Arylformamidase Additional Materials

Links

Protein Data Bank Entry for 2PBL

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

Return to the main page...

File:Carboxylesterase (archaeon).txt PDB File:Carboxylase.txt PDB

Human arylformamidase has the following catalytic activity.

N-formyl-L-kynurenine + H2O →  Formate + L-kynurenine 

Required for elimination of toxic metabolites

It belongs to the AB hydrolase super family.

Even though the structure of the human protein hasn’t been determined, looking at the sequence alignment the catalytic triad residues are conserved. The residues have resisted mutation indicating that they are important for activity.

Our protein is similar to carboxylesterase which also belongs to AB suberfamily.

Figure 5: Metagenomic Archea Carboxylesterase (Chain A ONLY).Note: Chain B not shown. The structure of carboxylesterase shows absence of ligands. From PDB ProteinWorkshop 1.5

Figure 6: Archaeoglobus fulgidus Carboxylesterase exhibiting chain A only. The ligand is present in this figure. From PDB ProteinWorkshop 1.5

File:DALI RESULT.txt

Each of the residues are linked to a turn region. The catalytic triad in Archaeoglobus fulgidus Carboxylesterase is very close to the ligand (see figure 12).

Figure 12: The conserved catalytic triad in Archaeoglobus fulgidus Carboxylesterase (PDB ID 1JJI)

Sequence alignment:

Sections of alignment showing the conserved residues across bacterial and eukaryotic species.