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aci-reductone oxidase (CO-forming)

Known as: E2 metalloenzyme, acireductone dioxygenase 
National Institutes of Health

Papers overview

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Review
2020
Review
2020
Nickel enzymes, present in archaea, bacteria, plants, and primitive eukaryotes are divided into redox and nonredox enzymes and… 
Review
2014
Review
2014
2011
2011
Heterotrimeric G protein complexes are conserved from plants to mammals, but the complexity of each system varies. Arabidopsis… 
Highly Cited
2009
Highly Cited
2009
Crop plants require nitrogen for key macromolecules, such as DNA, proteins and metabolites, yet they are generally inefficient at… 
2008
2008
The two acireductone dioxygenase (ARD) isozymes from the methionine salvage pathway of Klebsiella ATCC 8724 present an unusual… 
Highly Cited
2005
Highly Cited
2005
Methylthioadenosine (MTA) is formed as a by-product of ethylene biosynthesis from S-adenosyl-L-methionine (AdoMet). The… 
2005
2005
The synthesis, characterization, and reactivity properties of a mononuclear Ni(II) cis-beta-keto-enolate complex, [(6-Ph2TPA)Ni… 
Highly Cited
2002
Highly Cited
2002
Here we report the structure of acireductone dioxygenase (ARD), the first determined for a new family of metalloenzymes. ARD… 
2002
2002
Acireductone dioxygenases (ARDs) are enzymes involved in the methionine recycle pathway, which regulates aspects of the cell…