1arh: Difference between revisions

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[[Image:1arh.gif|left|200px]]
{{Seed}}
[[Image:1arh.png|left|200px]]


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{{STRUCTURE_1arh|  PDB=1arh  |  SCENE=  }}  
{{STRUCTURE_1arh|  PDB=1arh  |  SCENE=  }}  


'''ASPARTATE AMINOTRANSFERASE, Y225R/R386A MUTANT'''
===ASPARTATE AMINOTRANSFERASE, Y225R/R386A MUTANT===




==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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{{ABSTRACT_PUBMED_7556224}}


==About this Structure==
==About this Structure==
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[[Category: Jansonius, J N.]]
[[Category: Jansonius, J N.]]
[[Category: Malashkevich, V N.]]
[[Category: Malashkevich, V N.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:37:11 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:28:08 2008''

Revision as of 14:28, 30 June 2008

File:1arh.png

Template:STRUCTURE 1arh

ASPARTATE AMINOTRANSFERASE, Y225R/R386A MUTANT

Template:ABSTRACT PUBMED 7556224

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

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