Structural highlights
Publication Abstract from PubMed
Homoisocitrate dehydrogenase (HICDH) catalyzes the conversion of homoisocitrate to 2-oxoadipate, the third enzymatic step in the alpha-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 beta-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.
Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe.,Bulfer SL, Hendershot JM, Trievel RC Proteins. 2012 Feb;80(2):661-6. doi: 10.1002/prot.23231. Epub 2011 Nov 22. PMID:22105743[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bulfer SL, Hendershot JM, Trievel RC. Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe. Proteins. 2011 Oct 24. doi: 10.1002/prot.23231. PMID:22105743 doi:10.1002/prot.23231
