4rla
From Proteopedia
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ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION
Overview
Arginase is a thermostable (Tm = 75 degrees C) binuclear manganese, metalloenzyme which hydrolyzes l-arginine to form l-ornithine and urea., The three-dimensional structures of native metal-depleted arginase, metal-loaded H101N arginase, and metal-depleted H101N arginase have been, determined by X-ray crystallographic methods to probe the roles of the, manganese ion in site A (Mn2+A) and its ligand H101 in catalysis and, thermostability. We correlate these structures with thermal stability and, catalytic activity measurements reported here and elsewhere [Cavalli, R., C., Burke, C. J., Kawamoto, S., Soprano, D. R., and Ash, D. E. (1994), Biochemistry 33, 10652-10657]. We conclude that the substitution of a, wild-type histidine ligand to Mn2+A compromises metal binding, which in, turn ... [(full description)]
About this Structure
4RLA is a [Single protein] structure of sequence from [Rattus norvegicus] with MN as [ligand]. Active as [Arginase], with EC number [3.5.3.1]. Structure known Active Sites: MNA, MNB and MNC. Full crystallographic information is available from [OCA].
Reference
Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function., Scolnick LR, Kanyo ZF, Cavalli RC, Ash DE, Christianson DW, Biochemistry. 1997 Aug 26;36(34):10558-65. PMID:9265637
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