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| {{STRUCTURE_1ta1| PDB=1ta1 | SCENE= }} | | {{STRUCTURE_1ta1| PDB=1ta1 | SCENE= }} |
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| '''H141C mutant of rat liver arginase I'''
| | ===H141C mutant of rat liver arginase I=== |
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| ==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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16266687}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16266687 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16266687}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Binuclear manganese cluster]] | | [[Category: Binuclear manganese cluster]] |
| [[Category: H141c mutation]] | | [[Category: H141c mutation]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:43:37 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:07:49 2008'' |