1B8G

1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE

Summary for 1B8G

• Entry DOI: 10.2210/pdb1b8g/pdb
• Descriptor: PROTEIN (1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE), PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• Functional Keywords: ethylene biosynthesis, lyase
• Biological source: Malus x domestica
• Total number of polymer chains: 2
• Total formula weight: 97021.96

Authors

Capitani, G.,Hohenester, E.,Feng, L.,Storici, P.,Kirsch, J.F.,Jansonius, J.N. (deposition date: 1999-01-31, release date: 2000-01-26, Last modification date: 2023-12-27)

Primary citation

Capitani, G.,Hohenester, E.,Feng, L.,Storici, P.,Kirsch, J.F.,Jansonius, J.N.
Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene.
J.Mol.Biol., 294:745-756, 1999

PubMed Abstract: 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.

PubMed: 10610793
DOI: 10.1006/jmbi.1999.3255

Experimental method

X-RAY DIFFRACTION (2.37 Å)