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Updated: Mar 2, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
Published on: November 22, 2014
The molybdenum cofactor enzyme mARC: Moonlighting or promiscuous enzyme?
Angel Llamas1, Alejandro Chamizo-Ampudia1, Manuel Tejada-Jimenez1
1Dpto. de Bioquímica y Biología Molecular, Campus de Rabanales y Campus Internacional de Excelencia Agroalimentario (CeiA3), Edif. Severo Ochoa, Universidad de Córdoba, Spain.
Mitochondrial Amidoxime Reducing Component (mARC) is a newly identified enzyme that reduces amidoximes and N-hydroxylated compounds. This review proposes mARC is a moonlighting enzyme with potential roles in nitric oxide formation.
Area of Science:
- Biochemistry
- Enzymology
- Molecular Biology
Background:
- Molybdenum cofactor (Moco) is essential for four known eukaryotic enzymes.
- A fifth Moco-containing enzyme, mARC, has been identified.
- mARC reduces amidoximes, N-hydroxylated compounds, and nitrite.
Purpose of the Study:
- To review current knowledge on mARC.
- To propose mARC as a moonlighting enzyme.
- To explore mARC's role in nitric oxide production.
Main Methods:
- Literature review of mARC function and Moco-containing enzymes.
- Analysis of electron transfer pathways involving mARC, Cytb5, Cytb5-R, and NR.
- Examination of mARC's catalytic activities with various substrates.
Main Results:
- mARC reduces amidoximes and N-hydroxylated compounds.
- mARC can reduce nitrite to nitric oxide (NO), potentially utilizing NR for electron supply.
- mARC exhibits characteristics of a moonlighting enzyme.
Conclusions:
- mARC is a novel Moco-containing enzyme with diverse catalytic functions.
- mARC's role in NO formation suggests a new physiological pathway.
- Evidence supports classifying mARC as a moonlighting enzyme.
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