Article
Mobile loop mutations in an archaeal inositol monophosphatase: modulating three-metal ion assisted catalysis and lithium inhibition.
Protein science : a publication of the Protein Society - 1 Feb 2010
Li Zheng, Stieglitz Kimberly A, Shrout Anthony L, Wei Yang, Weis Robert M, Stec Boguslaw, Roberts Mary F
Abstract excerpt
The inositol monophosphatase (IMPase) enzyme from the hyperthermophilic archaeon Methanocaldococcus jannaschii requires Mg(2+) for activity and binds three to four ions tightly in the absence of ligands: K(D) = 0.8 muM for one ion with a K(D) of 38 muM for the other Mg(2+) ions. However, the enzyme requires 5-10 mM Mg(2+) for optimum catalysis, suggesting substrate alters the metal ion affinity. In crystal...
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