Details
| Original language | English |
|---|---|
| Pages (from-to) | 427-431 |
| Number of pages | 5 |
| Journal | FEBS letters |
| Volume | 532 |
| Issue number | 3 |
| Publication status | Published - 18 Dec 2002 |
Abstract
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.
Keywords
- 3-Mercaptopyruvate, Arabidopsis thaliana, Protein domain, Rhodanese, Sulfurtransferase, Thiosulfate
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biophysics
- Biochemistry, Genetics and Molecular Biology(all)
- Structural Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
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In: FEBS letters, Vol. 532, No. 3, 18.12.2002, p. 427-431.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Identification and characterization of single-domain thiosulfate sulfurtransferases from Arabidopsis thaliana
AU - Bauer, Michael
AU - Papenbrock, Jutta
N1 - Funding information: We would like to thank Pamela von Trzebiatowski and Julia Volker for their excellent technical assistance. We are grateful to Prof. A. Schmidt, University of Hannover, for helpful discussions. The work was financially supported by the Deutsche Forschungsgemeinschaft (PA 764/1-3, SCHM 307/15-1) and the Fonds der Chemischen Industrie.
PY - 2002/12/18
Y1 - 2002/12/18
N2 - 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.
AB - 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.
KW - 3-Mercaptopyruvate
KW - Arabidopsis thaliana
KW - Protein domain
KW - Rhodanese
KW - Sulfurtransferase
KW - Thiosulfate
UR - http://www.scopus.com/inward/record.url?scp=0037132550&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(02)03723-7
DO - 10.1016/S0014-5793(02)03723-7
M3 - Article
C2 - 12482606
AN - SCOPUS:0037132550
VL - 532
SP - 427
EP - 431
JO - FEBS letters
JF - FEBS letters
SN - 0014-5793
IS - 3
ER -