Arylformamidase Function Slide 3: Difference between revisions

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== Evidence from Similar Structures ==
== Evidence from Similar Sequences ==


A high structural similarity was found between 2pbl and 2c7b, a thermostable carboxylesterase from ... (Z = 24.7, see DALI results). The structure and function of 2c7b has been well characterised (references). From its structure, a catalytic triad has been identified (how?). To elucidate any functional similarity between 2pbl and 2c7b, conservation of the catalytic triad was assessed (see figure ...). Note: the clustalW alignment was found to differ from the alignment provided as part of the DALI results. All three residues were found to be conserved, though H... and E... were found to match is less conserved regions. Thus, it is possible that such conservation is the result of a chance or poor alignment. This might be explained by the poor sequence similarity between 2c7b and 2pdb (16%).  
- Catalytic triad identified in paper - Ser162, Asp247, and His279.  


[[Image:2c7b_alignment.png|centre|framed|'''Conservation of the catalytic triad between 2cb7 and 2pbl.''']]
- To assess functional similarity, conservation of the catalytic triad was analysed.
 
[[Image:arylformamidase_alignment.png|centre|framed|'''ClustalW alignment showing conservation of the catalytic triad between Arylformamidase and 2pbl.''']]
 
- Aspartic acid --> Glutamic acid - Semi-conservative: both polar, acidic.


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Latest revision as of 23:34, 9 June 2008

Evidence from Similar Sequences

- Catalytic triad identified in paper - Ser162, Asp247, and His279.

- To assess functional similarity, conservation of the catalytic triad was analysed.

ClustalW alignment showing conservation of the catalytic triad between Arylformamidase and 2pbl.

- Aspartic acid --> Glutamic acid - Semi-conservative: both polar, acidic.

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