The Active Site Structure of Thalassiosira weissflogii Carbonic Anhydrase 1
X-ray absorption spectroscopy at the Zn K-edge indicates that the active site of the marine diatom Thalassiosira weissflogii carbonic anhydrase is strikingly similar to that of mammalian α-carbonic anhydrase enzymes. The zinc has three histidine ligands and a single water at 1.98 Å. This is quite di...
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Veröffentlicht in: | Biochemistry (Easton) 2000-10, Vol.39 (40), p.12128-12130 |
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Hauptverfasser: | , , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | X-ray absorption spectroscopy at the Zn K-edge indicates that the active site of the marine diatom Thalassiosira weissflogii carbonic anhydrase is strikingly similar to that of mammalian α-carbonic anhydrase enzymes. The zinc has three histidine ligands and a single water at 1.98 Å. This is quite different from the β-carbonic anhydrases of higher plants in which zinc is coordinated by two cysteine thiolates, one histidine, and a water molecule. The diatom carbonic anhydrase shows no significant sequence similarity with other carbonic anhydrases and may represent an example of convergent evolution at the molecular level. |
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ISSN: | 0006-2960 1520-4995 |
DOI: | 10.1021/bi001416s |