1arh

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[[Image:1arh.gif|left|200px]]
[[Image:1arh.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1arh |SIZE=350|CAPTION= <scene name='initialview01'>1arh</scene>, resolution 2.3&Aring;
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The line below this paragraph, containing "STRUCTURE_1arh", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PPD:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYLENE)-AMINO]-SUCCINIC+ACID'>PPD</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1arh| PDB=1arh | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1arh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1arh OCA], [http://www.ebi.ac.uk/pdbsum/1arh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1arh RCSB]</span>
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}}
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'''ASPARTATE AMINOTRANSFERASE, Y225R/R386A MUTANT'''
'''ASPARTATE AMINOTRANSFERASE, Y225R/R386A MUTANT'''
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[[Category: Jansonius, J N.]]
[[Category: Jansonius, J N.]]
[[Category: Malashkevich, V N.]]
[[Category: Malashkevich, V N.]]
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[[Category: transferase (aminotransferase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:37:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:46:09 2008''
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Revision as of 07:37, 2 May 2008

Image:1arh.gif

Template:STRUCTURE 1arh

ASPARTATE AMINOTRANSFERASE, Y225R/R386A MUTANT


Overview

The electron distribution in the coenzyme-substrate adduct of aspartate aminotransferase was changed by replacing active-site Arg386 with alanine and introducing a new arginine residue nearby. [Y225R, R386A]Aspartate aminotransferase decarboxylates L-aspartate to L-alanine (kcat = 0.04 s-1), while its transaminase activity towards dicarboxylic amino acids is decreased by three orders of magnitude (kcat = 0.19 s-1). Molecular-dynamics simulations based on the crystal structure of the mutant enzyme suggest that a new hydrogen bond to the imine N atom of the pyridoxal-5'-phosphate- aspartate adduct and an altered electrostatic potential around its beta-carboxylate group underlie the 650,000-fold increase in the ratio of beta-decarboxylase/transaminase activity.

About this Structure

1ARH is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Changing the reaction specificity of a pyridoxal-5'-phosphate-dependent enzyme., Graber R, Kasper P, Malashkevich VN, Sandmeier E, Berger P, Gehring H, Jansonius JN, Christen P, Eur J Biochem. 1995 Sep 1;232(2):686-90. PMID:7556224 Page seeded by OCA on Fri May 2 10:37:11 2008

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