4rla

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{{STRUCTURE_4rla| PDB=4rla | SCENE= }}
{{STRUCTURE_4rla| PDB=4rla | SCENE= }}
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'''ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION'''
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===ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_9265637}}
==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Urea cycle]]
[[Category: Urea cycle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:28:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:49:12 2008''

Revision as of 10:49, 3 July 2008

Image:4rla.png

Template:STRUCTURE 4rla

ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION

Template:ABSTRACT PUBMED 9265637

About this Structure

4RLA is a Single protein structure of sequence from Rattus norvegicus. 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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