Carbonic anhydrase is an ancient enzyme widespread in prokaryotes.
Carbonic anhydrases catalyze the reversible hydration of CO(2) and are ubiquitous in highly evolved eukaryotes. The recent identification of a third class of carbonic anhydrase (gamma class) in a methanoarchaeon and our present finding that the beta class also extends into thermophilic species from the Archaea domain led us to initiate a systematic search for these enzymes in metabolically and phylogenetically diverse prokaryotes. Here we show that carbonic anhydrase is widespread in the Archaea and Bacteria domains, and is an ancient enzyme. The occurrence in chemolithoautotrophic species occupying deep branches of the universal phylogenetic tree suggests a role for this enzyme in the proposed autotrophic origin of life. The presence of the beta and gamma classes in metabolically diverse species spanning the Archaea and Bacteria domains demonstrates that carbonic anhydrases have a far more extensive and fundamental role in prokaryotic biology than previously recognized.
Smith
K S
KS
Department of Biochemistry, The Pennsylvania State University, University Park, PA 16802, USA.
Jakubzick
C
C
Whittam
T S
TS
Ferry
J G
JG
D001105:Archaea / Q000145:classification / Q000201:enzymology* / Q000235:genetics; D001419:Bacteria / Q000145:classification / Q000201:enzymology* / Q000235:genetics; D002256:Carbonic Anhydrases / Q000145:classification / Q000235:genetics*; D019143:Evolution, Molecular; D010802:Phylogeny; D011387:Prokaryotic Cells / Q000201:enzymology*
D002256:Carbonic Anhydrases