Arylformamidase Function Slide 2: Difference between revisions

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


Screening of BLAST result (see Sebastien) for associated literature.
- Screening of BLAST result (see Sebastien) for associated literature.


Resulted in the same paper as the literature search.
- Resulted in the same paper as the literature search.


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


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|'''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 1| ...Previous slide ]]|[[Arylformamidase| Return to the main page ]]|[[Arylformamidase Function Slide 3| Next slide... ]]
[[Arylformamidase Function Slide 1| ...Previous slide ]]|[[Arylformamidase| Return to the main page ]]|[[Arylformamidase Function Slide 3| Next slide... ]]

Revision as of 11:56, 8 June 2008

Evidence from Similar Sequences

- Screening of BLAST result (see Sebastien) for associated literature.

- Resulted in the same paper as the literature search.

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

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

Conservation of the catalytic triad between Arylformamidase and 2pbl.

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

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