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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function.

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 compromises protein thermostability and catalytic function. Therefore, a fully occupied binuclear manganese metal cluster is required for optimal catalysis and thermostability.[1]

References

  1. Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function. Scolnick, L.R., Kanyo, Z.F., Cavalli, R.C., Ash, D.E., Christianson, D.W. Biochemistry (1997) [Pubmed]
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