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

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

doi:10.1016/j.febslet.2010.11.013

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

FEBS Lett. 2011 Jan 3;585(1):111-4. doi: 10.1016/j.febslet.2010.11.013. Epub 2010 Nov 12.

Authors

Martin A Schärer¹, Andrew C Eliot, Markus G Grütter, Guido Capitani

Affiliation

¹ Biomolecular Research, Paul Scherrer Institut, Villigen PSI, Switzerland.

PMID: 21075107
DOI: 10.1016/j.febslet.2010.11.013

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Amino Acid Substitution
Catalytic Domain
Crystallography, X-Ray
Lyases / chemistry
Lyases / genetics*
Lyases / metabolism
Malus / enzymology
Malus / genetics*
Models, Molecular
Molecular Sequence Data
Mutation*
Plant Proteins / chemistry
Plant Proteins / genetics*
Plant Proteins / metabolism
Protein Structure, Tertiary
Sequence Homology, Amino Acid

Substances

Plant Proteins
Lyases
1-aminocyclopropanecarboxylate synthase