1zpe

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[[Image:1zpe.gif|left|200px]]
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{{Seed}}
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[[Image:1zpe.png|left|200px]]
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{{STRUCTURE_1zpe| PDB=1zpe | SCENE= }}
{{STRUCTURE_1zpe| PDB=1zpe | SCENE= }}
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'''Arginase I covalently modified with butylamine at Q19C'''
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===Arginase I covalently modified with butylamine at Q19C===
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_16266687}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16266687 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16266687}}
==About this Structure==
==About this Structure==
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[[Category: Viola, R E.]]
[[Category: Viola, R E.]]
[[Category: Chemically modified enzyme]]
[[Category: Chemically modified enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:54:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:18:09 2008''

Revision as of 04:18, 28 July 2008

Image:1zpe.png

Template:STRUCTURE 1zpe

Arginase I covalently modified with butylamine at Q19C

Template:ABSTRACT PUBMED 16266687

About this Structure

1ZPE is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Probing the role of the hyper-reactive histidine residue of arginase., Colleluori DM, Reczkowski RS, Emig FA, Cama E, Cox JD, Scolnick LR, Compher K, Jude K, Han S, Viola RE, Christianson DW, Ash DE, Arch Biochem Biophys. 2005 Dec 1;444(1):15-26. Epub 2005 Oct 13. PMID:16266687

Page seeded by OCA on Mon Jul 28 07:18:09 2008

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