Work

Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe

Year: 2011

Type: article

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.

Source: Proteins Structure Function and Bioinformatics

DOI: 10.1002/prot.23231

Authors: Stacie L. Bulfer, Jenna M. Hendershot, Raymond C. Trievel

Institutions: University of California, San Francisco, University of Michigan

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: green

Funders: Michigan Economic Development Corporation, Michigan Technology Tri-Corridor, National Institute of General Medical Sciences

Awards: G416541740, Cellular Biotechnology Training Program (CBTP), Cellular Biotechnology Training Program (CBTP) - Years 31-35