NDLI: The mammalian molybdenum enzymes of mARC

Content Provider	Springer Nature Link
Author	Ott, Gudrun Havemeyer, Antje Clement, Bernd
Copyright Year	2014
Abstract	The “mitochondrial amidoxime reducing component” (mARC) is the most recently discovered molybdenum-containing enzyme in mammals. All mammalian genomes studied to date contain two mARC genes: MARC1 and MARC2. The proteins encoded by these genes are mARC-1 and mARC-2 and represent the simplest form of eukaryotic molybdenum enzymes, only binding the molybdenum cofactor. In the presence of NADH, mARC proteins exert N-reductive activity together with the two electron transport proteins cytochrome b5 type B and NADH cytochrome b5 reductase. This enzyme system is capable of reducing a great variety of N-hydroxylated substrates. It plays a decisive role in the activation of prodrugs containing an amidoxime structure, and in detoxification pathways, e.g., of N-hydroxylated purine and pyrimidine bases. It belongs to a group of drug metabolism enzymes, in particular as a counterpart of P450 formed N-oxygenated metabolites. Its physiological relevance, on the other hand, is largely unknown. The aim of this article is to summarize our current knowledge of these proteins with a special focus on the mammalian enzymes and their N-reductive activity.
Starting Page	265
Ending Page	275
Page Count	11
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	20
Issue Number	2
e-ISSN	14321327
Language	English
Publisher	Springer Berlin Heidelberg
Publisher Date	2014-11-26
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	mARC Moco MOSC Biotransformation Amidoxime Biochemistry Microbiology
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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