Structure and metal exchange in the cadmium carbonic anhydrase of marine diatoms

@article{Xu2008StructureAM,
  title={Structure and metal exchange in the cadmium carbonic anhydrase of marine diatoms},
  author={Yan Xu and Liang Dong Feng and Philip D. Jeffrey and Yigong Shi and François M M Morel},
  journal={Nature},
  year={2008},
  volume={452},
  pages={56-61}
}
Carbonic anhydrase, a zinc enzyme found in organisms from all kingdoms, catalyses the reversible hydration of carbon dioxide and is used for inorganic carbon acquisition by phytoplankton. In the oceans, where zinc is nearly depleted, diatoms use cadmium as a catalytic metal atom in cadmium carbonic anhydrase (CDCA). Here we report the crystal structures of CDCA in four distinct forms: cadmium-bound, zinc-bound, metal-free and acetate-bound. Despite lack of sequence homology, CDCA is a… Expand
Cadmium‐Carbonic Anhydrase
Cadmium-carbonic anhydrase (CDCA1) is a ζ-carbonic anhydrase (CA) isolated from the marine diatom Thalassiosira weissflogii, which naturally uses Cd as its metal cofactor. Its homolog gene has beenExpand
Expression of cadmium carbonic anhydrase of diatoms in seawater
TLDR
CDCA is indeed expressed in ocean waters and is regulated in a manner consistent with its putative role in CO 2 acquisition, and a high level of CDCA expression was found in samples from the Equatorial Pacific and coastal New Jersey. Expand
Structural and inhibition insights into carbonic anhydrase CDCA1 from the marine diatom Thalassiosira weissflogii.
TLDR
The characterization of zeta-CA, a novel enzyme in the marine diatom Thalassiosira weissflogii, which consists of three repeats, has been completed, reporting the X-ray structure of the last repeat, CDCA1-R3 in its cadmium-bound form, and presenting a model of the full length protein obtained by docking approaches. Expand
Cadmium-Containing Carbonic Anhydrase CDCA1 in Marine Diatom Thalassiosira weissflogii
TLDR
The biochemical and structural features of CDCA1 enzyme will be presented together with its putative biotechnological applications for the detection of metal ions in seawaters. Expand
Catalytic activity of a ζ-class zinc and cadmium containing carbonic anhydrase. Compared work mechanisms.
TLDR
This study was inspired by the discovery that the replacement of zinc ion with cadmium does not entail significant differences in the catalytic performance of the enzyme and focused its attention on a carbonic anhydrase cambialistic enzyme belonging to this new class. Expand
δ-Carbonic Anhydrases: Structure, Distribution, and Potential Roles
TLDR
Intriguingly, primary structure alignments suggest the presence of a single large insert in the δ-CAs compared with the α-C as, and tertiary structure predictions suggest a common structure with a zinc atom in the active site coordinated by three histidine residues in both classes. Expand
Insights on the Functions and Ecophysiological Relevance of the Diverse Carbonic Anhydrases in Microalgae
TLDR
This review describes the essential role in carbon dioxide-concentrating mechanisms and photosynthesis, their regulation, as well as their less studied roles in non-photosynthetic processes and the presence in some microalgae of cambialistic CAs. Expand
Carbonic anhydrases--an overview.
Carbonic anhydrases (CAs, EC 4.2.1.1) are widespread metalloenzymes all over the phylogenetic tree, with at least 4 distinct gene families encoding for them. At least 16 different alpha-CA isoformsExpand
Carbonic anhydrase — a universal enzyme of the carbon-based life
TLDR
The existence of an extensive family of CA-related proteins (γCA-RPs) is proposed–the inactive forms of γ-CAs, which are widespread among the Archaea, Bacteria, and, to a lesser extent, in Eukarya. Expand
Crystal structure of a highly thermostable carbonic anhydrase from Persephonella marina EX-H1
Bacterial α-type carbonic anhydrase (α-CA) is a zinc metalloenzyme that catalyzes the reversible and extremely rapid interconversion of carbon dioxide to bicarbonate. In this study, we report theExpand
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