Determinants of Enzymatic Specificity in the Cys-Met-Metabolism PLP-Dependent Enzyme Family: Crystal Structure of Cystathionine γ-Lyase from Yeast and Intrafamiliar Structure Comparison

@inproceedings{Messerschmidt2003DeterminantsOE,
  title={Determinants of Enzymatic Specificity in the Cys-Met-Metabolism PLP-Dependent Enzyme Family: Crystal Structure of Cystathionine $\gamma$-Lyase from Yeast and Intrafamiliar Structure Comparison},
  author={Albrecht Messerschmidt and Michael Worbs and Clemens Steegborn and Markus C. Wahl and Robert Huber and Bernd Laber and Tim Clausen},
  booktitle={Biological chemistry},
  year={2003}
}
Abstract The crystal structure of cystathionine γ-lyase (CGL) from yeast has been solved by molecular replacement at a resolution of 2.6 å. The molecule consists of 393 amino acid residues and one PLP moiety and is arranged in the crystal as a tetramer with D2 symmetry as in other related enzymes of the CysMetmetabolism PLP-dependent family like cystathionine β-lyase (CBL). A structure comparison with other family members revealed surprising insights into the tuning of enzymatic specificity… 

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