Arylformamidase: Difference between revisions
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== Discussion == | == Discussion == |
Revision as of 05:02, 3 June 2008
Abstract
Contents
Presentations
Sequence & Homology - Sebastian Mynott
Structure - Basma Al Alaiwat
Function - Thomas Parker
Discussion
probable function
The function of 2c7b has been well characterised (references).
additional info on probable function
Carboxylesterases have a common reaction mechanism (see figure ...). This is somewhat similar to the arylformamidase reaction mechanism incorporating hydrolysis of a ... bond.
evolutionary link...
biological implications/applications...
Potential thermostability - applicability in industry.
further research...
Conclusion
Methods
Literature search
A literature search was performed using the putative annotation ‘arylformamidase’. A paper by Pabarcus et al. 2007 was returned which, ironically, described the arylformamidase from Mus Musculus.
Conservation of Catalytic Triad
An alignment of 2pbl and the protein of interest was performed using ClustalX. Default parameters were used. Residues of the catalytic triad were identified from the paper describing it and located in the sequence. Conservation of the residue and the surrounding sequence was observed. Note: in analysing conservation of the 2c7b catalytic triad with 2pbl, the clustalW alignment was found to differ from the alignment provided as part of the DALI results.
Additional Materials
Presentations
Links
Protein Data Bank Entry for 2PBL
FASTA Sequence
>gi|146387357|pdb|2PBL|A Chain A, Crystal Structure Of Putative Thioesterase (Yp_614486.1) From Silicibacter Sp. Tm1040 At 1.79 A Resolution GXELDDAYANGAYIEGAADYPPRWAASAEDFRNSLQDRARLNLSYGEGDRHKFDLFLPEGTPVGLFVFVH GGYWXAFDKSSWSHLAVGALSKGWAVAXPSYELCPEVRISEITQQISQAVTAAAKEIDGPIVLAGHSAGG HLVARXLDPEVLPEAVGARIRNVVPISPLSDLRPLLRTSXNEKFKXDADAAIAESPVEXQNRYDAKVTVW VGGAERPAFLDQAIWLVEAWDADHVIAFEKHHFNVIEPLADPESDLVAVITA