Biochemistry: A cadmium enzyme from a marine diatom

@article{Lane2005BiochemistryAC,
  title={Biochemistry: A cadmium enzyme from a marine diatom},
  author={T. Lane and M. Saito and G. George and I. Pickering and R. Prince and F. Morel},
  journal={Nature},
  year={2005},
  volume={435},
  pages={42-42}
}
The ocean biota contains a vast reservoir of genomic diversity. Here we present the sequence and preliminary characterization of a protein that is a cadmium-containing carbonic anhydrase from the marine diatom Thalassiosira weissflogii. The existence of a cadmium enzyme in marine phytoplankton may indicate that there is a unique selection pressure for metalloenzymes in the marine environment, and our discovery provides a long-awaited explanation for the nutrient-like behaviour of cadmium in the… 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
Diversity of the cadmium-containing carbonic anhydrase in marine diatoms and natural waters.
TLDR
It is shown that CDCA is widespread in diatom species and ubiquitous in the environment, and the cdca primers developed in this study should be useful for detecting cdca genes in the field, and studying the conditions under which they are expressed. Expand
Prokaryotic carbonic anhydrases of Earth's environment.
TLDR
The physiology and biochemistry of carbonic anhydrases from prokaryotes belonging to the domains Bacteria and Archaea that play key roles in the ecology of Earth's biosphere are focused on. Expand
CDCA1 From Thalassiosira weissflogii as Representative Member of ζ-Class CAs: General Features and Biotechnological Applications
TLDR
The high affinity of CDCA1 active site for cadmium makes this enzyme a good candidate for the development of CA-based biosensors for determination of free metal ions in the seawater, and potential biotechnological applications in CO2 capture processes may also be envisaged. Expand
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
Expression and regulation of carbonic anhydrases in the marine diatom Thalassiosira pseudonana and in natural phytoplankton assemblages from Great Bay, New Jersey.
TLDR
Investigation of expressed sequence tag libraries revealed putative homologs of the archetypal diatom delta-carbonic anhydrase TWCA1 in a broad range of eukaryotic phytoplankton including haptophytes, prasinophytes and dinoflagellates, indicating that this CA is expressed under a broadrange of environmental conditions and not restricted to low pCO(2) and low Zn. Expand
Structure and metal exchange in the cadmium carbonic anhydrase of marine diatoms
TLDR
Despite lack of sequence homology, CDCA is a structural mimic of a functional β-carbonic anhydrase dimer, with striking similarity in the spatial organization of the active site residues. 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
An External d-Carbonic Anhydrase in a Free-Living Marine Dinoflagellate May Circumvent Diffusion-Limited Carbon Acquisition 1 [ W ]
The oceans globally constitute an important sink for carbon dioxide (CO2) due to phytoplankton photosynthesis. However, the marine environment imposes serious restraints to carbon fixation. First,Expand
A new widespread subclass of carbonic anhydrase in marine phytoplankton
TLDR
Different lines of evidence are presented showing that the protein LCIP63, identified in the marine diatom Thalassiosira pseudonana, is a CA, but sequence analysis showed that it has a low identity with any known CA and therefore belongs to a new subclass that the authors designate as iota-CA. Expand
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