1YNU

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

Summary for 1YNU

• Entry DOI: 10.2210/pdb1ynu/pdb
• Related: 1B8G 1M4N 1M7Y
• Descriptor: 1-aminocyclopropane-1-carboxylate synthase, NICKEL (II) ION, POTASSIUM ION, ... (6 entities in total)
• Functional Keywords: lyase
• Biological source: Malus x domestica
• Total number of polymer chains: 1
• Total formula weight: 53927.33

Authors

Capitani, G.,Tschopp, M.,Eliot, A.C.,Kirsch, J.F.,Grutter, M.G. (deposition date: 2005-01-25, release date: 2005-05-03, Last modification date: 2024-10-23)

Primary citation

Capitani, G.,Tschopp, M.,Eliot, A.C.,Kirsch, J.F.,Grutter, M.G.
Structure of ACC synthase inactivated by the mechanism-based inhibitor L-vinylglycine.
Febs Lett., 579:2458-2462, 2005

PubMed Abstract: 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.

PubMed: 15848188
DOI: 10.1016/j.febslet.2005.03.048

Experimental method

X-RAY DIFFRACTION (2.25 Å)