1ynu
From Proteopedia
(New page: 200px<br /><applet load="1ynu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ynu, resolution 2.25Å" /> '''Crystal structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1ynu.gif|left|200px]]<br /><applet load="1ynu" size=" | + | [[Image:1ynu.gif|left|200px]]<br /><applet load="1ynu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ynu, resolution 2.25Å" /> | caption="1ynu, resolution 2.25Å" /> | ||
'''Crystal structure of apple ACC synthase in complex with L-vinylglycine'''<br /> | '''Crystal structure of apple ACC synthase in complex with L-vinylglycine'''<br /> | ||
==Overview== | ==Overview== | ||
| - | L-Vinylglycine (L-VG) is both a substrate for and a mechanism-based | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1YNU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Malus_x_domestica Malus x domestica] with NI, K, PY4 and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/1-aminocyclopropane-1-carboxylate_synthase 1-aminocyclopropane-1-carboxylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.14 4.4.1.14] Full crystallographic information is available from [http:// | + | 1YNU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Malus_x_domestica Malus x domestica] with <scene name='pdbligand=NI:'>NI</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=PY4:'>PY4</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/1-aminocyclopropane-1-carboxylate_synthase 1-aminocyclopropane-1-carboxylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.14 4.4.1.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YNU OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Capitani, G.]] | [[Category: Capitani, G.]] | ||
| - | [[Category: Eliot, A | + | [[Category: Eliot, A C.]] |
| - | [[Category: Grutter, M | + | [[Category: Grutter, M G.]] |
| - | [[Category: Kirsch, J | + | [[Category: Kirsch, J F.]] |
[[Category: Tschopp, M.]] | [[Category: Tschopp, M.]] | ||
[[Category: K]] | [[Category: K]] | ||
| Line 25: | Line 25: | ||
[[Category: lyase]] | [[Category: lyase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:22 2008'' |
Revision as of 14:07, 21 February 2008
|
Crystal structure of apple ACC synthase in complex with L-vinylglycine
Overview
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.
About this Structure
1YNU is a Single protein structure of sequence from Malus x domestica with , , and as ligands. Active as 1-aminocyclopropane-1-carboxylate synthase, with EC number 4.4.1.14 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
Page seeded by OCA on Thu Feb 21 16:07:22 2008
