1zpg: Difference between revisions

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New page: left|200px<br /><applet load="1zpg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zpg, resolution 1.90Å" /> '''Arginase I covalentl...
 
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[[Image:1zpg.gif|left|200px]]<br /><applet load="1zpg" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1zpg.gif|left|200px]]<br /><applet load="1zpg" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1zpg, resolution 1.90&Aring;" />
caption="1zpg, resolution 1.90&Aring;" />
'''Arginase I covalently modified with propylamine at Q19C'''<br />
'''Arginase I covalently modified with propylamine at Q19C'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1ZPG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZPG OCA].  
1ZPG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZPG OCA].  


==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ash, D.E.]]
[[Category: Ash, D E.]]
[[Category: Cama, E.]]
[[Category: Cama, E.]]
[[Category: Christianson, D.W.]]
[[Category: Christianson, D W.]]
[[Category: Colleluori, D.M.]]
[[Category: Colleluori, D M.]]
[[Category: Compher, K.]]
[[Category: Compher, K.]]
[[Category: Cox, J.D.]]
[[Category: Cox, J D.]]
[[Category: Emig, F.A.]]
[[Category: Emig, F A.]]
[[Category: Han, S.]]
[[Category: Han, S.]]
[[Category: Jude, K.]]
[[Category: Jude, K.]]
[[Category: Reczkowski, R.S.]]
[[Category: Reczkowski, R S.]]
[[Category: Scolnick, L.R.]]
[[Category: Scolnick, L R.]]
[[Category: Viola, R.E.]]
[[Category: Viola, R E.]]
[[Category: MN]]
[[Category: MN]]
[[Category: chemically modified enzyme]]
[[Category: chemically modified enzyme]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:35:23 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:17:49 2008''