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Christian Kubitza

Explore the profile of Christian Kubitza including associated specialties, affiliations and a list of published articles. Areas
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Articles 6
Citations 46
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Recent Articles
1.
Rixen S, Indorf P, Kubitza C, Struwe M, Klopp C, Scheidig A, et al.
Molecules . 2023 Sep; 28(17). PMID: 37687214
The mitochondrial amidoxime reducing component (mARC) is a human molybdoenzyme known to catalyze the reduction of various -oxygenated substrates. The physiological function of mARC enzymes, however, remains unknown. In this...
2.
Indorf P, Kubitza C, Scheidig A, Kunze T, Clement B
J Med Chem . 2019 Dec; 63(12):6538-6546. PMID: 31790578
For the development of new drugs, the investigation of their metabolism is of central importance. In the past, the focus was mostly on the consideration of established enzymes leading to...
3.
Kubitza C, Bittner F, Ginsel C, Havemeyer A, Clement B, Scheidig A
Proc Natl Acad Sci U S A . 2018 Nov; 115(47):11958-11963. PMID: 30397129
Biotransformation enzymes ensure a viable homeostasis by regulating reversible cycles of oxidative and reductive reactions. The metabolism of nitrogen-containing compounds is of high pharmaceutical and toxicological relevance because N-oxygenated metabolites...
4.
Ginsel C, Plitzko B, Froriep D, Stolfa D, Jung M, Kubitza C, et al.
Drug Metab Dispos . 2018 Jul; 46(10):1396-1402. PMID: 30045842
The mitochondrial amidoxime reducing component is a recently discovered molybdenum enzyme in mammals which, in concert with the electron transport proteins cytochrome b5 and NADH cytochrome b5 reductase, catalyzes the...
5.
Kubitza C, Ginsel C, Bittner F, Havemeyer A, Clement B, Scheidig A
Acta Crystallogr F Struct Biol Commun . 2018 Jun; 74(Pt 6):337-344. PMID: 29870017
The human mitochondrial amidoxime reducing component (hmARC) is a molybdenum cofactor-dependent enzyme that is involved in the reduction of a diverse range of N-hydroxylated compounds of either physiological or xenobiotic...
6.
Kubitza C, Faust A, Gutt M, Gath L, Ober D, Scheidig A
Acta Crystallogr D Struct Biol . 2018 May; 74(Pt 5):422-432. PMID: 29717713
The high-resolution crystal structure of the flavin-dependent monooxygenase (FMO) from the African locust Zonocerus variegatus is presented and the kinetics of structure-based protein variants are discussed. Z. variegatus expresses three...