Cloning, Expression and Characterization of the δ-carbonic Anhydrase of Thalassiosira weissflogii (Bacillariophyceae)
© 2012 Phycological Society of America.
| Veröffentlicht in: | Journal of phycology. - 1966. - 49(2013), 1 vom: 23. Feb., Seite 170-7 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2013
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| Zugriff auf das übergeordnete Werk: | Journal of phycology |
| Schlagworte: | Journal Article Thalassiosira weissflogii carbon-concentrating mechanism esterase activity marine diatom photosynthesis δ-carbonic anhydrase |
| Zusammenfassung: | © 2012 Phycological Society of America. Carbonic anhydrase (CA) is a ubiquitous metalloenzyme responsible for accelerating the interconversion of CO2 and bicarbonate. Although CAs are involved in a broad range of biochemical processes involving carboxylation or decarboxylation reactions, they are of special interest due to their role in photosynthetic CO2 assimilation in marine phytoplankton, especially under low-CO2 conditions. Several phylogenetically independent classes of CAs have been identified in a variety of marine phytoplankton. TWCA1, first discovered in Thalassiosira weissflogii (Grunow) G. Fryxell & Hasle, is the founding member of the δ-class of CAs; these appear to be extracellular enzymes, but are still relatively poorly characterized. To date, it has remained uncertain whether TWCA1 possesses true CA activity due to the difficulty in producing a functional protein in a heterologous expression system. Herein we describe the fusion of a full-length open reading frame of TWCA1 to the coding sequence of a self-splicing intein in a pTWIN2 expression vector that has allowed successful production of a functional enzyme in Escherichia coli. Assay of the recombinant protein shows that TWCA1 is a catalytically active δ-CA possessing both CO2 hydration and esterase activity |
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| Beschreibung: | Date Completed 25.03.2016 Date Revised 24.03.2016 published: Print-Electronic Citation Status PubMed-not-MEDLINE |
| ISSN: | 0022-3646 |
| DOI: | 10.1111/j.1529-8817.2012.01226.x |