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

被引:6
作者
Schaerer, Martin A. [1 ]
Eliot, Andrew C. [2 ]
Gruetter, Markus G. [3 ]
Capitani, Guido [1 ,3 ]
机构
[1] Paul Scherrer Inst, CH-5232 Villigen, Switzerland
[2] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA
[3] Univ Zurich, Dept Biochem, CH-8057 Zurich, Switzerland
关键词
1-aminocyclopropane-1-carboxylate synthase; Pyridoxal 5 '-phosphate; Andromonoecy; Ethylene signalling; Protein crystallography; Comparative modelling; ACC SYNTHASE; WILD-TYPE; ETHYLENE; COMPLEX; AMINOETHOXYVINYLGLYCINE; BIOSYNTHESIS; SPECIFICITY; ENZYME; LEADS;
D O I
10.1016/j.febslet.2010.11.013
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 angstrom resolution. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
引用
收藏
页码:111 / 114
页数:4
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