title: Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe.
abstract: Homoisocitrate dehydrogenase (HICDH) catalyzes the conversion of homoisocitrate to 2-oxoadipate, the third enzymatic step in the α-aminoadipate pathway by which lysine is synthesized in fungi and certain archaebacteria. This enzyme represents a potential target for anti-fungal drug design. Here, we describe the first crystal structures of a fungal HICDH, including structures of an apoenzyme and a binary complex with a glycine tri-peptide. The structures illustrate the homology of HICDH with other β-hydroxyacid oxidative decarboxylases and reveal key differences with the active site of Thermus thermophilus HICDH that provide insights into the differences in substrate specificity of these enzymes.
authors: Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109.
authors: Stacie L
authors: SL
authors: Bulfer
authors: Jenna M
authors: JM
authors: Hendershot
authors: Raymond C
authors: RC
authors: Trievel
mesh_terms: D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D011487:Protein Conformation; D029702:Schizosaccharomyces pombe Proteins / Q000737:chemistry* / Q000378:metabolism; D040681:Structural Homology, Protein
chemical_list: D029702:Schizosaccharomyces pombe Proteins; D000429:Alcohol Oxidoreductases; C021368:homoisocitrate dehydrogenase