Isopropylmalate isomerase
FunctionIsopropylmalate isomerase (IPMI) catalyzes a stereo-specific isomerization of 3-isopropylmalate by dehydration followed by rehydration at a different position to 2-isopropylmalate. IPMI contains an Fe4S4 center. IPMI is a homodimer composed of a large subunit (LeuC) and a small subunit (LeuD)[1]. DiseaseRelevanceStructural highlights |
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3D structures of Isopropylmalate isomerase3D structures of Isopropylmalate isomerase
Updated on 04-April-2016
1v7l – PhIPMI small subunit – Pyrococcus horikoshii
2hcu – SmIPMI small subunit – Streptococcus mutans
3q3w – CjIPMI small subunit – Campylobacter jejuni
3vba – MjIPMI small subunit – Methanocaldococcus janaschii
4kp1, 4nqy – MjIPMI large subunit
3h5e, 5h5h, 5h5j – MtIPMI small subunit – Mycobacterium tuberculosis
ReferencesReferences
- ↑ Yasutake Y, Yao M, Sakai N, Kirita T, Tanaka I. Crystal structure of the Pyrococcus horikoshii isopropylmalate isomerase small subunit provides insight into the dual substrate specificity of the enzyme. J Mol Biol. 2004 Nov 19;344(2):325-33. PMID:15522288 doi:10.1016/j.jmb.2004.09.035