3rla
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="3rla" size="450" color="white" frame="true" align="right" spinBox="true" caption="3rla, resolution 2.54Å" /> '''ALTERING THE BINUCL...)
Next diff →
Revision as of 14:39, 29 October 2007
|
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
3RLA is a [Single protein] structure of sequence from [Rattus norvegicus] with MN as [ligand]. Active as [[1]], with EC number [3.5.3.1]. 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
Page seeded by OCA on Mon Oct 29 16:44:02 2007
