Modification of the reactivity of spinach chloroplast thioredoxin f by site-directed mutagenesis

Details

Serval ID
serval:BIB_2B3FA227DAED
Type
Article: article from journal or magazin.
Collection
Publications
Title
Modification of the reactivity of spinach chloroplast thioredoxin f by site-directed mutagenesis
Journal
Plant Science
Author(s)
del Val G., Maurer F., Stutz E., Schurmann P.
ISSN
0168-9452
Publication state
Published
Issued date
12/1999
Volume
149
Number
2
Pages
183-190
Notes
Old month value: Dec 3
Abstract
Spinach chloroplast thioredoxin f has a third cysteine residue which is surface exposed and close to the active site disulfide. In addition its N-terminus is rather long compared to other thioredoxins. By site-directed mutagenesis the third cysteine has been replaced, the long N-terminal tail has been removed and the properties of the modified proteins have been examined. Truncation of the N-terminus renders the protein more soluble and stable and has little influence on its catalytic capacities. Replacement of the exposed third cysteine clearly impairs its capacity to interact and reduce target enzymes and shows that this cysteine can be involved in homo-dimer formation.
Keywords
Cysteine, Dimer, Enzymes, Fructose 1,6-bisphosphatase, Mutagenesis, PROTEIN, protein-protein interaction, Proteins, Reactivity, Site-directed mutagenesis, Spinach, Tail, Thioredoxin f
Web of science
Create date
30/01/2008 8:40
Last modification date
20/08/2019 13:10
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