1arg: Difference between revisions

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[[Image:1arg.gif|left|200px]]
[[Image:1arg.gif|left|200px]]


{{Structure
<!--
|PDB= 1arg |SIZE=350|CAPTION= <scene name='initialview01'>1arg</scene>, resolution 2.2&Aring;
The line below this paragraph, containing "STRUCTURE_1arg", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=PPD:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYLENE)-AMINO]-SUCCINIC+ACID'>PPD</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|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>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_1arg| PDB=1arg  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1arg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1arg OCA], [http://www.ebi.ac.uk/pdbsum/1arg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1arg RCSB]</span>
}}


'''ASPARTATE AMINOTRANSFERASE, PHOSPHO-5'-PYRIDOXYL ASPARTATE COMPLEX'''
'''ASPARTATE AMINOTRANSFERASE, PHOSPHO-5'-PYRIDOXYL ASPARTATE COMPLEX'''
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[[Category: Jansonius, J N.]]
[[Category: Jansonius, J N.]]
[[Category: Malashkevich, V N.]]
[[Category: Malashkevich, V N.]]
[[Category: transferase (aminotransferase)]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:37:10 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:46:07 2008''

Revision as of 10:37, 2 May 2008

File:1arg.gif

Template:STRUCTURE 1arg

ASPARTATE AMINOTRANSFERASE, PHOSPHO-5'-PYRIDOXYL ASPARTATE COMPLEX


OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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 10:37:10 2008

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