1arg: Difference between revisions
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[[Image:1arg.gif|left|200px]] | [[Image:1arg.gif|left|200px]] | ||
'''ASPARTATE AMINOTRANSFERASE, PHOSPHO-5'-PYRIDOXYL ASPARTATE COMPLEX''' | {{Structure | ||
|PDB= 1arg |SIZE=350|CAPTION= <scene name='initialview01'>1arg</scene>, resolution 2.2Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PPD:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYLENE)-AMINO]-SUCCINIC ACID'>PPD</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''ASPARTATE AMINOTRANSFERASE, PHOSPHO-5'-PYRIDOXYL ASPARTATE COMPLEX''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ARG is a [ | 1ARG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ARG OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7556224 7556224] | ||
[[Category: Aspartate transaminase]] | [[Category: Aspartate transaminase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: transferase (aminotransferase)]] | [[Category: transferase (aminotransferase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:01:23 2008'' | ||
Revision as of 08:01, 20 March 2008
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| 1arg, resolution 2.2Å | |||||||||||||
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| Ligands: | PPD | ||||||||||||
| Activity: | Aspartate transaminase, with EC number 2.6.1.1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
ASPARTATE AMINOTRANSFERASE, PHOSPHO-5'-PYRIDOXYL ASPARTATE COMPLEX
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
1ARG 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
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