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