Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Gerard M. Lacourciere"'
Autor:
Timothy J. Larson, Matt D. Wolfe, Farzana Ahmed, Thressa C. Stadtman, Charles T. Lauhon, Gerard M. Lacourciere
Publikováno v:
Journal of Biological Chemistry. 279:1801-1809
Escherichia coli has eight genes predicted to encode sulfurtransferases having the active site consensus sequence Cys-Xaa-Xaa-Gly. One of these genes, ybbB, is frequently found within bacterial operons that contain selD, the selenophosphate synthetas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::948050d15a5d016abd34fd7d0befede3
https://doi.org/10.1074/jbc.m310442200
https://doi.org/10.1074/jbc.m310442200
Autor:
Hisaaki Mihara, Tatsuo Kurihara, Thressa C. Stadtman, Nobuyoshi Esaki, Umechiyo Tokumoto, Robert A. J. D. Kennedy, Gerard M. Lacourciere, Yasuhiro Takahashi, Shin-ichiro Kato
Publikováno v:
Proceedings of the National Academy of Sciences. 99:6679-6683
Three NifS-like proteins, IscS, CSD, and CsdB, from Escherichia coli catalyze the removal of sulfur and selenium from l -cysteine and l -selenocysteine, respectively, to form l -alanine. These enzymes are proposed to function as sulfur-delivery prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc63ec470527a317bfecff86166613b4
https://doi.org/10.1073/pnas.102176099
https://doi.org/10.1073/pnas.102176099
Publikováno v:
Proceedings of the National Academy of Sciences. 98:9494-9498
Selenophosphate is the active selenium-donor compound required by bacteria and mammals for the specific synthesis of Secys-tRNA, the precursor of selenocysteine in selenoenzymes. Although free selenide can be used in vitro for the synthesis of seleno
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66db563c4c004b69d89bb8324936e32d
https://doi.org/10.1073/pnas.171320998
https://doi.org/10.1073/pnas.171320998
Publikováno v:
BioFactors. 14:69-74
Selenophosphate synthetase (SPS), the selD gene product from Escherichia coli, catalyzes the biosynthesis of monoselenophosphate from selenide and ATP. Characterization of selenophosphate synthetase revealed the determined K(m) value for selenide is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::302af5050b62c258d5f46070f183318b
https://doi.org/10.1002/biof.5520140110
https://doi.org/10.1002/biof.5520140110
Publikováno v:
Annual Review of Nutrition. 19:1-16
Selenocysteine-containing enzymes that have been identified in mammals include the glutathione peroxidase family (GPX1, GPX2, GPX3, and GPX4), one or more iodothyronine deiodinases and two thioredixin reductases. Selenoprotein P, a glycoprotein that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d2f359b3ca98b2aed9a00237edfbf1a
https://doi.org/10.1146/annurev.nutr.19.1.1
https://doi.org/10.1146/annurev.nutr.19.1.1
Publikováno v:
Proceedings of the National Academy of Sciences. 96:44-48
The selD gene from Haemophilus influenzae has been overexpressed in Escherichia coli . The expressed protein was purified to homogeneity in a four-step procedure and then carboxymethylated by reaction with chloroacetate. N-terminal sequencing by Edma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::085927e1e0d524bf74094c08d695c8d9
https://doi.org/10.1073/pnas.96.1.44
https://doi.org/10.1073/pnas.96.1.44
Autor:
Gerard M. Lacourciere
Publikováno v:
BioFactors. 10:237-244
Selenophosphate synthetase, the product of the selD gene, produces the highly active selenium donor, monoselenophosphate, from selenide and ATP. Positional isotope exchange experiments have shown hydrolysis of ATP occurs by way of a phosphoryl-enzyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08b2b293610a1c5456223ede11dfe4a6
https://doi.org/10.1002/biof.5520100222
https://doi.org/10.1002/biof.5520100222
Publikováno v:
Journal of Biological Chemistry. 273:30921-30926
The NIFS protein from Azobacter vinelandii is a pyridoxal phosphate-containing homodimer that catalyzes the formation of equimolar amounts of elemental sulfur and L-alanine from the substrate L-cysteine (Zheng, L., White, R. H., Cash, V. L., Jack, R.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6630fe8ba69536a4841ef510d257c1b1
https://doi.org/10.1074/jbc.273.47.30921
https://doi.org/10.1074/jbc.273.47.30921
Publikováno v:
Chemical Research in Toxicology. 7:121-124
Sequence alignments of mammalian microsomal (MEH) and soluble epoxide hydrolases (SEH) with bacterial haloalkane dehalogenase (HAD) and haloacetate dehalogenase (HAcD) together with structural and functional evidence suggest that these four enzymes a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93035c25f62ee5036cf65693033bd799
https://doi.org/10.1021/tx00038a001
https://doi.org/10.1021/tx00038a001
Autor:
Malcolm Moos, Carina P. Tan, Gerard M. Lacourciere, Gerard H. Edwards, Richard N. Armstrong, Vikram N. Vakharia, Diane I. Morris
Publikováno v:
Biochemistry. 32:2610-2616
A recombinant baculovirus (vEHX) encoding rat hepatic microsomal epoxide hydrolase has been constructed. Infection of Spodoptera frugiperda (Sf9) cells with the recombinant virus results in the expression of the enzyme at a level estimated to be betw
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09e4c88448c13d38a7af84fd86be8763
https://doi.org/10.1021/bi00061a019
https://doi.org/10.1021/bi00061a019