1arg: Difference between revisions

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

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

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~~'''~~ASPARTATE AMINOTRANSFERASE, PHOSPHO-5'-PYRIDOXYL ASPARTATE COMPLEX~~'''~~

===ASPARTATE AMINOTRANSFERASE, PHOSPHO-5'-PYRIDOXYL ASPARTATE COMPLEX===

~~==Overview==~~

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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.

The line below this paragraph, {{ABSTRACT_PUBMED_7556224}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 7556224 is the PubMed ID number.

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==About this Structure==

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[[Category: Jansonius, J N.]]

[[Category: Malashkevich, V N.]]

''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 Mon Jun 30 17:28:00 2008''

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-[[Image:1arg.gif|left|200px]]
+{{Seed}}
+[[Image:1arg.png|left|200px]]
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 {{STRUCTURE_1arg|  PDB=1arg  |  SCENE=  }}
-'''ASPARTATE AMINOTRANSFERASE, PHOSPHO-5'-PYRIDOXYL ASPARTATE COMPLEX'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_7556224}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7556224 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7556224}}
 ==About this Structure==
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 [[Category: Jansonius, J N.]]
 [[Category: Malashkevich, V N.]]
-''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 Mon Jun 30 17:28:00 2008''