Arylformamidase: Difference between revisions
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== Abstract == | == Abstract == | ||
2pbl, initially annotated as an arylformamidase, was isolated from '' | 2pbl, initially annotated as an arylformamidase, was isolated from ''Silicibacter 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 groups that are 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. Principal residues of a probable catalytic triad were identified as Ser137, His242 and Glu215. Although its specific function is still not known, 2pbl shares a high structural similarity with thermostable HSL esterases. Further experimental characterisation of 2pbl is needed. | ||
== Contents == | == Contents == | ||
Revision as of 22:46, 9 June 2008
by Basma Al Alaiwat, Sebastian Mynott and Thomas Parker
Abstract
2pbl, initially annotated as an arylformamidase, was isolated from Silicibacter 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 groups that are 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. Principal residues of a probable catalytic triad were identified as Ser137, His242 and Glu215. Although its specific function is still not known, 2pbl shares a high structural similarity with thermostable HSL esterases. Further experimental characterisation of 2pbl is needed.
Contents
Presentations
Sequence & Homology - Sebastian Mynott
Structure - Basma Al Alaiwat
Function - Thomas Parker
