Abstract:
: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 alpha-carbonic anhydrase enzymes. The zinc has three histidine ligands and a single water at 1.98 A. This is quite different from the beta-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.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Cox EH,McLendon GL,Morel FM,Lane TW,Prince RC,Pickering IJ,George GNdoi
10.1021/bi001416ssubject
Has Abstractpub_date
2000-10-10 00:00:00pages
12128-30issue
40eissn
0006-2960issn
1520-4995pii
bi001416sjournal_volume
39pub_type
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