Arylformamidase: Difference between revisions
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[[Image:Pretty protein.PNG|centre|framed|'''Figure 1.''' ''Arylformamidase'']] | [[Image:Pretty protein.PNG|centre|framed|'''Figure 1.''' ''Arylformamidase'']] | ||
Revision as of 12:05, 7 June 2008
by Basma Al Alaiwat, Sebastian Mynott and Thomas Parker
Abstract
2pbl, initially annotated as an arylformamidase, was isolated from Silibacter sp. TM1040 and its structure determined by the JCSG. Based on structural, functional and evolutionary analysis, we have further characterised 2pbl. It was found to contain a conserved functional group that is present in a broad range of hydrolases in many taxonomic groups. Specifically, it was found to share similar structural and sequence characteristics of the HSL family of esterases. Probable residues of a catalytic triad were identified as Ser137, His242 and Glu215. Although the specific function is still not known, 2pbl shares a high structural simlarity with thermostable HSL esterases and thus, may present novel industrial applications.
Contents
Presentations
Sequence & Homology - Sebastian Mynott
Structure - Basma Al Alaiwat
Function - Thomas Parker
