Evolution of a family of metazoan active-site-serine enzymes from penicillin-binding proteins: a novel facet of the bacterial legacy
2008
Evolution of Metazoan Enzymes from Bacterial Proteins
publication
Evidence: moderate
Author Information
Author(s): Nina Peitsaro, Zydrune Polianskyte, Jarno Tuimala, Isabella Pörn-Ares, Julius Liobikas, Oliver Speer, Dan Lindholm, James Thompson, Ove Eriksson
Primary Institution: University of Helsinki
Hypothesis
We hypothesize that PBP-βL proteins in the early eukaryotic cell enabled the degradation of peptidoglycan from ingested bacteria.
Conclusion
A few PBP-βL proteins were conserved in metazoans, suggesting they have distinct functions in metabolic processes.
Supporting Evidence
- LACTB shares unique structural features with bacterial penicillin-binding proteins.
- Metazoan PBP-βL homologs are active-site-serine enzymes.
- Phylogenetic analysis indicates that metazoan PBP-βL homologs derive from α-proteobacteria.
Takeaway
Some proteins in humans come from bacteria and help with digestion. They might help our cells get energy from food.
Methodology
Phylogenetic and structural analysis of metazoan PBP-βL homologs.
Limitations
The physiological function of LACTB remains unknown.
Digital Object Identifier (DOI)
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