1M7Y

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

Summary for 1M7Y

• Entry DOI: 10.2210/pdb1m7y/pdb
• Related: 1b8g 1m4n
• Descriptor: 1-aminocyclopropane-1-carboxylate synthase, (2E,3E)-4-(2-aminoethoxy)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid, (4R)-2-METHYLPENTANE-2,4-DIOL, ... (4 entities in total)
• Functional Keywords: fruit ripening, ethylene biosynthesis, pyridoxal phosphate, lyase
• Biological source: Malus x domestica
• Total number of polymer chains: 1
• Total formula weight: 49599.27

Authors

Capitani, G.,McCarthy, D.,Gut, H.,Gruetter, M.G.,Kirsch, J.F. (deposition date: 2002-07-23, release date: 2002-12-23, Last modification date: 2023-10-25)

Primary citation

Capitani, G.,McCarthy, D.L.,Gut, H.,Gruetter, M.G.,Kirsch, J.F.
Apple 1-Aminocyclopropane-1-carboxylate Synthase in Complex with the Inhibitor L-Aminoethoxyvinylglycine
J.Biol.Chem., 277:49735-49742, 2002

PubMed Abstract: The 1.6-A crystal structure of the covalent ketimine complex of apple 1-aminocyclopropane-1-carboxylate (ACC) synthase with the potent inhibitor l-aminoethoxyvinylglycine (AVG) is described. ACC synthase catalyzes 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. AVG is widely used in plant physiology studies to inhibit the activity of ACC synthase. The structural assignment is supported by the fact that the complex absorbs maximally at 341 nm. These results are not in accord with the recently reported crystal structure of the tomato ACC synthase AVG complex, which claims that the inhibitor only associates noncovalently. The rate constant for the association of AVG with apple ACC synthase was determined by stopped-flow spectrophotometry (2.1 x 10(5) m(-1) s(-1)) and by the rate of loss of enzyme activity (1.1 x 10(5) m(-1) s(-1)). The dissociation rate constant determined by activity recovery is 2.4 x 10(-6) s(-1). Thus, the calculated K(d) value is 10-20 pm.

PubMed: 12228256
DOI: 10.1074/jbc.M208427200

Experimental method

X-RAY DIFFRACTION (1.6 Å)