Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-48202
Schärer, M A; Eliot, A C; Grütter, M G; Capitani, G (2011). Structural basis for reduced activity of 1-aminocyclopropane-1-carboxylate synthase affected by a mutation linked to andromonoecy. FEBS Letters, 585(1):111-114.
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1-aminocyclopropane-1-carboxylate synthase (ACS) is a key enzyme in the biosynthesis of the plant hormone ethylene. Recently, a new biological role for ACS has been found in Cucumis melo where a single point mutation (A57V) of one isoform of the enzyme, causing reduced activity, results in andromonoecious plants. We present here a straightforward structural basis for the reduced activity of the A57V mutant, based on our work on Malus domestica ACS, including a new structure of the unliganded apple enzyme at 1.35Å resolution.
|Item Type:||Journal Article, refereed, original work|
|Communities & Collections:||04 Faculty of Medicine > Institute of Biochemistry|
07 Faculty of Science > Institute of Biochemistry
|DDC:||570 Life sciences; biology|
|Deposited On:||01 Jun 2011 15:56|
|Last Modified:||27 Nov 2013 19:26|
|Citations:||Web of Science®. Times cited: 1|
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