The active site structure of Thalassiosira weissflogii carbonic anhydrase 1.

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

Biochemistry

journal_title

Biochemistry

authors

Cox EH,McLendon GL,Morel FM,Lane TW,Prince RC,Pickering IJ,George GN

doi

10.1021/bi001416s

subject

Has Abstract

pub_date

2000-10-10 00:00:00

pages

12128-30

issue

40

eissn

0006-2960

issn

1520-4995

pii

bi001416s

journal_volume

39

pub_type

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