Biochemistry: A cadmium enzyme from a marine diatom

@article{Lane2005BiochemistryAC,
  title={Biochemistry: A cadmium enzyme from a marine diatom},
  author={Todd W. Lane and Mak A. Saito and Graham N. George and Ingrid J. Pickering and Roger C. Prince and François M M 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… 

Cadmium-Containing Carbonic Anhydrase CDCA1 in Marine Diatom Thalassiosira weissflogii

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.

Diversity of the cadmium-containing carbonic anhydrase in marine diatoms and natural waters.

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.

Prokaryotic carbonic anhydrases of Earth's environment.

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.

Expression of cadmium carbonic anhydrase of diatoms in seawater

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.

Expression and regulation of carbonic anhydrases in the marine diatom Thalassiosira pseudonana and in natural phytoplankton assemblages from Great Bay, New Jersey.

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.

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

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.

An External d-Carbonic Anhydrase in a Free-Living Marine Dinoflagellate May Circumvent Diffusion-Limited Carbon Acquisition 1 [ W ]

A carbonic anhydrase (CA) from the free-living marine dinoflagellate Lingulodinium polyedrum that appears to play a role in carbon acquisition is identified and results suggest that this enzyme may help to increase CO2 availability at the cell surface.

A new widespread subclass of carbonic anhydrase in marine phytoplankton

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.
...

References

SHOWING 1-10 OF 10 REFERENCES

A biological function for cadmium in marine diatoms.

  • T. LaneF. M. Morel
  • Environmental Science, Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 2000
Evidence is provided of a biological role for Cd in the marine diatom Thalassiosira weissflogii under conditions of low zinc, typical of the marine environment, and of a Cd-specific CA which can replace the Zn enzyme TWCA1 in its carbon-concentrating mechanism.

A Novel Evolutionary Lineage of Carbonic Anhydrase (ε Class) Is a Component of the Carboxysome Shell

It is reported that the carboxysomal shell protein, CsoS3, from Halothiobacillus neapolitanus is a novel carbonic anhydrase (epsilon-class CA) that has an evolutionary lineage distinct from those previously recognized in animals, plants, and other prokaryotes.

Prokaryotic carbonic anhydrases.

Recent work has shown that carbonic anhydrase is widespread in metabolically diverse species from both the Archaea and Bacteria domains indicating that the enzyme has a more extensive and fundamental role in prokaryotic biology than previously recognized.

Cadmium and cobalt substitution for zinc in a marine diatom

In sea water with low Zn concentration, mimicking conditions of the ocean surface waters, Cd stimulates the growth of the marine diatom Thalassiosira weissflogii by substituting for Zn in certain macromolecules, indicating that Co could be an important nutrient for algal growth for reasons other than its role in vitamin B12.

Zinc and carbon co-limitation of marine phytoplankton

PROCESSES that control carbon uptake by marine phytoplankton are important in the global carbon cycle11–3. Uptake of CO2 itself may be limited by diffusion4. Bicarbonate uptake may be limited by zinc

Environmental Genome Shotgun Sequencing of the Sargasso Sea

Over 1.2 million previously unknown genes represented in these samples, including more than 782 new rhodopsin-like photoreceptors are identified, suggesting substantial oceanic microbial diversity.

The active site architecture of Pisum sativum β‐carbonic anhydrase is a mirror image of that of α‐carbonic anhydrases

Despite differing folds, α‐ and β‐carbonic anhydrase have converged upon a very similar active site design and are likely to share a common mechanism.

On the marine geochemistry of cadmium

STUDIES of the geochemistry of trace metals in sea water are of great potential importance, given the wide diversity in their properties. Knowledge of their distribution provides information not only