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© Ahmed Haouz
Cristaux d'une protéine de Mycobacterium tuberculosis produits dans le cadre du Grand Programme Horizontal sur la Tuberculose à l'Institut Pasteur. La caractérisation structurale de protéines mycobactériennes aide à une meilleure compréhension de la physiologie et de la pathogénicité des mycobactéries et fournit un point de départ pour la conception de nouveaux agents antibactériens.
Publication : FEBS letters

Recombinant plant gamma carbonic anhydrase homotrimers bind inorganic carbon

Team: Crystallography
Member: Ahmed Haouz
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in FEBS letters - 04 Oct 2009

Martin V, Villarreal F, Miras I, Navaza A, Haouz A, González-Lebrero RM, Kaufman SB, Zabaleta E

Link to Pubmed [PMID] – 19808034

FEBS Lett. 2009 Nov;583(21):3425-30

Gamma carbonic anhydrases (gammaCA) are widespread in Prokaryotes. In Eukaryotes, homologous genes were found only in plant genomes. In Arabidopsis and maize, the corresponding gene products are subunits of mitochondrial Complex I. At present, only gammaCA homotrimers of Methanosarcina thermophila (CAM) show reversible carbon dioxide (CO(2)) hydration activity. In the present work, it is shown that recombinant plant gammaCA2 could form homotrimers and bind H(14)CO(3)(-). However, they are unable to catalyse the reversible hydration of CO(2). These results suggest that plant gammaCAs do not act as carbonic anhydrases but with a related activity possibly contributing to recycle CO(2) in the context of photorespiration.