Erratum to: Purification and characterization of protocatechuate 3,4-dioxygenase from Pseudomonas pseudoalcaligenes KF707
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چکیده
منابع مشابه
Purification and characterization of nitrobenzene nitroreductase from Pseudomonas pseudoalcaligenes JS45.
Pseudomonas pseudoalcaligenes JS45 grows on nitrobenzene as a sole source of carbon, nitrogen, and energy. The catabolic pathway involves reduction to hydroxylaminobenzene followed by rearrangement to o-amino-phenol and ring fission (S. F. Nishino and J. C. Spain, Appl. Environ. Microbiol. 59:2520, 1993). A nitrobenzene-inducible, oxygen-insensitive nitroreductase was purified from extracts of ...
متن کاملGenome sequence of the polychlorinated-biphenyl degrader Pseudomonas pseudoalcaligenes KF707.
Pseudomonas pseudoalcaligenes KF707 is a soil polychlorinated biphenyl (PCB) degrader, able to grow both planktonically and as a biofilm in the presence of various toxic metals and metalloids. Here we report the genome sequence (5,957,359 bp) of P. pseudoalcaligenes KF707, which provides insights into metabolic degradation pathways, flagellar motility, and chemotaxis.
متن کاملAnalysis of bph operon from the polychlorinated biphenyl-degrading strain of Pseudomonas pseudoalcaligenes KF707.
The entire nucleotide sequences (6.8 kilobase pairs) of the bphABC genes and their products involved in the initial dioxygenation and ring-meta-cleavage of biphenyls and polychlorinated biphenyls were determined. The first bphA gene starts about a 100 base pairs downstream from the transcriptional initiation site. The bphA region, which encodes a cluster of enzymes including biphenyl dioxygenas...
متن کاملCloning, Expression and Purification of Creatininase From Pseudomonas Pseudoalkaligene KF707 in E. coli.
Creatinine amidohydrolase(EC 3.5.2.10) catalyzes the reversible conversion of creatinine to creatine. Creatininase in combination with other enzymes is used for detection of creatinine in serum and urine which is of significant value for detection of renal, muscular and thyroid functions. The aim of this study was to produce recombinant creatininase enzyme in E.coli expression system to use it ...
متن کاملPurification and partial characterization of an alkaline lipase from Pseudomonas pseudoalcaligenes F-111.
An extracellular alkaline lipase of alkalophilic Pseudomonas pseudoalcaligenes F-111 was purified to homogeneity. The apparent molecular weight determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was 32,000, and the isoelectric point was 7.3. With p-nitrophenyl esters as its substrates, the enzyme shows preference for C12 acyl and C14 acyl groups. It was stable in the pH ran...
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ژورنال
عنوان ژورنال: Journal of the Korean Society for Applied Biological Chemistry
سال: 2013
ISSN: 1738-2203,2234-344X
DOI: 10.1007/s13765-013-3380-6