1ivr: Difference between revisions

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

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

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~~'''~~STRUCTURE OF ASPARTATE AMINOTRANSFERASE~~'''~~

===STRUCTURE OF ASPARTATE AMINOTRANSFERASE===

~~==Overview==~~

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The ~~crystal structure of mitochondrial aspartate aminotransferase~~ (~~mAAT) of chicken complexed with erythro-beta-hydroxyaspartate has been determined~~ at 2.~~4 A resolution~~. ~~Pregrown crystals of mAAT complexed with the inhibitor maleate (closed enzyme conformation~~, orthorhombic space group C222(1)) were soaked in solutions of erythro-beta-hydroxyaspartate. The ligand exchange was monitored by microspectrophotometry. The active site turned out to be predominantly occupied by the carbinolamine intermediate. The carbinolamine is ~~a true intermediate of the catalytic cycle forming the last covalently bound enzyme:substrate complex before release of~~ the ~~keto acid product~~. Occupancies of approximately 80% for the carbinolamine and of approximately 20% for the quinonoid intermediate were obtained. Two hydrogen bonds were identified that are potentially relevant for the accumulation of the carbinolamine intermediate: one to the hydroxyl group of Tyr 70* and the other to the epsilon-~~NH2 group of Lys 258.~~

The line below this paragraph, {{ABSTRACT_PUBMED_8952476}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8952476 is the PubMed ID number.

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==About this Structure==

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[[Category: Carbinolamine]]

[[Category: Erythro-beta-hydroxyaspartate]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 20~~:28:41 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:05:05 2008''

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-[[Image:1ivr.gif|left|200px]]
+{{Seed}}
+[[Image:1ivr.png|left|200px]]
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 {{STRUCTURE_1ivr|  PDB=1ivr  |  SCENE=  }}
-'''STRUCTURE OF ASPARTATE AMINOTRANSFERASE'''
+===STRUCTURE OF ASPARTATE AMINOTRANSFERASE===
-==Overview==
+<!--
-The crystal structure of mitochondrial aspartate aminotransferase (mAAT) of chicken complexed with erythro-beta-hydroxyaspartate has been determined at 2.4 A resolution. Pregrown crystals of mAAT complexed with the inhibitor maleate (closed enzyme conformation, orthorhombic space group C222(1)) were soaked in solutions of erythro-beta-hydroxyaspartate. The ligand exchange was monitored by microspectrophotometry. The active site turned out to be predominantly occupied by the carbinolamine intermediate. The carbinolamine is a true intermediate of the catalytic cycle forming the last covalently bound enzyme:substrate complex before release of the keto acid product. Occupancies of approximately 80% for the carbinolamine and of approximately 20% for the quinonoid intermediate were obtained. Two hydrogen bonds were identified that are potentially relevant for the accumulation of the carbinolamine intermediate: one to the hydroxyl group of Tyr 70* and the other to the epsilon-NH2 group of Lys 258.
+The line below this paragraph, {{ABSTRACT_PUBMED_8952476}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8952476 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8952476}}
 ==About this Structure==
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 [[Category: Carbinolamine]]
 [[Category: Erythro-beta-hydroxyaspartate]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:28:41 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 14:05:05 2008''