PUBLICATION
Eukaryotic copper-only superoxide dismutases (SODs): A new class of SOD enzymes and SOD-like protein domains
- Authors
- Robinett, N.G., Peterson, R.L., Culotta, V.C.
- ID
- ZDB-PUB-190307-1
- Date
- 2018
- Source
- The Journal of biological chemistry 293: 4636-4643 (Journal)
- Registered Authors
- Keywords
- copper, metalloprotein, redox signaling, superoxide dismutase (SOD), superoxide ion
- MeSH Terms
-
- Copper*/chemistry
- Copper*/metabolism
- Metalloproteins*/chemistry
- Metalloproteins*/classification
- Metalloproteins*/metabolism
- Fungi/enzymology*
- Fungal Proteins*/chemistry
- Fungal Proteins*/classification
- Fungal Proteins*/metabolism
- Superoxide Dismutase*/chemistry
- Superoxide Dismutase*/classification
- Superoxide Dismutase*/metabolism
- Mycobacterium/enzymology*
- Zinc*/chemistry
- Zinc*/metabolism
- Oomycetes/enzymology*
- Periplasmic Proteins*/chemistry
- Periplasmic Proteins*/classification
- Periplasmic Proteins*/metabolism
- PubMed
- 29259135 Full text @ J. Biol. Chem.
Citation
Robinett, N.G., Peterson, R.L., Culotta, V.C. (2018) Eukaryotic copper-only superoxide dismutases (SODs): A new class of SOD enzymes and SOD-like protein domains. The Journal of biological chemistry. 293:4636-4643.
Abstract
The copper-containing superoxide dismutases (SODs) represent a large family of enzymes that participate in the metabolism of reactive oxygen species by disproportionating superoxide anion radical to oxygen and hydrogen peroxide. Catalysis is driven by the redox-active copper ion, and in most cases, SODs also harbor a zinc at the active site that enhances copper catalysis and stabilizes the protein. Such bimetallic Cu,Zn-SODs are widespread, from the periplasm of bacteria to virtually every organelle in the human cell. However, a new class of copper-containing SODs has recently emerged that function without zinc. These copper-only enzymes serve as extracellular SODs in specific bacteria (i.e. Mycobacteria), throughout the fungal kingdom, and in the fungus-like oomycetes. The eukaryotic copper-only SODs are particularly unique in that they lack an electrostatic loop for substrate guidance and have an unusual open-access copper site, yet they can still react with superoxide at rates limited only by diffusion. Copper-only SOD sequences similar to those seen in fungi and oomycetes are also found in the animal kingdom, but rather than single-domain enzymes, they appear as tandem repeats in large polypeptides we refer to as CSRPs (copper-only SOD-repeat proteins). Here, we compare and contrast the Cu,Zn versus copper-only SODs and discuss the evolution of copper-only SOD protein domains in animals and fungi.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping