Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 43-57 |
| Seitenumfang | 15 |
| Fachzeitschrift | AMINO ACIDS |
| Jahrgang | 41 |
| Ausgabenummer | 1 |
| Publikationsstatus | Veröffentlicht - 1 Juni 2011 |
Abstract
Sulfurtransferases/rhodaneses (Str) comprise a group of enzymes widely distributed in all phyla which catalyze in vitro the transfer of a sulfur atom from suitable sulfur donors to nucleophilic sulfur acceptors. The best characterized Str is bovine rhodanese (EC 2.8.1.1) which catalyses in vitro the transfer of a sulfane sulfur atom from thiosulfate to cyanide, leading to the formation of sulfite and thiocyanate. Plants as well as other organisms contain many proteins carrying a typical rhodanese pattern or domain forming multi-protein families (MPF). Despite the presence of Str activities in many living organisms, the physiological role of the members of this MPF has not been established unambiguously. While in mammals these proteins are involved in the elimination of toxic cyanogenic compounds, their ubiquity suggests additional physiological functions. In plants, Str are localized in the cytoplasm, mitochondria, plastids, and nucleus. Str probably also transfer reduced sulfur onto substrates as large as peptides or proteins. Several studies in different organisms demonstrate a protein-protein interaction with members of the thioredoxin MPF indicating a role of Str in maintenance of the cellular redox homeostasis. The increased expression of several members of the Str MPF in various stress conditions could be a response to oxidative stress. In summary, data indicate that Str are involved in various essential metabolic reactions.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biochemie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Klinische Biochemie
- Chemie (insg.)
- Organische Chemie
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in: AMINO ACIDS, Jahrgang 41, Nr. 1, 01.06.2011, S. 43-57.
Publikation: Beitrag in Fachzeitschrift › Übersichtsarbeit › Forschung › Peer-Review
}
TY - JOUR
T1 - Latest news about the sulfurtransferase protein family of higher plants
AU - Papenbrock, Jutta
AU - Guretzki, Sebastian
AU - Henne, Melina
N1 - Funding information: We would like to thank Dr. Fabio Forlani, Milan, Italy, for stimulating discussions. The work was financially supported by the Deutsche Forschungsgemeinschaft (PA 764/1-4 and 5, PA 764/7-1) and by the DAAD (Vigoni 0815171).
PY - 2011/6/1
Y1 - 2011/6/1
N2 - Sulfurtransferases/rhodaneses (Str) comprise a group of enzymes widely distributed in all phyla which catalyze in vitro the transfer of a sulfur atom from suitable sulfur donors to nucleophilic sulfur acceptors. The best characterized Str is bovine rhodanese (EC 2.8.1.1) which catalyses in vitro the transfer of a sulfane sulfur atom from thiosulfate to cyanide, leading to the formation of sulfite and thiocyanate. Plants as well as other organisms contain many proteins carrying a typical rhodanese pattern or domain forming multi-protein families (MPF). Despite the presence of Str activities in many living organisms, the physiological role of the members of this MPF has not been established unambiguously. While in mammals these proteins are involved in the elimination of toxic cyanogenic compounds, their ubiquity suggests additional physiological functions. In plants, Str are localized in the cytoplasm, mitochondria, plastids, and nucleus. Str probably also transfer reduced sulfur onto substrates as large as peptides or proteins. Several studies in different organisms demonstrate a protein-protein interaction with members of the thioredoxin MPF indicating a role of Str in maintenance of the cellular redox homeostasis. The increased expression of several members of the Str MPF in various stress conditions could be a response to oxidative stress. In summary, data indicate that Str are involved in various essential metabolic reactions.
AB - Sulfurtransferases/rhodaneses (Str) comprise a group of enzymes widely distributed in all phyla which catalyze in vitro the transfer of a sulfur atom from suitable sulfur donors to nucleophilic sulfur acceptors. The best characterized Str is bovine rhodanese (EC 2.8.1.1) which catalyses in vitro the transfer of a sulfane sulfur atom from thiosulfate to cyanide, leading to the formation of sulfite and thiocyanate. Plants as well as other organisms contain many proteins carrying a typical rhodanese pattern or domain forming multi-protein families (MPF). Despite the presence of Str activities in many living organisms, the physiological role of the members of this MPF has not been established unambiguously. While in mammals these proteins are involved in the elimination of toxic cyanogenic compounds, their ubiquity suggests additional physiological functions. In plants, Str are localized in the cytoplasm, mitochondria, plastids, and nucleus. Str probably also transfer reduced sulfur onto substrates as large as peptides or proteins. Several studies in different organisms demonstrate a protein-protein interaction with members of the thioredoxin MPF indicating a role of Str in maintenance of the cellular redox homeostasis. The increased expression of several members of the Str MPF in various stress conditions could be a response to oxidative stress. In summary, data indicate that Str are involved in various essential metabolic reactions.
KW - 3-Mercaptopyruvate
KW - Arabidopsis thaliana
KW - Oxidative stress
KW - Thioredoxin
KW - Thiosulfate
UR - http://www.scopus.com/inward/record.url?scp=79960395086&partnerID=8YFLogxK
U2 - 10.1007/s00726-010-0478-6
DO - 10.1007/s00726-010-0478-6
M3 - Review article
C2 - 20135153
AN - SCOPUS:79960395086
VL - 41
SP - 43
EP - 57
JO - AMINO ACIDS
JF - AMINO ACIDS
SN - 0939-4451
IS - 1
ER -