii YH105 was isolated for its ability to utilize p-nitrobenzoate as the sole source of carbon, nitrogen, and energy. Degradation of p-nitrobenzoate by this strain proceeds through a reductive route as evidenced by the accumulation of ammonia in the culture medium during growth on p-nitrobenzoate. Enzyme assays and high-performance liquid chromatography (HPLC) analysis of cult...
متن کاملPurification and characterization of Ku-2, an octamer-binding protein related to the autoantigen Ku.
The octamer motif (ATTTGCAT) is an important regulatory element in eukaryotic gene expression. A previously unidentified protein that recognizes this motif has been isolated from the human B cell line, Daudi. The protein, which we term Ku-2, bears a close resemblance to the DNA-binding autoantigen Ku. Like Ku, it is a heterodimer with subunits of 83 and 72 kDa; antisera raised against either su...
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ژورنال
عنوان ژورنال: Bioscience, Biotechnology, and Biochemistry
سال: 2007
ISSN: 0916-8451,1347-6947
DOI: 10.1271/bbb.60419