Arylformamidase Function Slide 4: Difference between revisions

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- A thermostable carboxylesterase from an uncultured archaeon - isolated in an environmental sample.
- A thermostable carboxylesterase from an uncultured archaeon - isolated in an environmental sample.
== Evidence from Similar Structures ==
- Catalytic triad identified in paper - Ser154, Asp251, and His281.
- To assess functional similarity, conservation of the catalytic triad was analysed.
[[Image:2c7b_alignment.png|centre|framed|'''Conservation of the catalytic triad between 2cb7 and 2pbl.''']]
- Catalytic triad conserved.
- Note: difference in clustalW alignment from DALI sequence alignment. Unstable region of alignment?
== Similarity in mechanism? ==
[[Image:Arylformadisae_reaction.gif|centre|framed|The reaction catalysed by Arylformamidase.]]
[[Image:Carboxylesterase_reaction.gif|centre|framed|The fundamental reaction catalysed by carboxylesterases.]]


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Latest revision as of 12:29, 8 June 2008

Evidence from Similar Structures

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

- Most similar structure 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 thermostable carboxylesterase from an uncultured archaeon - isolated in an environmental sample.

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