New Class of Alkaline Phosphatase from Sphingomonas
Author Information
Author(s): Bihani Subhash C., Das Amit, Nilgiriwala Kayzad S., Prashar Vishal, Pirocchi Michel, Apte Shree Kumar, Ferrer Jean-Luc, Hosur Madhusoodan V.
Primary Institution: Bhabha Atomic Research Centre, Trombay, Mumbai, India
Hypothesis
The study investigates the structure and evolutionary significance of a novel alkaline phosphatase (SPAP) from Sphingomonas sp. strain BSAR-1.
Conclusion
The crystal structure of SPAP reveals it as a new class of alkaline phosphatases with unique catalytic and structural features.
Supporting Evidence
- The structure of SPAP shows a threonine as the catalytic residue instead of the typical serine found in other alkaline phosphatases.
- SPAP lacks the third metal ion binding pocket that is conserved in other alkaline phosphatases.
- Unique residues in the active site of SPAP suggest it has evolved independently from other alkaline phosphatases.
Takeaway
Scientists studied a new enzyme from a bacterium that helps break down certain chemicals. They found it works differently than similar enzymes.
Methodology
The enzyme was purified and its crystal structure was determined using X-ray diffraction.
Limitations
The study primarily focuses on structural analysis and does not extensively cover functional assays or in vivo applications.
Digital Object Identifier (DOI)
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