Identification and characterization of single-domain thiosulfate sulfurtransferases from Arabidopsis thaliana.
Sulfurtransferases/rhodaneses (ST) are a group of enzymes widely distributed in all three phyla that catalyze the transfer of sulfur from a donor to a thiophilic acceptor substrate. All ST contain distinct structural domains, and can exist as single-domain proteins, as tandemly repeated modules in which the C-terminal domain bears the active site, or as members of multi-domain proteins. We identified several ST in Arabidopsis resembling the C-terminus of the Arabidopsis two-domain ST1 and the single-domain GlpE protein from Escherichia coli. Two of them (accession numbers BAB10422 and BAB10409) were expressed in E. coli and purified. Both proteins showed thiosulfate-specific ST enzyme activity.
Bauer
Michael
M
Institute for Botany, University of Hannover, Herrenhäuserstr. 2, D-30419, Hannover, Germany.
Papenbrock
Jutta
J
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000201:enzymology*; D020134:Catalytic Domain; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry*; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins; D007700:Kinetics; D008969:Molecular Sequence Data; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C102897:GlpE protein, E coli