@article { , title = {The carbonic anhydrase of Clostridium autoethanogenum represents a new subclass of β-carbonic anhydrases}, abstract = {Carbonic anhydrase catalyses the interconversion of carbon dioxide and water to bicarbonate and protons. It was unknown if the industrial relevant acetogen Clostridium autoethanogenum possesses these enzymes. We identified two putative carbonic anhydrase genes in its genome, one of the β class and one of the γ class. Carbonic anhydrase activity was found for the purified β class enzyme, but not the γ class candidate. Functional complementation of an Escherichia coli carbonic anhydrase knock-out mutant showed that the β class carbonic anhydrase could complement this activity, but not the γ class candidate gene. Phylogenetic analysis showed that the β class carbonic anhydrase of Clostridium autoethanogenum represents a novel sub-class of β class carbonic anhydrases that form the F-clade. The members of this clade have the shortest primary structure of any known carbonic anhydrase.}, doi = {10.1007/s00253-019-10015-w}, eissn = {1432-0614}, issn = {0175-7598}, issue = {17}, journal = {Applied Microbiology and Biotechnology}, note = {For OA.}, pages = {7275-7286}, publicationstatus = {Published}, publisher = {Springer Verlag}, url = {https://nottingham-repository.worktribe.com/output/2357174}, volume = {103}, keyword = {Biotechnology, Applied Microbiology and Biotechnology, General Medicine}, year = {2019}, author = {Pander, Bart and Harris, Gemma and Scott, David J. and Winzer, Klaus and Köpke, Michael and Simpson, Sean D. and Minton, Nigel P. and Henstra, Anne M.} }