Arylformamidase Function Slide 3

Evidence from Similar Sequences

- 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.

Evidence from Similar Structures

- Screening of DALI result (see Basma) for functional information.

- Most similar result well-characterised:

Byun JS, Rhee JK, Kim ND, Yoon J, Kim DU, Koh E, Oh JW, Cho HS.
Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties.
BMC Struct Biol. 2007 Jul 12;7:47.

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%).

Conservation of the catalytic triad between 2cb7 and 2pbl.

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