Abstract:
Carbonic anhydrases (CAs), the metalloenzymes that catalyze the conversion between carbon dioxide and bicarbonate, continue to be surprising targets, as many exciting new discoveries related to them emerge constantly. This is indeed unprecedented as these are quite "old" enzymes, which were discovered in 1933, and thoroughly investigated since then as drug targets. Furthermore, their inhibitors are in clinical use since the 50s. However, in the last years, a host of interesting reports were made regarding the catalytic/inhibition mechanism as well as isolation/characterization of new isozymes belonging to this family, as well as of CAs of non-vertebrate origin.
Insights
Carbonic anhydrases (CAs), enzymes discovered in 1933, are surprisingly yielding new insights. Recent research reveals novel catalytic mechanisms, isozymes, and non-vertebrate origins for these metalloenzymes.
Area of Science:
- Biochemistry and enzymology
- Metalloprotein chemistry
Background:
- Carbonic anhydrases (CAs) are ancient metalloenzymes catalyzing CO2 hydration.
- CA inhibitors have been clinically utilized since the 1950s.
- Despite extensive historical research, CAs remain active areas of investigation.
Discussion:
- Recent studies explore novel catalytic and inhibition mechanisms of carbonic anhydrases.
- The discovery and characterization of new CA isozymes are expanding the known family.
- Emerging research includes the identification and study of carbonic anhydrases from non-vertebrate sources.
Key Insights:
- Unexpectedly, significant new discoveries continue to emerge for carbonic anhydrases.
- This includes advancements in understanding their catalytic functions and inhibition.
- New isozymes and non-vertebrate CAs broaden the scope of research.
Outlook:
- Continued exploration of CA mechanisms and diversity promises further breakthroughs.
- Investigating non-vertebrate CAs may unveil novel therapeutic targets.
- The ancient nature of CAs belies their ongoing relevance in modern scientific discovery.
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