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Thioesterase superfamily member 2

Cat. No.: CBCRY16
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
MMDB ID: 42159
Source: E.coli
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 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

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