1ynu: Difference between revisions

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


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{{STRUCTURE_1ynu|  PDB=1ynu  |  SCENE=  }}  
{{STRUCTURE_1ynu|  PDB=1ynu  |  SCENE=  }}  


'''Crystal structure of apple ACC synthase in complex with L-vinylglycine'''
===Crystal structure of apple ACC synthase in complex with L-vinylglycine===




==Overview==
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L-Vinylglycine (L-VG) is both a substrate for and a mechanism-based inhibitor of 1-aminocyclopropane-1-carboxylate (ACC) synthase. The ratio of the rate constants for catalytic conversion to alpha-ketobutyrate and ammonia to inactivation is 500/1. The crystal structure of the covalent adduct of the inactivated enzyme was determined at 2.25 Angstroms resolution. The active site contains an external aldimine of the adduct of L-VG with the pyridoxal 5'-phosphate cofactor. The side chain gamma-carbon of L-VG is covalently bound to the epsilon-amino group of Lys273. This species corresponds to one of the two alternatives proposed by Feng and Kirsch [Feng, L. and Kirsch, J.F. (2000) L-Vinylglycine is an alternative substrate as well as a mechanism-based inhibitor of 1-aminocyclopropane-1-carboxylate synthase. Biochemistry 39, 2436-2444] and presumably results from Michael addition to a vinylglycine ketimine intermediate.
The line below this paragraph, {{ABSTRACT_PUBMED_15848188}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_15848188}}


==About this Structure==
==About this Structure==
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[[Category: Tschopp, M.]]
[[Category: Tschopp, M.]]
[[Category: Lyase]]
[[Category: Lyase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:33:35 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:21:56 2008''

Revision as of 13:21, 28 July 2008

File:1ynu.png

Template:STRUCTURE 1ynu

Crystal structure of apple ACC synthase in complex with L-vinylglycine

Template:ABSTRACT PUBMED 15848188

About this Structure

1YNU is a Single protein structure of sequence from Malus x domestica. Full crystallographic information is available from OCA.

Reference

Structure of ACC synthase inactivated by the mechanism-based inhibitor L-vinylglycine., Capitani G, Tschopp M, Eliot AC, Kirsch JF, Grutter MG, FEBS Lett. 2005 Apr 25;579(11):2458-62. PMID:15848188

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