Arylformamidase: Difference between revisions

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== Abstract ==
== 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.
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 its specific function is still not known, 2pbl shares a high structural similarity with thermostable HSL esterases. Further characterisation is needed.


== Contents ==
== Contents ==

Revision as of 14:14, 8 June 2008

Figure 1. Arylformamidase

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 its specific function is still not known, 2pbl shares a high structural similarity with thermostable HSL esterases. Further characterisation is needed.

Contents

Introduction

Results

Discussion

Methods

Additional Materials

References

Presentations

Sequence & Homology - Sebastian Mynott

Structure - Basma Al Alaiwat

Function - Thomas Parker