Arylformamidase Function Slide 2: Difference between revisions
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[[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 --> | 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.
