Structural basis for reduced activity of 1‐aminocyclopropane‐1‐carboxylate synthase affected by a mutation linked to andromonoecy | Zendy

Schärer Martin A. | Zendy; Eliot Andrew C. | Zendy; Grütter Markus G. | Zendy; Capitani Guido | Zendy

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Structural basis for reduced activity of 1‐aminocyclopropane‐1‐carboxylate synthase affected by a mutation linked to andromonoecy

Author(s) -

Schärer Martin A.,

Eliot Andrew C.,

Grütter Markus G.,

Capitani Guido

Publication year - 2011

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2010.11.013

Subject(s) - mutant , enzyme , cucumis , biochemistry , enzyme assay , biosynthesis , mutation , atp synthase , chemistry , point mutation , biology , botany , gene

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 1.35 Å resolution.

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