1b8g: Difference between revisions

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[[Image:1b8g.~~gif~~|left|200px]]

[[Image:1b8g.png|left|200px]]

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~~'''~~1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE~~'''~~

===1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE===

~~==Overview==~~

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The ~~2.4 A crystal structure of the vitamin B6-dependent enzyme 1-aminocyclopropane-1-carboxylate (ACC) synthase is described. This enzyme catalyses the committed step in the biosynthesis of ethylene~~, a plant hormone that is responsible for the initiation of fruit ripening and for regulating many other developmental processes. ACC synthase has 15 % sequence identity with the well-studied aspartate aminotransferase, ~~and a completely different catalytic activity yet~~ the ~~overall folds and~~ the active sites are very similar. The new structure together with available biochemical data enables a comparative mechanistic analysis that largely explains the catalytic roles of the conserved and non-conserved active site residues. An external aldimine reaction intermediate (~~external aldimine with ACC, i~~.e. ~~with the product~~) ~~has been modeled. The new structure provides a basis for~~ the ~~rational design of inhibitors with broad agricultural applications~~.

The line below this paragraph, {{ABSTRACT_PUBMED_10610793}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10610793 is the PubMed ID number.

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==About this Structure==

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[[Category: Storici, P.]]

[[Category: Ethylene biosynthesis]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 11~~:12:15 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:33:27 2008''

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-[[Image:1b8g.gif|left|200px]]
+{{Seed}}
+[[Image:1b8g.png|left|200px]]
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 {{STRUCTURE_1b8g|  PDB=1b8g  |  SCENE=  }}
-'''1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE'''
+===1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE===
-==Overview==
+<!--
-The 2.4 A crystal structure of the vitamin B6-dependent enzyme 1-aminocyclopropane-1-carboxylate (ACC) synthase is described. This enzyme catalyses the committed step in the biosynthesis of ethylene, a plant hormone that is responsible for the initiation of fruit ripening and for regulating many other developmental processes. ACC synthase has 15 % sequence identity with the well-studied aspartate aminotransferase, and a completely different catalytic activity yet the overall folds and the active sites are very similar. The new structure together with available biochemical data enables a comparative mechanistic analysis that largely explains the catalytic roles of the conserved and non-conserved active site residues. An external aldimine reaction intermediate (external aldimine with ACC, i.e. with the product) has been modeled. The new structure provides a basis for the rational design of inhibitors with broad agricultural applications.
+The line below this paragraph, {{ABSTRACT_PUBMED_10610793}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10610793 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10610793}}
 ==About this Structure==
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 [[Category: Storici, P.]]
 [[Category: Ethylene biosynthesis]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:12:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:33:27 2008''