Characterization of a novel type of carbonic anhydrase that acts without metal cofactors.

ABSTRACT:

Background

Carbonic anhydrases (CAs) are universal metalloenzymes that catalyze the reversible conversion of carbon dioxide (CO₂) and bicarbonate (HCO₃^-). They are involved in various biological processes, including pH control, respiration, and photosynthesis. To date, eight evolutionarily unrelated classes of CA families (α, β, γ, δ, ζ, η, θ, and ι) have been identified. All are characterized by an active site accommodating the binding of a metal cofactor, which is assumed to play a central role in catalysis. This feature is thought to be the result of convergent evolution.

Results

Here, we report that a previously uncharacterized protein group, named "COG4337," constitutes metal-independent CAs from the newly discovered ι-class. Genes codin

SUBMITTER: Hirakawa Y 

PROVIDER: S-EPMC8132391 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature