Arylformamidase: Difference between revisions

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== Menu ==
[[Image:Pretty protein.PNG|centre|framed|'''Figure 1.''' ''2PBL'']]


''by Basma Al Alaiwat, Sebastian Mynott and Thomas Parker''


== Abstract ==


[[Introduction]]
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 region present in A/B-hydrolases of many taxonomic groups. Specifically, it was found to share similar structural and sequence characteristics of the prokaryotic HSL family of esterases. Residues of a probable catalytic triad were identified as Ser137, His242 and Glu215. Further experimental characterisation of 2PBL is required to better understand its function.


== Contents ==


[[Methods]]
[[Arylformamidase Introduction|Introduction]]  


[[Arylformamidase Results|Results]]


[[Results]]
[[Arylformamidase Discussion|Discussion]]


[[Arylformamidase Methods|Methods]]


[[Arylformamidase Sequence & Homology | Sequence & Homology]] - ''Sebastian Mynott''
[[Arylformamidase Additional Materials|Additional Materials]]


[[Arylformamidase Structure | Structure]] - ''Basma Al Alaiwat''
[[Arylformamidase References|References]]


[[Arylformamidase Function | Function]] - ''Thomas Parker''
== Presentations ==


[[Arylformamidase Sequence & Homology | Sequence & Homology]] - ''Sebastian Mynott''


[[Discussion]]
[[Arylformamidase Structure | Structure]] - ''Basma Al Alaiwat''
 
 
[[Conclusion]]
 
== Putative Synonyms ==
 
Kynurenine formamidase
 
== 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
 
== Literature ==
 
'''[http://www.ncbi.nlm.nih.gov/pubmed/15935693?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_RVDocSum Cloning, expression, and catalytic triad of recombinant arylformamidase.]'''
''Pabarcus MK, Casida JE.''
Protein Expr Purif. Nov;44(1):39-44.


2-''Effect of arylformamidase (kynurenine formamidase) gene inactivation in mice on enzymatic activity, kynurenine pathway metabolites and phenotype''
[[Arylformamidase Function Slide 1 | Function]] - ''Thomas Parker''
  http://www.ncbi.nlm.nih.gov/pubmed/12007602?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=2&log$=relatedarticles&dbfrom=pubmed

Latest revision as of 03:29, 10 June 2008

Figure 1. 2PBL

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 region present in A/B-hydrolases of many taxonomic groups. Specifically, it was found to share similar structural and sequence characteristics of the prokaryotic HSL family of esterases. Residues of a probable catalytic triad were identified as Ser137, His242 and Glu215. Further experimental characterisation of 2PBL is required to better understand its function.

Contents

Introduction

Results

Discussion

Methods

Additional Materials

References

Presentations

Sequence & Homology - Sebastian Mynott

Structure - Basma Al Alaiwat

Function - Thomas Parker

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