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

来源：

FEBS LETTERS | 2011年 / 585卷 / 01期

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

页码：111 / 114

页数：4

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