Download MendeleyCrystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe.
Bulfer, S.L., Hendershot, J.M., Trievel, R.C.(2012) Proteins 80: 661-666
- PubMed: 22105743
- DOI: https://doi.org/10.1002/prot.23231
- Primary Citation of Related Structures:
3TY3, 3TY4 - PubMed 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.
Organizational Affiliation:
Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109.
