Arylformamidase Function Slide 3: Difference between revisions

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


[[Image:arylformamidase_alignment.png|centre|framed|'''Conservation of the catalytic triad between Arylformamidase and 2pbl.''']]
[[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.
- Aspartic acid --> Glutamic acid - Semi-conservative: both polar, acidic.


[[Arylformamidase Function Slide 2| ...Previous slide ]]|[[Arylformamidase| Return to the main page ]]|[[Arylformamidase Function Slide 4| Next slide... ]]
[[Arylformamidase Function Slide 2| ...Previous slide ]]|[[Arylformamidase| Return to the main page ]]|[[Arylformamidase Function Slide 4| Next slide... ]]

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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