Crystal Structure of Lactobacillus johnsonii Cinnamoyl Esterase
Author Information
Author(s): Lai Kin-Kwan, Stogios Peter J., Vu Clara, Xu Xiaohui, Cui Hong, Molloy Sara, Savchenko Alexei, Yakunin Alexander, Gonzalez Claudio F.
Primary Institution: University of Florida
Hypothesis
The inserted α/β subdomain is critical for substrate binding and catalysis in the cinnamoyl esterase LJ0536.
Conclusion
The unique structural features of LJ0536 suggest it should be classified in a new group of bacterial cinnamoyl esterases.
Supporting Evidence
- The enzyme LJ0536 is produced by Lactobacillus johnsonii, which is found in the human gut.
- The study identified a unique α/β subdomain that plays a significant role in substrate binding.
- Mutational analysis showed that specific residues in the α/β subdomain are critical for enzyme activity.
- Crystallization of the enzyme revealed its dimeric structure and catalytic pocket characteristics.
Takeaway
This study looks at a special enzyme from a probiotic bacteria that helps break down certain compounds in food, which could be good for our health.
Methodology
The enzyme was crystallized in both apo form and substrate-bound complexes, and its structure was analyzed using X-ray diffraction.
Limitations
The study does not explore the direct involvement of enzymatic activity in the observed health benefits.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website