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
Hauptverfasser: Cox, Elizabeth H, McLendon, George L, Morel, François M. M, Lane, Todd W, Prince, Roger C, Pickering, Ingrid J, George, Graham N
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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.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi001416s