Results 231 to 240 of about 24,002 (247)
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[Predicting the cofactors of oxidoreductases by the modified pseudo-amino acid composition].
Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 2009Types of cofactor independency for newly found oxidoreductases sequences are usually determined by experimental analysis. These experimental methods are both time-consuming and costly. With the explosion of oxidoreductases sequences entering into the databanks, it is highly desirable to explore the feasibility of selectively classifying newly found ...
Guangya, Zhang +2 more
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Endocrinology, 1965
Partially purified mammalian L-amino acid: O2 oxidoreductase, which catalyzes oxidative deamination of thyroid hormones, converted 3:5 diiodo-4-hydroxyphenyl lactic acid to 3:5 diiodo-4-hydroxyphenyl pyruvic acid. It is suggested, therefore, that this enzyme preparation not only deaminates thyroid hormones but also catalyzes the dehydrogenation of ...
MINORU NAKANO +2 more
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Partially purified mammalian L-amino acid: O2 oxidoreductase, which catalyzes oxidative deamination of thyroid hormones, converted 3:5 diiodo-4-hydroxyphenyl lactic acid to 3:5 diiodo-4-hydroxyphenyl pyruvic acid. It is suggested, therefore, that this enzyme preparation not only deaminates thyroid hormones but also catalyzes the dehydrogenation of ...
MINORU NAKANO +2 more
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Archives of Insect Biochemistry and Physiology, 2010
AbstractThe NADPH‐cytochrome P450 oxidoreductase (CYPOR) enzyme is a membrane‐bound protein and contains both FAD and FMN cofactors. The enzyme transfers two electrons, one at a time, from NADPH to cytochrome P450 enzymes to function in the enzymatic reactions.
Songklod, Sarapusit +2 more
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AbstractThe NADPH‐cytochrome P450 oxidoreductase (CYPOR) enzyme is a membrane‐bound protein and contains both FAD and FMN cofactors. The enzyme transfers two electrons, one at a time, from NADPH to cytochrome P450 enzymes to function in the enzymatic reactions.
Songklod, Sarapusit +2 more
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N‐Methyl‐
We found N‐methyl‐l‐amino acid dehydrogenase activity in various bacterial strains, such as Pseudomonas putida and Bacillus alvei, and cloned the gene from P. putida ATCC12633 into Escherichia coli. The enzyme purified to homogeneity from recombinant E.
Hisaaki, Mihara +6 more
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Biochemistry, 1990
NAD(P)H:quinone oxidoreductases (NQOs) are flavoproteins that catalyze the oxidation of NADH or NADPH by various quinones and oxidation-reduction dyes. We have previously described a complementary DNA that encodes a dioxin-inducible cytosolic form of human NAD(P)H:quinone oxidoreductase (NQO1).
A K, Jaiswal +3 more
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NAD(P)H:quinone oxidoreductases (NQOs) are flavoproteins that catalyze the oxidation of NADH or NADPH by various quinones and oxidation-reduction dyes. We have previously described a complementary DNA that encodes a dioxin-inducible cytosolic form of human NAD(P)H:quinone oxidoreductase (NQO1).
A K, Jaiswal +3 more
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POLYNUCLEOTIDE ENCODING AN AMINO ACID SEQUENCE, ENCODING AN OXIDOREDUCTASE
2022SCHAFFER STEFFEN +7 more
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[Glutamic acid oxidoreductase activity of polyanhydro-alpha-amino acids (proteinoids)].
Die Naturwissenschaften, 1968G, Krampitz, W, Haas, S, Baars-Diehl
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