Arylformamidase

Additional Materials

Presentations

Sequence & Homology - Sebastian Mynott

Structure - Basma Al Alaiwat

Function - Thomas Parker

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

References

Pabarcus MK, Casida JE.
Cloning, expression, and catalytic triad of recombinant arylformamidase.
Protein Expr Purif. Nov;44(1):39-44.

De Simone G, Menchise V, Manco G, Mandrich L, Sorrentino N, Lang D, Rossi M, Pedone C.
The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus.
J Mol Biol. 2001 Nov 30;314(3):507-18.

Byun JS, Rhee JK, Kim ND, Yoon J, Kim DU, Koh E, Oh JW, Cho HS.
Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties.
BMC Struct Biol. 2007 Jul 12;7:47.

2-Effect of arylformamidase (kynurenine formamidase) gene inactivation in mice on enzymatic activity, kynurenine pathway metabolites and phenotype

 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