Thioesterase superfamily member 2

• Cat.No.: CBCRY16

Specification

• Source: E.coli
• Tag: Non
• Background: The crystallographic structure of recombinant hTHEM2, determined by the single-wavelength anomalous dispersion method at 2.3A resolution, demonstrates that hTHEM2 indeed contains a hotdog-fold and forms a back-to-back tetramer as other hotdog proteins. Based on structural and sequence conservation, the thioesterase active site in hTHEM2 is predicted. The structure and substrate specificity are most similar to those of the bacterial phenylacetyl-CoA hydrolase. Asp65, located on the central alpha-helix of subunit B, was shown by site-directed mutagenesis to be essential to catalysis.
• Protein Classification: Hydrolase
• Structure Weight: 132969.96 Da
• Polymer: 1
• Molecule: Thioesterase superfamily member 2
• Chain Length: 176 amino acids
• PDB ID: 2F0X
• MMDB ID: 42159
• Method: X-Ray Diffraction
• Resolution: 2.3Å
• Ligand Chemical Component: sulfate ion
• Reference: Cheng, Z., Song, F., Shan, X., Wei, Z., Wang, Y., Dunaway-Mariano, D., Gong, W.(2006) Crystal structure of human thioesterase superfamily member 2Biochem.Biophys.Res.Commun.349: 172-177

Gene Information

• Gene Name: THEM2
• Synonyms: HT012; MGC4961; PNAS-27; 15 Kd protein; OTTHUMP00000016090; OTTHUMP00000039398; hypothalamus protein HT012
• UniProt ID: Q9NPJ3
• Gene ID: 55856
• Chromosome Location: 6p22.2
• Function: hydrolase activity