The carbonic anhydrase of Clostridium autoethanogenum represents a new subclass of [beta]-carbonic anhydrases

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 [beta] class...

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Bibliographic Details
Published in:Applied microbiology and biotechnology 2019-09, Vol.103 (17), p.7275
Main Authors: Pander, Bart, Harris, Gemma, Scott, David J, Winzer, Klaus, Köpke, Michael, Simpson, Sean D, Minton, Nigel P
Format: Article
Language:English
Subjects:
Analysis
Carbon dioxide
Carbonates
Enzymes
Escherichia coli
Genomics
Phylogeny
Online Access:Get full text
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Summary: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 [beta] class and one of the [gamma] class. Carbonic anhydrase activity was found for the purified [beta] class enzyme, but not the [gamma] class candidate. Functional complementation of an Escherichia coli carbonic anhydrase knock-out mutant showed that the [beta] class carbonic anhydrase could complement this activity, but not the [gamma] class candidate gene. Phylogenetic analysis showed that the [beta] class carbonic anhydrase of Clostridium autoethanogenum represents a novel sub-class of [beta] class carbonic anhydrases that form the F-clade. The members of this clade have the shortest primary structure of any known carbonic anhydrase.
ISSN:0175-7598
1432-0614
DOI:10.1007/s00253-019-10015-w