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2012
Abstract The heme dioxygenase enzymes involved in tryptophan oxidation catalyse the first and rate-limiting step in the kynurenine pathway—the O 2 -dependent oxidation of l-tryptophan to N -formylkynurenine. In the past 10 years, there have been substantial new developments, including new structural information, bacterial expression systems for a ...
Efimov, I +5 more
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Abstract The heme dioxygenase enzymes involved in tryptophan oxidation catalyse the first and rate-limiting step in the kynurenine pathway—the O 2 -dependent oxidation of l-tryptophan to N -formylkynurenine. In the past 10 years, there have been substantial new developments, including new structural information, bacterial expression systems for a ...
Efimov, I +5 more
openaire +2 more sources
Biochemical and Biophysical Research Communications, 2005
Mats Hamberg +3 more
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Mats Hamberg +3 more
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1975
Publisher Summary Pyrocatechase was isolated from cells of a pseudomonad, which catalyzed oxidative ring cleavage of the benzene ring of catechol forming cis, cis-muconic acid as the reaction product. This enzyme exhibited properties unlike those of an oxidase or dehydrogenase because it was not associated with any of the previously known coenzymes ...
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Publisher Summary Pyrocatechase was isolated from cells of a pseudomonad, which catalyzed oxidative ring cleavage of the benzene ring of catechol forming cis, cis-muconic acid as the reaction product. This enzyme exhibited properties unlike those of an oxidase or dehydrogenase because it was not associated with any of the previously known coenzymes ...
openaire +1 more source