1tbj: Difference between revisions

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[[Image:1tbj.gif|left|200px]]
{{Seed}}
[[Image:1tbj.png|left|200px]]


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{{STRUCTURE_1tbj|  PDB=1tbj  |  SCENE=  }}  
{{STRUCTURE_1tbj|  PDB=1tbj  |  SCENE=  }}  


'''H141A mutant of rat liver arginase I'''
===H141A mutant of rat liver arginase I===




==Overview==
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Rat liver arginase (arginase I) is potently inactivated by diethyl pyrocarbonate, with a second-order rate constant of 113M(-1)s(-1) for the inactivation process at pH 7.0, 25 degrees C. Partial protection from inactivation is provided by the product of the reaction, l-ornithine, while nearly complete protection is afforded by the inhibitor pair, l-ornithine and borate. The role of H141 has been probed by mutagenesis, chemical modulation, and X-ray diffraction. The hyper-reactivity of H141 towards diethyl pyrocarbonate can be explained by its proximity to E277. A proton shuttling role for H141 is supported by its conformational mobility observed among the known arginase structures. H141 is proposed to serve as an acid/base catalyst, deprotonating the metal-bridging water molecule to generate the metal-bridging hydroxide nucleophile, and by protonating the amino group of the product to facilitate its departure.
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{{ABSTRACT_PUBMED_16266687}}


==About this Structure==
==About this Structure==
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[[Category: Binuclear manganese cluster]]
[[Category: Binuclear manganese cluster]]
[[Category: H141a mutant]]
[[Category: H141a mutant]]
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