PMID- 15653770
OWN - NLM
STAT- MEDLINE
DCOM- 20050301
LR  - 20231105
IS  - 0027-8424 (Print)
IS  - 1091-6490 (Electronic)
IS  - 0027-8424 (Linking)
VI  - 102
IP  - 4
DP  - 2005 Jan 25
TI  - Characterization of potential selenium-binding proteins in the selenophosphate 
      synthetase system.
PG  - 1012-6
AB  - Selenophosphate, an activated form of selenium that can serve as a selenium 
      donor, is generated by the selD gene product, selenophosphate synthetase (SPS). 
      Selenophosphate is required by several bacteria and by mammals for the specific 
      synthesis of Secys-tRNA, the precursor of selenocysteine in selenoenzymes. 
      Although free selenide can be used in vitro for synthesis of selenophosphate, the 
      physiological system that donates selenium to SPS is incompletely characterized. 
      To detect potential selenium-delivery proteins, two known sulfurtransferases and 
      glyceraldehyde-3-phosphate dehydrogenase (GAPDH; EC 1.2.1.12) were analyzed for 
      ability to bind and transfer selenium. Rhodanese (EC 2.8.1.1) was shown to bind 
      selenium tightly, with only part of the selenium being available as substrate for 
      SPS in the presence of added reductant. 3-Mercaptopyruvate sulfurtransferase 
      (3-MST; EC 2.8.1.2) and GAPDH also bound selenium supplied as selenodiglutathione 
      formed from SeO3(2-) and glutathione. Selenium bound to 3-MST and GAPDH was 
      released more readily than that from rhodanese and also was more available as a 
      substrate for SPS. Although rhodanese retained tightly bound selenium under 
      aerobic conditions, the protein gradually became insoluble, whereas GAPDH 
      containing bound selenium was stable at neutral pH for a long period. These 
      results indicate that 3-MST and GAPDH have more suitable potentials as a 
      physiological selenium-delivery protein than rhodanese. In the presence of a 
      selenium-binding protein, a low level of selenodiglutathione formed from SeO3(2-) 
      and glutathione could effectively replace the high concentrations of selenide 
      routinely used as substrate in the SPS in vitro assays.
FAU - Ogasawara, Yuki
AU  - Ogasawara Y
AD  - Department of Environmental Biology, Meiji Pharmaceutical University, 2-522-1 
      Noshio, Kiyose, Nishitokyo, Tokyo 204-8588, Japan. yo@my-pharm.ac.jp
FAU - Lacourciere, Gerard M
AU  - Lacourciere GM
FAU - Ishii, Kazuyuki
AU  - Ishii K
FAU - Stadtman, Thressa C
AU  - Stadtman TC
LA  - eng
PT  - Journal Article
DEP - 20050114
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Carrier Proteins)
RN  - 0 (Selenium-Binding Proteins)
RN  - EC 2.7.- (Phosphotransferases)
RN  - EC 2.7.9.3 (selenophosphate synthetase)
RN  - GAN16C9B8O (Glutathione)
RN  - H6241UJ22B (Selenium)
SB  - IM
MH  - Carrier Proteins/*analysis
MH  - Chromatography, High Pressure Liquid
MH  - Glutathione/pharmacology
MH  - Phosphotransferases/*analysis/chemistry
MH  - Selenium/*metabolism
MH  - Selenium-Binding Proteins
PMC - PMC545862
EDAT- 2005/01/18 09:00
MHDA- 2005/03/02 09:00
PMCR- 2005/07/25
CRDT- 2005/01/18 09:00
PHST- 2005/01/18 09:00 [pubmed]
PHST- 2005/03/02 09:00 [medline]
PHST- 2005/01/18 09:00 [entrez]
PHST- 2005/07/25 00:00 [pmc-release]
AID - 0409042102 [pii]
AID - 01021012 [pii]
AID - 10.1073/pnas.0409042102 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 2005 Jan 25;102(4):1012-6. doi: 
      10.1073/pnas.0409042102. Epub 2005 Jan 14.