Purification and characterization of morphinone reductase from Pseudomonas putida M10
نویسندگان
چکیده
منابع مشابه
Purification and characterization of morphinone reductase from Pseudomonas putida M10.
The NADH-dependent morphinone reductase from Pseudomonas putida M10 catalyses the reduction of morphinone and codeinone to hydromorphone and hydrocodone respectively. Morphinone reductase was purified from crude cell extracts to apparent homogeneity in a single affinity-chromatography step using Mimetic Yellow 2. The purified enzyme was a dimeric flavoprotein with two identical subunits of M(r)...
متن کاملIsolation, Purification and Characterization of Proline Dehydrogenase from a Pseudomonas putida POS-F84 Isolate
The purpose of this study was to isolate and characterize Proline Dehydrogenase (ProDH) enzyme frommicroorganisms isolated from soil in Iran. Isolation and screening of L-proline degradative enzymes from soilsamples was carried out. The isolate was characterized by biochemical markers and 16S rRNA geneanalysis. The target ProDH was purified and the effects of pH and temperatur...
متن کاملPurification to homogeneity and characterization of a novel Pseudomonas putida chromate reductase.
Cr(VI) (chromate) is a widespread environmental contaminant. Bacterial chromate reductases can convert soluble and toxic chromate to the insoluble and less toxic Cr(III). Bioremediation can therefore be effective in removing chromate from the environment, especially if the bacterial propensity for such removal is enhanced by genetic and biochemical engineering. To clone the chromate reductase-e...
متن کاملNucleotide sequence and over-expression of morphine dehydrogenase, a plasmid-encoded gene from Pseudomonas putida M10.
Pseudomonas putida M10 was originally isolated from factory waste liquors by selection for growth on morphine. The NADP(+)-dependent morphine dehydrogenase that initiates morphine catabolism is encoded by a large plasmid of 165 kb. Treatment of P. putida M10 with ethidium bromide led to the isolation of a putative plasmid-free strain that was incapable of growth on morphine. The structural gene...
متن کاملPurification of 2,3-dihydroxybiphenyl 1,2-dioxygenase from Pseudomonas putida OU83 and characterization of the gene (bphC).
The 2,3-dihydroxybiphenyl 1,2-dioxygenase (2,3-DBPD) of Pseudomonas putida OU83 was constitutively expressed and purified to apparent homogeneity. The apparent molecular mass of the native enzyme was 256 kDa, and the subunit molecular mass was 32 kDa. The data suggested that 2,3-DBPD was an octamer of identical subunits. The nucleotide sequence of a DNA fragment containing the bphC region was d...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1994
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3010097