The enolases of ice plant and Arabidopsis contain a potential disulphide and are redox sensitive

• Published in: Phytochemistry (Oxford) Vol. 47; no. 5; pp. 707 - 713
• Main Authors: Anderson, Louise E., Alex Dong Li, Stevens, Fred J.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier Ltd 01.03.1998; Elsevier
• Subjects: Amino Acid Sequence; amino acid sequences; Analytical, structural and metabolic biochemistry; Arabidopsis; Arabidopsis - enzymology; Arabidopsis thaliana; Binding Sites; Biological and medical sciences; chemistry; cysteine; Disulfides; Disulfides - chemistry; Disulfides - metabolism; embryo (plant); Enzyme Activation; enzyme activity; Enzymes; Enzymes and enzyme inhibitors; enzymology; Fundamental and applied biological sciences. Psychology; hydro-lyases; interspecific variation; leaves; Lyases; Mesembryanthemum crystallinum; Metabolism; molecular conformation; Molecular Sequence Data; Oxidation-Reduction; Phosphopyruvate Hydratase; Phosphopyruvate Hydratase - chemistry; Phosphopyruvate Hydratase - metabolism; Plant physiology and development; Plant Proteins; Plant Proteins - chemistry; Plant Proteins - metabolism; Plants; Plants - enzymology; Protein Structure, Tertiary; redox reactions; Ricinus communis; roots; Sequence Homology, Amino Acid; Solanum lycopersicum var. lycopersicum; Zea mays; Arabidopsis thaliana; thale cress; common ice plant; Mesembryanthemum crystallinum; enolase; activity modulation; Aizoaceae; Brassicaceae; redox-sensitive cysteines; Monocotyledones; Cysteine; Active site; Lyases; Phylogeny; Regulation(control); Structure activity relation; Three dimensional structure; Cruciferae; Gramineae; Dicotyledones; Angiospermae; Lycopersicon esculentum; Euphorbiaceae; Solanaceae; Phosphopyruvate hydratase; Aminoacid sequence; Ricinus communis; Halophyte; Oxidation reduction; Zea mays; Enzyme; Disulfide bond; Spermatophyta; Experimental plant; Carbon-oxygen lyases; Hydro-lyases

The simulated structures of the enolases of Arabidopsis and the common ice plant contain a pair of Cys residues in the correct orientation to form a disulphide bond. Formation of this disulphide might be expected to affect the positioning of several residues in the active site. The enzyme in crude e...