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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Abstract
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 |
| Language: | English |
| Date: | 2011 |
| Deposited On: | 01 Jun 2011 15:56 |
| Last Modified: | 09 Jul 2012 06:51 |
| Publisher: | Elsevier |
| ISSN: | 0014-5793 |
| Publisher DOI: | 10.1016/j.febslet.2010.11.013 |
| PubMed ID: | 21075107 |
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