print visible entries

print all entries

Ligand selenium

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for selenium

close all tables

open all tables

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

top print hide

Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.1.96

S-adenosyl-L-methionine + selenium = S-adenosyl-L-homocysteine + ?

676338

-

2.5.1.144

O-acetyl-L-serine + selenide = L-selenocysteine + acetate

761117

-

2.7.9.3

ATP + selenide + H2O = AMP + selenophosphate + phosphate

702181, 738336, 738466, 761118, 761271, 705151, 737876, 760584, 737371, 737653, 762427, 645480, 645479, 645492, 645494, 645493, 645482, 663220, 693677, 728320

-

2.7.9.3

ATP + selenide = AMP + selenophosphate + phosphate

694096, 691493, 690290, 694071, 691196, 691179

-

2.7.9.3

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

top print hide

Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.97.1.9

selenite + NADH + H+ = selenium + H2O + NAD+

-

-

4.4.1.16

L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor

648740, 648751, 648753, , 645630, 645632, 648745, 648742, 648744, 648741, 648743, 648750, 648748, 648746, 648747

-

Substrate in Enzyme-catalyzed Reactions (7 results)

top print hide

Show Substrate (7 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.1.96

S-adenosyl-L-methionine + selenium = S-adenosyl-L-homocysteine + ?

676338

-

2.5.1.144

O-acetyl-L-serine + selenide = L-selenocysteine + acetate

761117

-

2.5.1.47

O-acetyl-Ser + selenide = selenocysteine + acetate

34691

-

2.7.9.3

2'(3')-O-(2,4,6-trinitrophenyl)adenosine-5'-triphosphate + selenide + H2O = 2'(3')-O-(2,4,6-trinitrophenyl)adenosine-5'-monophosphate + selenophosphate + phosphate

738466

-

2.7.9.3

ATP + selenide + H2O = AMP + selenophosphate + phosphate

645480, 721940, 645490, 645492, 662872, 671895, 645483, 645484, 645485, 702181, 738336, 738466, 761118, 761271, 645489, 675033, 675895, 645486, 705151, 737876, 760584, 737371, 737653, 722096, 722547, 728320, 762427, 645487, 645479, 645482, 645481, 645488, 645491, 645494, 645493, 663220, 693677

-

2.7.9.3

ATP + selenide = AMP + selenophosphate + phosphate

694794, 694096, 694071, 691179, 691493, 690290, 691196

-

2.7.9.3

3 entries

2.9.1.1

L-Seryl-tRNASec + selenide = ?

22917

-

Product in Enzyme-catalyzed Reactions (12 results)

top print hide

Show Product (12 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.12.7.2

(SeO3)2- + H2 + ? = Se + H2O + ?

-

-

1.8.98.7

Ac-YYTSPMSeCAPARSMLLTGN + S-adenosyl-L-methionine = Ac-YYTSPM-3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen selenide

-

-

1.8.99.5

SeO32- + a [DsrC protein]-dithiol + 2 reduced methyl viologen + 2 H+ = HSe- + a [DsrC protein]-disulfide + 2 oxidized methyl viologen + 3 H2O

-

-

1.97.1.9

selenite + NADH + H+ = selenium + H2O + NAD+

-

-

2.8.1.7

L-selenocysteine = L-alanine + selenium

, 645632, 645624

-

2.8.1.9

L-selenocysteine = L-alanine + H2Se

-

-

4.4.1.11

L-selenodjenkolate = pyruvate + NH3 + H2Se + formaldehyde

34525

-

4.4.1.15

DL-selenocysteine + H2O = selenide + L-alanine

-

-

4.4.1.15

L-selenocystine + H2O = selenide + L-alanine

-

-

4.4.1.16

L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor

648740, 648751, 648753, , 645630, 645632, 648746, 648745, 648742, 648744, 648747, 648741, 648743, 648750, 648748

-

4.4.1.16

selenomethionine reduced acceptor = methylselenole + selenide

-

-

4.4.1.16

L-selenocysteine + reduced acceptor = L-alanine + selenium + acceptor

-

-

4.4.1.15

2 entries

4.4.1.16

3 entries

Activator in Enzyme-catalyzed Reactions (3 results)

top print hide

Show Activating Compound (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.11.1.13

-

696578

-

1.13.11.19

cofactor-like compound

396333, 396416, 396417

-

1.13.11.19

sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)

396333

-

1.13.11.19

2 entries

Inhibitor in Enzyme-catalyzed Reactions (3 results)

top print hide

Show Inhibitors (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.11.1.13

-

696578

-

1.13.11.19

sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)

396333

-

1.2.3.1

enzyme activity towards substrates (S)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine and vanillin is increased by selenium deficiency to 250% of initial rate, and this corresponds to an increase of Aox1 protein level, but not to a decrease in mRNA level

696560

-

Metals and Ions (98 results)

top print hide

Show Metals Ions (98 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

steady-state fluorescence properties of alcohol dehydrogenase and its selenomethionyl derivative

720145

-

1.1.1.1

the effect of significant decrease in intrinsic fluorescence intensity of the enzyme caused by replacement of S atoms of methionine residues to Se is explained on the basis of the analysis of its 3D structure. All selenium atoms are located far from both Trp95 and Trp117 and can not cause their fluorescence quenching. Substitution of S by Se causes enhanced protein absorption in the UV-region. This effect is explained by the formation of Se complex with some groups of protein

720330

-

1.1.1.1

2 entries

1.1.1.157

the enzyme contains selenomethionine. Incorporation of selenium into the enzyme occurs randomly and is not required for any specific function

286046

-

1.11.1.12

-

394878, 394877, 394880, 394870, 394876, 394882

-

1.11.1.12

1 g-atom Se per mol protein

394864

-

1.11.1.12

10 selenocysteines per protein molecule

394873

-

1.11.1.12

enzyme contains a selenocysteine residue at the active site

394879, 394867

-

1.11.1.12

Se in selenol form

394864

-

1.11.1.12

TGA-encoded selenocysteine at residue 46 and active site residues Gln82 and Trp135 that interact with the selenocysteine

674008

-

1.11.1.12

-

696435, 698045, 701272, 701138, 697470, 697468, 696173

-

1.11.1.12

selenoprotein

658247, 658758

-

1.11.1.9

selenium-dependent enzyme

677190

-

1.11.1.9

-

675985, 673172

-

1.11.1.9

activity depends on selenium

684496

-

1.11.1.9

contains one selenium ion per subunit

690043

-

1.11.1.9

dependent on

690120, 723898, 725048, 724798

-

1.11.1.9

Gpx is a selenium-containing enzyme

701138

-

1.11.1.9

one atom of selenium per subunit

396640

-

1.11.1.9

selenium supplementation (0.2 mg/kg) remarkably improves glutathione peroxidase activity

696580

-

1.11.1.9

selenium supplementation by selenoprotein P prevents oxidative damage of human endothelial cells by restoring expression and enzymatic activity of glutathione peroxidase

673807

-

1.11.1.9

selenium-containing enzyme

702092

-

1.11.1.9

selenium-dependent enzyme

658896, 742715, 742568

-

1.11.1.9

selenocysteine

396603, 396604, 396605, 396627, 396632, 396635, 396613, 396621, 396622, 396606, 396639

-

1.11.1.9

selenoenzyme

687123, 701039

-

1.11.1.9

selenoprotein

685333, 685439, 684392

-

1.11.1.9

selenoprotein, selenium is necessary for activity

685921

-

1.11.1.9

subtoxic range of selenium (100 nM) concentrations are required to increase and maintain the expression of anti-oxidant selenoproteins glutathione peroxidase GPX1 and GPX4 at a constant level in cultures of human adenocarcinoma cell lines (H460, H1703 and H1944) and in HPL1D, a non-transformed lung epithelial cell line

675758

-

1.11.1.9

the enzyme contains selenium

700072

-

1.12.2.1

NiFeSe enzyme, contains selenium in equimolar amounts to Ni

674919

-

1.12.2.1

[NiFeSe] enzyme, ratio Ni:Se:Fe is 1:1:15

674919

-

1.12.2.1

0.45 selenium atoms per molecule

395567

-

1.12.2.1

[NiFeSe] hydrogenase

395571

-

1.11.1.12

8 entries

1.11.1.9

17 entries

1.12.2.1

4 entries

1.12.7.2

the large subunit contains a selenocysteine

439656

-

1.12.98.1

as selenocysteine, only present in 42000 D subunit

395079

-

1.12.98.1

no selenium detected

395093

-

1.12.98.1

2 entries

1.12.99.6

[NiFeSe]-hydrogenase

704162

-

1.17.1.10

-

288217, 288220

-

1.17.1.10

2 mol of selenium per mol of enzyme, resides in the alpha-subunit

288219

-

1.17.1.4

-

644577

-

1.17.1.4

0.13 g-atom selenium per native enzyme molecule

644592

-

1.17.1.4

3.4 g-atom per mol enzyme

644566

-

1.17.1.4

-

659012

-

1.17.1.4

dependent on, selenium is required in a labile form

715377

-

1.17.5.3

the enzyme contains (in relative molar amounts): 1.0 heme, 0.95 molybdenum, 0.96 selenium, 14 non-heme iron, and 13 acid-labile sulfide. The alpha polypeptide contains significant amounts of selenium

698681

-

1.17.5.3

the enzyme contains selenocysteine. Both stability and specific nucleotide sequences of a mRNA stem-loop likely contribute to the appropriate mRNA context for selenocysteine incorporation into the fdnG gene product

698689

-

1.17.98.4

formate dehydrogenase H contains selenocysteine as an integral amino acid. Selenium of formate dehydrogenase H is directly involved in formate oxidation

701023

-

1.17.98.4

Mo of the molybdopterin is coordinated with the Se atom of selenocysteine

701024

-

1.17.98.4

selenocysteine is located at amino acid position 140

695650

-

1.17.98.4

selenocysteine-containing enzyme. The molybdenum-coordinated selenocysteine is essential for catalytic activity of the native enzyme

698704

-

1.17.98.4

selenocysteine-containing polypeptide

701021

-

1.17.98.4

the enzyme contains selenocysteine

698686

-

1.17.98.4

the enzyme contains selenocysteine. The Mo-Se bond is estimated to be covalent to the extent of 17-27% of the unpaired electron spin density residing in the valence 4s and 4p selenium orbitals, based on comparison of the scalar and dipolar hyperfine components to atomic 77Se. Two electron oxidation of formate by the Mo(VI) state converts Mo to the reduced Mo(IV) state with the formate proton, H+(formate), transferring to a nearby base Y-. Transfer of one electron to the Fe4S4 center converts Mo(IV) to the EPR detectable Mo(V) state. The Y- is located within magnetic contact to the [Mo-Se] center, as shown by its strong dipolar 1Hf hyperfine couplings. Photolysis of the formate-induced Mo(V) state abolishes the 1Hf hyperfine splitting from YH(formate), suggesting photoisomerization of this group or phototransfer of the proton to a more distant proton acceptor group A-. The minor effect of photolysis on the 77Se-hyperfine interaction with [77Se] selenocysteine suggests that the Y- group is not the Se atom, but instead might be the imidazole ring of the His141 residue which is located in the putative substrate-binding pocket close to the [Mo-Se] center. It is proposed that the transfer of H+(formate) from formate to the active site base Y- is thermodynamically coupled to two-electron oxidation of the formate molecule, thereby facilitating formation of CO2

696191

-

1.17.98.4

the enzyme contains selenocysteine.The trxB gene is required for the formation of selenocysteine containing FDHH polypeptide

687454

-

1.17.98.4

the fdhF gene of Escherichia coli codes for the selenocysteine-including protein subunit of formate dehydrogenase H

700262

-

1.17.98.4

the reinterpretation of the crystal structure suggests a new reaction mechanism: In step I, formate binds directly to Mo, displacing Se-Cys140. In step II, the alpha-proton from formate may be transferred to the nearby His141 that acts as general base. In this step the CO2 molecule can be released and two electrons transferred to Mo. Alternatively, step II may involve a selenium-carboxylated intermediate. In step III, electrons from Mo(IV) are transferred via the [4Fe-4S] center to an external electron acceptor and the catalytic cycle is completed

674932

-

1.17.98.4

anaerobic oxidation of formate by Methanococcus vannielii is catalyzed by two readily separable formate dehydrogenases. One of these is a 105000 Da protein that contains molybdenum, iron, and acid-labile sulfide, but not selenium. The other is a high molecular weight complex composed of selenoprotein and molybdo-iron sulfur protein subunits

727803

-

1.17.1.10

2 entries

1.17.1.4

5 entries

1.17.5.3

2 entries

1.17.98.4

11 entries

1.2.2.1

enzyme from cells grown in selenite contains selenium, covalently bound to the largest subunit

390369

-

1.2.5.3

-

725392

-

1.2.5.3

active-site residues S-selanyl-Cys385 and Glu757

656481

-

1.2.5.3

an S-selanylcysteine-containing large subunit

736397

-

1.2.5.3

necessity of S-selanylcysteine for the catalyzed reaction, the selenium atom of S-selanylcysteine at the active site is located in a distance of 3.7 A from the Mo ion. It is near the equatorial oxo and hydroxo group of the Mo ion

390482

-

1.21.99.3

selenoenzyme

659569

-

1.21.99.3

selenoprotein

716049

-

1.21.99.4

contains selenocysteine in the active center

658557

-

1.21.99.4

enzyme contains selenocysteine

659748

-

1.21.99.4

enzyme contains selenocysteine in the highly conserved active senter at position 133. Selenium plays a critical role in deiodination

658556

-

1.21.99.4

selenoprotein

659156

-

1.21.99.4

-

701298, 700153

-

1.21.99.4

selenoprotein

716049

-

1.2.5.3

4 entries

1.21.99.3

2 entries

1.21.99.4

6 entries

1.8.1.7

regulates the enzyme expression pattern, enzyme contains a catalytic selenocysteine

659484

-

1.8.1.9

-

675564

-

1.8.1.9

0.001 mM, 5fold increase of activity after 7 days

675915

-

1.8.1.9

all three isoenzymes of mammalian TrxR contain an essential selenocysteine residue, which is the target of several drugs in cancer treatment or mercury intoxication

711101

-

1.8.1.9

contains an essential selenocysteine residue

659902

-

1.8.1.9

selenocysteine-containing enzyme

658760

-

1.8.1.9

selenoenzyme

696435, 659779, 686324

-

1.8.1.9

selenoprotein

711146, 658795, 659211, 658794, 689708, 684809

-

1.8.1.9

selenoprotein, expression and function depends on adequate supply of selenium

685445

-

1.8.1.9

selenoprotein. TrxR1 is more sensitive to Se depletion than TrxR2, greater changes in liver than kidney. There is a prioritisation of TrxR2 over TrxR1 during Se deficiency such that TrxR1 expression is more sensitive to Se supply than TrxR2 but this sensitivity of TrxR1 is not fully accounted for by TrxR1 5' or 3'-untranslated region sequences when assessed using luciferase reporter constructs

684671

-

1.8.1.9

the enzyme possesses selenium in the form of selenocysteine in the active site

710835

-

1.8.1.9

the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin

696235

-

1.8.1.9

thioredoxin reductase 1 is a selenoprotein, the oxidized enzyme presents a selenenylsulfide motif in trans-configuration, with the selenium atom of selenocysteine-498 positioned beneath the side chain of Tyr-116

698965

-

1.8.1.9

thioredoxin reductase is a selenoprotein

696439

-

1.8.1.9

TrxR1 contains a selenocysteine in the active site (Gly-Cys-SeCys-Gly)

713184

-

1.8.1.9

TrxR1 is a selenoprotein that contains a selenocysteine residue at the penultimate C-terminal

698053

-

1.8.1.B1

glutathione reductase and thioredoxin reductase activities are dependent on the Sec-containing redox center. The activity loss caused by the Sec-to-Cys mutation can be partially compensated by a Cys-to-Sec mutation of the neighboring residue, indicating that Sec can support catalysis at this alternative position

687730

-

1.8.1.B1

selenocysteine protein

688886

-

1.8.4.11

selenocysteine-containing

684984

-

1.8.4.11

selenoprotein, has a single selenocysteine residue at the catalytic site, the selenocysteine-containing MsrA exhibits at least a 20fold higher activity than its cysteine mutant form U16C, indicating a critical role of selenocysteine in the catalytic activity of the enzyme

701130

-

1.8.4.12

selenocysteine-containing

684984

-

1.8.4.12

selenoprotein

393076, 710848, 658704, 658212

-

1.8.4.12

selenoprotein. Se status affects Msr (most likely through effects on the selenoprotein MsrB)

685479

-

1.8.4.12

the selenocysteine-containing Clostridium MsrB form exhibits 100fold higher activity than its Cys-containing form, revealing that selenocysteine provides the catalytic advantage of higher activity. A resolving Cys is required for the thioredoxin-dependent recycling process of the selenocysteine-containing form. Thus, thioredoxin can reduce the selenylsulfide bond, but its Trx-dependent recycling process is much less efficient compared to that for the disulfide bond in the Cys-containing form, demonstrating an obvious catalytic disadvantage

684729

-

1.8.1.9

15 entries

1.8.1.B1

2 entries

1.8.4.11

2 entries

1.8.4.12

4 entries

1.97.1.1

contains selenium 2.9 mol, based of apparent molecular mass of 420000 Da

437685

-

1.97.1.9

isolated enzyme contains a reduced form of selenium, probably as selenocysteine

658902

-

2.3.1.67

as a consequence of Se deficiency increased phospholipase D activity and phosphatidic acid production contribute to enhanced enzyme activity, which results in an overall increase in platelet activating factor. The regulation of enzyme activity by Se may constitute an important control mechanism for the maintenance of levels of platelet activating factor in endothelial cells

657735

-

2.5.1.18

production of recombinant selenoproteins with internal selenocysteine residues in Escherichia coli. Introduction of a selenocysteine residue into the catalytic site of glutathione S-transferase is not sufficient to induce glutathione peroxidase activity in spite of a maintained glutathione-binding capacity

660881

-

2.7.9.3

selenoprotein

728320

-

3D Structure of Enzyme-Ligand-Complex (PDB) (80 results)

top print hide

Show 3D Structure of Enzyme-Ligand-Complex (PDB) (80 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.1.1.6

3uhj, 3D-view

1.18.6.1

5bvg, 3D-view

1.18.6.1

6op2, 3D-view

1.18.6.1

6op3, 3D-view

1.18.6.1

5bvg, 3D-view

1.18.6.1

6op2, 3D-view

1.18.6.1

6op3, 3D-view

1.18.6.1

5bvg, 3D-view

1.18.6.1

6op2, 3D-view

1.18.6.1

6op3, 3D-view

1.18.6.1

5bvg, 3D-view

1.18.6.1

6op2, 3D-view

1.18.6.1

6op3, 3D-view

1.18.6.1

5bvg, 3D-view

1.18.6.1

6op2, 3D-view

1.18.6.1

6op3, 3D-view

1.18.6.1

5bvg, 3D-view

1.18.6.1

6op2, 3D-view

1.18.6.1

6op3, 3D-view

1.18.6.1

18 entries

2.7.4.6

1pae, 3D-view

2.7.7.48

7bak, 3D-view

2.7.7.48

7bal, 3D-view

2.7.7.48

7bak, 3D-view

2.7.7.48

7bal, 3D-view

2.7.7.48

7bak, 3D-view

2.7.7.48

7bal, 3D-view

2.7.7.48

7bak, 3D-view

2.7.7.48

7bal, 3D-view

2.7.7.48

7bak, 3D-view

2.7.7.48

7bal, 3D-view

2.7.7.48

7bak, 3D-view

2.7.7.48

7bal, 3D-view

3.4.19.12

7bak, 3D-view

3.4.19.12

7bal, 3D-view

3.4.19.12

7bak, 3D-view

3.4.19.12

7bal, 3D-view

3.4.19.12

7bak, 3D-view

3.4.19.12

7bal, 3D-view

3.4.19.12

7bak, 3D-view

3.4.19.12

7bal, 3D-view

3.4.19.12

7bak, 3D-view

3.4.19.12

7bal, 3D-view

3.4.19.12

7bak, 3D-view

3.4.19.12

7bal, 3D-view

3.4.22.69

7bak, 3D-view

3.4.22.69

7bal, 3D-view

3.4.22.69

7bak, 3D-view

3.4.22.69

7bal, 3D-view

3.4.22.69

7bak, 3D-view

3.4.22.69

7bal, 3D-view

3.4.22.69

7bak, 3D-view

3.4.22.69

7bal, 3D-view

3.4.22.69

7bak, 3D-view

3.4.22.69

7bal, 3D-view

3.4.22.69

7bak, 3D-view

3.4.22.69

7bal, 3D-view

3.6.4.12

7bak, 3D-view

3.6.4.12

7bal, 3D-view

3.6.4.12

7bak, 3D-view

3.6.4.12

7bal, 3D-view

3.6.4.12

7bak, 3D-view

3.6.4.12

7bal, 3D-view

3.6.4.12

7bak, 3D-view

3.6.4.12

7bal, 3D-view

3.6.4.12

7bak, 3D-view

3.6.4.12

7bal, 3D-view

3.6.4.12

7bak, 3D-view

3.6.4.12

7bal, 3D-view

3.6.4.13

7bak, 3D-view

3.6.4.13

7bal, 3D-view

3.6.4.13

7bak, 3D-view

3.6.4.13

7bal, 3D-view

3.6.4.13

7bak, 3D-view

3.6.4.13

7bal, 3D-view

3.6.4.13

7bak, 3D-view

3.6.4.13

7bal, 3D-view

3.6.4.13

7bak, 3D-view

3.6.4.13

7bal, 3D-view

3.6.4.13

7bak, 3D-view

3.6.4.13

7bal, 3D-view

2.7.7.48

12 entries

3.4.19.12

12 entries

3.4.22.69

12 entries

3.6.4.12

12 entries

3.6.4.13

12 entries

Enzyme Kinetic Parameters

K_M Value (3 results)

top print hide

Show KM Value (3 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.7.9.3

0.02

-

pH 7.8, 37°C

645490

2.7.9.3

0.025

-

pH 7.8, 37°C

645490

2.7.9.3

0.046

-

pH 7.2, 37°C

645482

2.7.9.3

3 entries

References & Links

Literature References (204)

top print hide

Show Reference (204 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

22917

9688279

Bacterial selenocysteine synthase

1998

Tormay, P.; Wilting, R.; Lottspeich, F.; Mehta, P.K.; Christen, P.; Böck, A.

Eur. J. Biochem.

254

655-661

34525

4061824

Synthesis of L-selenodjenkolate and its degradation with methionine gamma-lyase

1985

Chocat, P.; Esaki, N.; Tanaka, H.; Soda, K.

Anal. Biochem.

148

485-489

34691

14692

Sulphur metabolism in Paracoccus denitrificans. Purification, properties and regulation of serine transacetylase, O-acetylserine sulphydrylase and beta-cystathionase

1977

Burnell, J.N.; Whatley, F.R.

Biochim. Biophys. Acta

481

246-265

286046

4092496

Selenomethionine-containing thiolase and 3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri

1985

Hartmanis, M.G.N.; Sliwkowski, M.X.

Curr. Top. Cell. Regul.

27

479-486

288217

713844

Formate dehydrogenase, a selenium-tungsten enzyme from Clostridium thermoaceticum

1970

Ljungdahl, L.G.; Andreesen, J.R.

Methods Enzymol.

53

360-372

288219

6822536

Purification and properties of NADP-dependent formate dehydrogenase from Clostridium thermoaceticum, a tungsten-selenium-iron protein

1983

Yamamoto, I.; Saiki, T.; Liu, S.M.; Ljungdahl, L.G.

J. Biol. Chem.

258

1826-1832

288220

6311213

Characterization and spectroscopic properties of reduced Mo and W formate dehydrogenase from C. thermoaceticum

1983

Durfor, C.N.; Wetherbee, P.J.

Biochem. Biophys. Res. Commun.

115

61-67

390369

6759195

Escherichia coli formate to nitrate respiratory pathway: structural analysis

1982

Boxer, D.; Malcolm, A.; Graham, A.

Biochem. Soc. Trans.

10

480-481

390482

10430865

Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine

1999

Dobbek, H.; Gremer, L.; Meyer, O.; Huber, R.

Proc. Natl. Acad. Sci. USA

96

8884-8889

393076

11929995

Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase

2002

Kryukov, G.V.; Kumar, R.A.; Koc, A.; Sun, Z.; Gladyshev, V.N.

Proc. Natl. Acad. Sci. USA

99

4245-4250

394864

3978121

The selenoenzyme phospholipid hydroperoxide glutathione peroxidase

1985

Ursini, F.; Maiorini, M.; Gregolin, C.

Biochim. Biophys. Acta

839

62-70

394867

2233312

Phospholipid hydroperoxide glutathione peroxidase

1990

Maiorino, M.; Gregolin, C.; Ursini, F.

Methods Enzymol.

186

448-457

394870

2386798

Enzymatic reduction of phospholipid and cholesterol hydroperoxides in artificial bilayers and lipoproteins

1990

Thomas, J.P.; Geiger, P.G.; Maiorino, M.; Ursini, F.; Girotti, A.W.

Biochim. Biophys. Acta

1045

252-260

394873

9915822

Selenoprotein P in human plasma as an extracellular phospholipid hydroperoxide glutathione peroxidase. Isolation and enzymatic characterization of human selenoprotein P

1999

Saito, Y.; Hayashi, T.; Tanaka, A.; Watanabe, Y.; Suzuki, M.; Saito, E.; Takahashi, K.

J. Biol. Chem.

274

2866-2871

394876

8436014

Purification of phospholipid hydroperoxide glutathione peroxidase from bovine retina

1993

Lam, K.W.; Wang, L.; Hong, B.S.; Treble, D.

Curr. Eye Res.

12

9-15

394877

11903656

Enzymatic and immunochemical evaluation of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in testes and epididymal spermatozoa of rats of different ages

2002

Tramer, F.; Micali, F.; Sandri, G.; Bertoni, A.; Lenzi, A.; Gandini, L.; Panfili, E.

Int. J. Androl.

25

72-83

394878

7851631

Purification of a cytosolic enzyme from human liver with phospholipid hydroperoxide glutathione peroxidase activity

1994

Chambers, S.J.; Lambert, N.; Williamson, G.

Int. J. Biochem.

26

1279-1286

394879

10910731

Bacterial and nonbacterial expression of wild-type and mutant human phospholipid hydroperoxide glutathione peroxidase and purification of the mutant enzyme in the milligram scale

2000

Schnurr, K.; Borchert, A.; Gerth, C.; Anton, M.; Kuhn, H.

Protein Expr. Purif.

19

403-410

394880

7524677

Purification and characterization of phospholipid hydroperoxide glutathione peroxidase from rat testis mitochondrial membranes

1994

Roveri, A.; Maiorino, M.; Nisii, C.; Ursini, F.

Biochim. Biophys. Acta

1208

211-221

394882

8706688

A selenium-containing phospholipid-hydroperoxide glutathione peroxidase in Schistosoma mansoni

1996

Maiorino, M.; Roche, C.; Kiess, M.; Koenig, K.; Gawlik, D.; Matthes, M.; Naldini, E.; Pierce, R.; Flohe, L.

Eur. J. Biochem.

238

838-844

395079

6211447

A selenium-containing hydrogenase from Methanococcus vannielii. Identification of the selenium moiety as a selenocysteine residue

1982

Yamazaki, S.

J. Biol. Chem.

257

7926-7929

395093

2738024

Purification and properties of the membrane-associated coenzyme F420-reducing hydrogenase from Methanobacterium formicicum

1989

Baron, S.F.; Ferry, J.G.

J. Bacteriol.

171

3846-3853

395567

6096145

Purification and properties of the soluble hydrogenase from Desulfovibrio desulfuricans (strain Norway 4)

1984

Rieder, R.; Cammack, R.; Hall, D.O.

Eur. J. Biochem.

145

637-643

395571

10606770

A sequential electron transfer from hydrogenases to cytochromes in sulfate-reducing bacteria

2000

Aubert, C.; Brugna, M.; Dolla, A.; Bruschi, M.; Giudici-Orticoni, M.T.

Biochim. Biophys. Acta

1476

85-92

396333

-

Nonheme iron dioxygenase

1974

Nozaki, M.

Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York

-

135-165

396416

6052430

Enzymic oxidation of cysteamine to hypotaurine in the absence of a cofactor

1967

Wood, J.L.; Cavallini, D.

Arch. Biochem. Biophys.

119

368-372

396417

5912113

The enzymatic oxidation of cysteamine to hypotaurine. Purification and properties of the enzyme

1966

Cavallini, D.; De Marco, C.; Scandurra, R.; Dupre, S.; Graziani, M.T.

J. Biol. Chem.

241

3189-3196

396603

4092495

The glutathione peroxidase reaction: molecular basis of the antioxidant function of selenium in mammals

1985

Flohe, L.

Curr. Top. Cell. Regul.

27

473-478

396604

4088069

Glutathione peroxidase

1985

Mannervik, B.

Methods Enzymol.

113

490-495

396605

6238814

Selenium-glutathione peroxidase: properties and synthesis

1984

Tappel, A.L.

Curr. Top. Cell. Regul.

24

87-96

396606

6094966

Oxidation states of glutathione peroxidase

1984

Ganther, H.E.; Kraus, R.J.

Methods Enzymol.

107

593-602

396613

537063

Structure analysis and molecular model of the selenoenzyme glutathione peroxidase at 2.8 A resolution

1979

Ladenstein, R.; Epp, O.; Bartels, K.; Jones, A.; Huber, R.

J. Mol. Biol.

134

199-218

396621

6714945

The amino-acid sequence of bovine glutathione peroxidase

1984

Gunzler, W.A.; Steffens, G.J.; Grossmann, A.; Kim, S.M.A.; Ítting, F.; Wendel, A.; Flohe, L.

Hoppe-Seyler's Z. Physiol. Chem.

365

195-212

396622

6852035

The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution

1983

Epp, O.; Ladenstein, R.; Wendel, A.

Eur. J. Biochem.

133

51-69

396627

-

The selenoprotein glutathione peroxidase

1989

Flohe, L.

Coenzymes and cofactors, Glutathione, Chem. Biochem. Med. Aspects Pt. A (Dolphin D, Poulson R, Avromonic O, eds. ) John Wiley & Sons, New York

-

643-731

396632

8428933

Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI

1993

Chu, F.F.; Doroshow, J.H.; Esworthy, R.S.

J. Biol. Chem.

268

2571-2576

396635

9030530

Subunit Ya-specific glutathione peroxidase activity toward cholesterol 7-hydroperoxides of glutathione S-transferases in cytosols from rat liver and skin

1997

Hiratsuka, A.; Yamane, H.; Yamazaki, S.; Ozawa, N.; Watabe, T.

J. Biol. Chem.

272

4763-4769

396639

8926102

Expression and characterization of glutathione peroxidase activity in the human blood fluke Schistosoma mansoni

1996

Mei, H.; Thakur, A.; Schwartz, J.; Lo Verde, P.T.

Infect. Immun.

64

4299-4306

396640

8193675

Purification and characterization of a glutathione peroxidase from the Aloe vera plant

1994

Sabeh, F.; Wright, T.; Norton, S.J.

Enzyme Protein

47

92-98

437685

10542172

Purification and characterization of (per)chlorate reductase from the chlorate-respiring strain GR-1

1999

Kengen, S.W.M.; Rikken, G.B.; Hagen, W.R.; Van Ginkel, C.G.; Stams, A.J.M.

J. Bacteriol.

181

6706-6711

439656

10378275

The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center

1999

Garcin, E.; Vernede, X.; Hatchikian, E.C.; Volbeda, A.; Frey, M.; Fontecilla-Camps, J.C.

Structure

7

557-566

644566

10491134

Selenium-containing xanthine dehydrogenase from Eubacterium barkeri

1999

Schräder, T.; Rienhöfer, A.; Andreesen, J.R.

Eur. J. Biochem.

264

862-871

644577

10860985

Selenium-dependent metabolism of purines: A selenium-dependent purine hydroxylase and xanthine dehydrogenase were purified from Clostridium purinolyticum and characterized

2000

Self, W.T.; Stadtman, T.C.

Proc. Natl. Acad. Sci. USA

97

7208-7213

644592

-

Purification and characterization of xanthine dehydrogenase from Clostridium acidiurici grown in the presence of selenium

1984

Wagner, R.; Cammack, R.; Andreesen, J.R.

Biochim. Biophys. Acta

791

63-74

645479

8144648

Selenophosphate synthetase. Enzyme properties and catalytic reaction

1994

Veres, Z.; Kim, I.Y.; Scholz, T.D.; Stadtman, T.C.

J. Biol. Chem.

269

10597-10603

645480

7520175

A purified selenophosphate-dependent enzyme from Salmonella typhimurium catalyzes the replacement of sulfur in 2-thiouridine residues in tRNAs with selenium

1994

Veres, Z.; Stadtman, T.C.

Proc. Natl. Acad. Sci. USA

91

8092-8096

645481

9482859

Isotope exchange studies on the Escherichia coli selenophosphate synthetase mechanism

1998

Walker, H.; Ferretti, J.A.; Stadtman, T.C.

Proc. Natl. Acad. Sci. USA

95

2180-2185

645482

1557403

Synthesis of 5-methylaminomethyl-2-selenouridine in tRNAs: 31P NMR studies show the labile selenium donor synthesized by the selD gene product contains selenium bonded to phosphorus

1992

Veres, Z.; Tsai, L.; Scholz, T.D.; Politino, M.; Balaban, R.S.; Stadtman, T.C

Proc. Natl. Acad. Sci. USA

89

2975-2979

645483

8041789

Effects of monovalent cations and divalent metal ions on Escherichia coli selenophosphate synthetase

1994

Kim, I.Y.; Stadtman, T.C.

Proc. Natl. Acad. Sci. USA

91:

7326-7329

645484

7644481

Selenophosphate synthetase: detection in extracts of rat tissues by immunoblot assay and partial purification of the enzyme from the archaeon Methanococcus vannielii

1995

Kim, I.Y.; Stadtman, T.C.

Proc. Natl. Acad. Sci. USA

92

7710-7713

645485

8262938

Biochemical analysis of Escherichia coli selenophosphate synthetase mutants

1993

Kim, I.Y.; Veres, Z.; Stadtman, T.C.

J. Biol. Chem.

268

27020-27025

645486

7665581

Cloning and functional characterization of human selenophosphate synthetase, an essential component of selenoprotein synthesis

1995

Low, S.C.; Harney, J.W.; Berry, M.J.

J. Biol. Chem.

270

21659-21664

645487

9012797

Fetal mouse selenophosphate synthetase 2 (SPS2): Characterization of the cysteine mutant form overproduced in a baculovirus-insect cell system

1997

Kim, I.Y.; Guimaraes, M.J.; Zlotnik, A.; Bazan, J.F.; Stadtman, T.C.

Proc. Natl. Acad. Sci. USA

94

418-421

645488

9169026

Selenophosphate synthetase: enzyme labeling studies with [gamma-32P]ATP, [beta-32P]ATP, [8-14C]ATP, and [75Se]selenide

1997

Liu, S.Y.; Stadtman, T.C.

Arch. Biochem. Biophys.

341

353-359

645489

9288401

A non-r4adioactive and two radioactive assays for selenophosphate synthetase activity

1997

Liu, S.Y.; Stadtman, T.C.

BioFactors

6

305-309

645490

9874769

Catalytic properties of selenophosphate synthetases: comparison of the selenocysteine-containing enzyme from Haemophilus influenzae with the corresponding cysteine-containing enzyme from Escherichia coli

1999

Lacourciere, G.M.; Stadtman, T.C.

Proc. Natl. Acad. Sci. USA

96

44-48

645491

-

Identification of a phosphorylated enzyme intermediate in the catalytic mechanism for selenophosphate synthetase

1997

Mullins, L.S.; Hong, S.B.; Gibson, G.E.; Walker, H.; Stadtman, T.C.; Raushel, F.M.

J. Am. Chem. Soc.

119

6684-6685

645492

8986768

Identification of a novel selD homolog from eukaryotes, bacteria, and archaea: Is there an autoregulatory mechanism in selenocysteine metabolism?

1996

Guimaraes, M.J.; Peterson, D.; Vicari, A.; Cocks, B.G.; Copeland, N.G.; Gilbert, D.J.; Jenkins, N.A.; Ferrick, D.A.; Kastelein, R.A.; Bazan, J.F.; Zlotnik, A.

Proc. Natl. Acad. Sci. USA

93

15086-15091

645493

11568451

The Drosophila selenophosphate synthetase (selD) gene is required for development and cell proliferation

2001

Serras, F.; Morey, M.; Alsina, B.; Baguna, J.; Corominas, M.

Biofactors

14

143-149

645494

12527370

Halving the selenophosphate synthetase gene dose confers hypersensitivity to oxidative stress in Drosophila melanogaster

2003

Morey, M.; Serras, F.; Corominas, M.

FEBS Lett.

534

111-114

645624

9812986

The NIFS protein can function as a selenide delivery protein in the biosynthesis of selenophosphate

1998

Lacourciere, G.M.; Stadtman, T.C.

J. Biol. Chem.

273

30921-30926

645630

11983074

Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: implications for its specificity toward selenocysteine

2002

Mihara, H.; Fujii, T.; Kato, S.; Kurihara, T.; Hata, Y.; Esaki, N.

J. Biochem.

131

679-685

645632

10739946

Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions

2000

Mihara, H.; Kurihara, T.; Yoshimura, T.; Esaki, N.

J. Biochem.

127

559-567

648740

6461656

Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine

1982

Esaki, N.; Nakamura, T.; Tanaka, H.; Soda, K.

J. Biol. Chem.

257

4386-4391

648741

2991201

Purification and characterization of selenocysteine beta-lyase from Citrobacter freundii

1985

Chocat, P.; Esaki, N.; Tanizawa, K.; Nakamura, T.; Tanaka, H.; Soda, K.

J. Bacteriol.

163

669-676

648742

3158280

Mechanism of reactions catalyzed by selenocysteine beta-lyase

1985

Esaki, N.; Karai, N.; Nakamura, T.; Tanaka, H.; Soda, K.

Arch. Biochem. Biophys.

238

418-423

648743

-

Selenocysteine beta-lyase from Citrobacter freundii

1987

Esaki, N.; Soda, K.

Methods Enzymol.

143

493-496

648744

2821348

Selenocysteine beta-lyase (porcine)

1987

Esaki, N.; Soda, K.

Methods Enzymol.

143

415-418

648745

1483038

Characterization of selenocysteine lyase in human tissues and its relationship to tissue selenium concentrations

1992

Daher, R.; Van Lente, F.

J. Trace Elem. Electrolytes Health Dis.

6

189-194

648746

10329673

A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. Gene cloning, purification, characterization and preliminary X-ray crystallographic studies

1999

Mihara, H.; Maeda, M.; Fujii, T.; Kurihara, T.; Hata, Y.; Esaki, N.

J. Biol. Chem.

274

14768-14772

648747

10692412

cDNA cloning, purification, and characterization of mouse liver selenocysteine lyase. Candidate for selenium delivery protein in selenoprotein synthesis

2000

Mihara, H.; Kurihara, T.; Watanabe, T.; Yoshimura, T.; Esaki, N.

J. Biol. Chem.

275

6195-6200

648748

10684605

Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase

2000

Fujii, T.; Maeda, M.; Mihara, H.; Kurihara, T.; Esaki, N.; Hata, Y.

Biochemistry

39

1263-1273

648750

11898407

Selenocysteine lyase from mouse liver

2002

Mihara, H.; Esaki, N.

Methods Enzymol.

347

198-203

648751

-

Expression of a mouse selenocysteine lyase in Brassica juncea chloroplasts affects selenium tolerance and accumulation

2003

Garifullina, G.F.; Owen, J.D.; Lindblom, S.D.; Tufan, H.; Pilon, M.; Pilon-Smits, E.A.H.

Physiol. Plant.

118

538-544

648753

12644675

Enhanced selenium tolerance and accumulation in transgenic Arabidopsis expressing a mouse selenocysteine lyase

2003

Pilon, M.; Owen, J.D.; Garifullina, G.F.; Kurihara, T.; Mihara, H.; Esaki, N.; Pilon-Smits, E.A.

Plant Physiol.

131

1250-1257

656481

10966817

The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase

2000

Hanzelmann, P.; Dobbek, H.; Gremer, L.; Huber, R.; Meyer, O.

J. Mol. Biol.

301

1221-1235

657735

12615078

Oxidant stress enhances Lyso-PAF-AcT activity by modifying phospholipase D and phosphatidic acid in aortic endothelial cells

2003

Corl, C.M.; Cao, Y.Z.; Cohen, Z.S.; Sordillo, L.M.

Biochem. Biophys. Res. Commun.

302

610-614

658212

15680228

Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage

2005

Weissbach, H.; Resnick, L.; Brot, N.

Biochim. Biophys. Acta

1703

203-212

658247

12193409

Male fertility is linked to the selenoprotein phospholipid hydroperoxide glutathione peroxidase

2002

Foresta, C.; Flohe, L.; Garolla, A.; Roveri, A.; Ursini, F.; Maiorino, M.

Biol. Reprod.

67

967-971

658556

11108274

The role of selenocysteine 133 in catalysis by the human type 2 iodothyronine deiodinase

2000

Buettner, C.; Harney, J.W.; Larsen, P.R.

Endocrinology

141

4606-4612

658557

11897672

Substitution of cysteine for a conserved alanine residue in the catalytic center of type II iodothyronine deiodinase alters interaction with reducing cofactor

2002

Kuiper, G.G.; Klootwijk, W.; Visser, T.J.

Endocrinology

143

1190-1198

658704

12220640

Activity, tissue distribution and site-directed mutagenesis of a human peptide methionine sulfoxide reductase of type B: hCBS1

2002

Jung, S.; Hansel, A.; Kasperczyk, H.; Hoshi, T.; Heinemann, S.H.

FEBS Lett.

527

91-94

658758

15670826

Primary structure of the nuclear forms of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat spermatozoa

2005

Maiorino, M.; Mauri, P.; Roveri, A.; Benazzi, L.; Toppo, S.; Bosello, V.; Ursini, F.

FEBS Lett.

579

667-670

658760

15670839

The conserved histidine 106 of large thioredoxin reductases is likely to have a structural role but not a base catalyst function

2005

Jacob, J.; Schirmer, R.H.; Gromer, S.

FEBS Lett.

579

745-748

658794

15110392

Human mitochondrial thioredoxin reductase reduces cytochrome c and confers resistance to complex III inhibition

2004

Nalvarte, I.; Damdimopoulos, A.E.; Spyrou, G.

Free Radic. Biol. Med.

36

1270-1278

658795

14980707

Evidence for intriguingly complex transcription of human thioredoxin reductase 1

2004

Rundlof, A.K.; Janard, M.; Miranda-Vizuete, A.; Arner, E.S.J.

Free Radic. Biol. Med.

36

641-656

658896

12635692

In vivo inhibition of selenium dependent glutathione peroxidase and superoxide dismutase in rats by diethyldithiocarbamate

2002

Prabhu, H.R.

Indian J. Exp. Biol.

40

258-261

658902

14730999

X-ray absorption spectroscopy of selenate reductase

2004

Maher, M.J.; Santini, J.; Pickering, I.J.; Prince, R.C.; Macy, J.M.; George, G.N.

Inorg. Chem.

43

402-404

659012

11889113

Regulation of purine hydroxylase and xanthine dehydrogenase from Clostridium purinolyticum in response to purines, selenium, and molybdenum

2002

Self, W.T.

J. Bacteriol.

184

2039-2044

659156

11425850

The human type 2 iodothyronine deiodinase is a selenoprotein highly expressed in a mesothelioma cell line

2001

Curcio, C.; Baqui, M.M.; Salvatore, D.; Rihn, B.H.; Mohr, S.; Harney, J.W.; Larsen, P.R.; Bianco, A.C.

J. Biol. Chem.

276

30183-30187

659211

12435734

The mammalian cytosolic selenoenzyme thioredoxin reductase reduces ubiquinone. A novel mechanism for defense against oxidative stress

2003

Xia, L.; Nordman, T.; Olsson, J.M.; Damdimopoulos, A.; Bjorkhem-Bergman, L.; Nalvarte, I.; Eriksson, L.C.; Arner, E.S.; Spyrou, G.; Bjornstedt, M.

J. Biol. Chem.

278

2141-2146

659484

15901730

Mammalian selenoprotein thioredoxin/glutathione reductase: roles in disulfide bond formation and sperm maturation

2005

Su, D.; Novoselov, S.V.; Sun, Q.A.; Moustafa, M.E.; Zhou, Y.; Oko, R.; Hatfield, D.L.; Gladyshev, V.N.

J. Biol. Chem.

280

26491-26498

659569

12629133

Type 3 iodothyronine deiodinase is highly expressed in the human uteroplacental unit and in fetal epithelium

2003

Huang, S.A.; Dorfman, D.M.; Genest, D.R.; Salvatore, D.; Larsen, P.R.

J. Clin. Endocrinol. Metab.

88

1384-1388

659748

15956354

Expression of recombinant membrane-bound type I iodothyronine deiodinase in yeast

2005

Kuiper, G.G.; Klootwijk, W.; Visser, T.J.

J. Mol. Endocrinol.

34

865-878

659779

15165039

Purification, characterization, and immunolocalization of a thioredoxin reductase from adult

2004

Maggioli, G.; Piacenza, L.; Carambula, B.; Carmona, C.

J. Parasitol.

90

205-211

659902

14668013

Purification, characterization and kinetic properties of the multifunctional thioredoxin-glutathione reductase from Taenia crassiceps metacestode (cysticerci)

2004

Rendon, J.L.; del Arenal, I.P.; Guevara-Flores, A.; Uribe, A.; Plancarte, A.; Mendoza-Hernandez, G.

Mol. Biochem. Parasitol.

133

61-69

660881

15358220

Expression of selenocysteine-containing glutathione S-transferase in Escherichia coli

2004

Jiang, Z.; Arner, E.S.J.; Mu, Y.; Johansson, L.; Shi, J.; Zhao, S.; Liu, S.; Wang, R.; Zhang, T.; Yan, G.; Liu, J.; Shen, J.; Luo, G.

Biochem. Biophys. Res. Commun.

321

94-101

662872

10515607

Fetal mouse selenophosphate synthetase 2 (SPS2): biological activities of mutant forms in Escherichia coli

1999

Kim, T.S.; Yu, M.H.; Chung, Y.W.; Kim, J.; Choi, E.J.; Ahn, K.; Kim, I.Y.

Mol. Cells

9

422-428

663220

15534230

Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling L-selenocysteine and Sps2 for selenite assimilation

2004

Tamura, T.; Yamamoto, S.; Takahata, M.; Sakaguchi, H.; Tanaka, H.; Stadtman, T.C.; Inagaki, K.

Proc. Natl. Acad. Sci. USA

101

16162-16167

671895

17346238

Selenophosphate synthetase 2 is essential for selenoprotein biosynthesis

2007

Xu, X.M.; Carlson, B.A.; Irons, R.; Mix, H.; Zhong, N.; Gladyshev, V.N.; Hatfield, D.L.

Biochem. J.

404

115-120

673172

16945589

Identification, sequencing and expression of selenium-dependent glutathione peroxidase transcript in the freshwater bivalve Unio tumidus exposed to Aroclor 1254

2006

Doyen, P.; Vasseur, P.; Rodius, F.

Comp. Biochem. Physiol. C

144

122-129

673807

17015273

Selenoprotein P protects endothelial cells from oxidative damage by stimulation of glutathione peroxidase expression and activity

2006

Steinbrenner, H.; Bilgic, E.; Alili, L.; Sies, H.; Brenneisen, P.

Free Radic. Res.

40

936-943

674008

16291093

Molecular cloning of a phospholipid-hydroperoxide glutathione peroxidase gene from the tick, Boophilus microplus (Acari: Ixodidae)

2005

Cossio-Bayugar, R.; Miranda, E.; Holman, P.J.

Insect Biochem. Mol. Biol.

35

1378-1387

674919

16187073

Hydrogenases in Desulfovibrio vulgaris Hildenborough: structural and physiologic characterisation of the membrane-bound [NiFeSe] hydrogenase

2005

Valente, F.M.; Oliveira, A.S.; Gnadt, N.; Pacheco, I.; Coelho, A.V.; Xavier, A.V.; Teixeira, M.; Soares, C.M.; Pereira, I.A.

J. Biol. Inorg. Chem.

10

667-682

674932

16830149

Formate-reduced E. coli formate dehydrogenase H: The reinterpretation of the crystal structure suggests a new reaction mechanism

2006

Raaijmakers, H.C.; Romao, M.J.

J. Biol. Inorg. Chem.

11

849-854

675033

16786570

p53-mediated enhancement of radiosensitivity by selenophosphate synthetase 1 overexpression

2006

Chung, H.J.; Yoon, S.I.; Shin, S.H.; Koh, Y.A.; Lee, S.J.; Lee, Y.S.; Bae, S.

J. Cell. Physiol.

209

131-141

675564

16857846

Hemolysate thioredoxin reductase and glutathione peroxidase activities correlate with serum selenium in a group of New Zealand men at high prostate cancer risk

2006

Karunasinghe, N.; Ferguson, L.R.; Tuckey, J.; Masters, J.

J. Nutr.

136

2232-2235

675758

17052796

Effects of selenium supplementation on expression of glutathione peroxidase isoforms in cultured human lung adenocarcinoma cell lines

2007

Romanowska, M.; Kikawa, K.D.; Fields, J.R.; Maciag, A.; North, S.L.; Shiao, Y.H.; Kasprzak, K.S.; Anderson, L.M.

Lung Cancer

55

35-42

675895

17611817

Cloning and functional characterization of an O-acetylserine(thiol)lyase-encoding gene in wild soybean (Glycine soja)

2008

Zhang, C.; Meng, Q.; Gai, J.; Yu, D.

Mol. Biol. Rep.

35

527-534

675915

16546977

Molecular pharmacology and antitumor activity of palmarumycin-based inhibitors of thioredoxin reductase

2006

Powis, G.; Wipf, P.; Lynch, S.M.; Birmingham, A.; Kirkpatrick, D.L.

Mol. Cancer Ther.

5

630-636

675985

16427183

The antioxidant glutathione peroxidase family and spermatozoa: a complex story

2006

Drevet, J.R.

Mol. Cell. Endocrinol.

250

70-79

676338

16403846

mRNA expression in mouse hypothalamus and basal forebrain during influenza infection: a novel model for sleep regulation

2006

Ding, M.; Toth, L.A.

Physiol. Genomics

24

225-234

677190

15955363

Activity, substrate detection and immunolocalization of glutathione peroxidase (GPx) in bovine reproductive organs and semen

2005

Vaisberg, C.N.; Jelezarsky, L.V.; Dishlianova, B.; Chaushev, T.A.

Theriogenology

64

416-428

684392

17437091

Multitechnique mass-spectrometric approach for the detection of bovine glutathione peroxidase selenoprotein: focus on the selenopeptide

2007

Ballihaut, G.; Mounicou, S.; Lobinski, R.

Anal. Bioanal. Chem.

388

585-591

684496

18498225

Evolutionary and structural insights into the multifaceted glutathione peroxidase (Gpx) superfamily

2008

Toppo, S.; Vanin, S.; Bosello, V.; Tosatto, S.C.

Antioxid. Redox Signal.

10

1501-1514

684671

17291446

Differential regulation of expression of cytosolic and mitochondrial thioredoxin reductase in rat liver and kidney

2007

Crosley, L.K.; Meplan, C.; Nicol, F.; Rundloef, A.K.; Arner, E.S.; Hesketh, J.E.; Arthur, J.R.

Arch. Biochem. Biophys.

459

178-188

684729

18722338

An anaerobic bacterial MsrB model reveals catalytic mechanisms, advantages, and disadvantages provided by selenocysteine and cysteine in reduction of methionine-R-sulfoxide

2008

Lee, T.H.; Kim, H.Y.

Arch. Biochem. Biophys.

478

175-180

684809

17651309

Effect of lead acetate on cytosolic thioredoxin reductase activity and oxidative stress parameters in rat kidneys

2007

Conterato, G.M.; Augusti, P.R.; Somacal, S.; Einsfeld, L.; Sobieski, R.; Torres, J.R.; Emanuelli, T.

Basic Clin. Pharmacol. Toxicol.

101

96-100

684984

17922679

Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals

2007

Kim, H.Y.; Gladyshev, V.N.

Biochem. J.

407

321-329

685333

17714875

Sperm nuclei glutathione peroxidases and their occurrence in animal species with cysteine-containing protamines

2007

Bertelsmann, H.; Kuehbacher, M.; Weseloh, G.; Kyriakopoulos, A.; Behne, D.

Biochim. Biophys. Acta

1770

1459-1467

685439

17937614

Molecular biology of glutathione peroxidase 4: from genomic structure to developmental expression and neural function

2007

Savaskan, N.E.; Ufer, C.; Kuehn, H.; Borchert, A.

Biol. Chem.

388

1007-1017

685445

17937623

Effect of selenium on thioredoxin reductase activity in Txnrd1 or Txnrd2 hemizygous mice

2007

Kiermayer, C.; Michalke, B.; Schmidt, J.; Brielmeier, M.

Biol. Chem.

388

1091-1097

685479

17625247

Specific activity of methionine sulfoxide reductase in CD-1 mice is significantly affected by dietary selenium but not zinc

2007

Uthus, E.O.; Moskovitz, J.

Biol. Trace Elem. Res.

115

265-276

685921

17993721

Activity of the glutathione peroxidase-2. Differences in the selenium-dependent expression between colon and small intestine

2007

Bartel, J.; Bartz, T.; Wolf, C.; Charkiewicz, E.; Kuhbacher, M.; Pohl, T.; Kyriakopoulos, A.

Cancer Genomics Proteomics

4

369-372

686324

17316382

Quantification of alternative mRNA species and identification of thioredoxin reductase 1 isoforms in human tumor cells

2007

Rundloef, A.; Fernandes, A.P.; Selenius, M.; Babic, M.; Shariatgorji, M.; Nilsonne, G.; Ilag, L.L.; Dobra, K.; Bjoernstedt, M.

Differentiation

75

123-132

687123

18373941

A novel selenium-containing glutathione transferase zeta1-1, the activity of which surpasses the level of some native glutathione peroxidases

2008

Zheng, K.; Board, P.G.; Fei, X.; Sun, Y.; Lv, S.; Yan, G.; Liu, J.; Shen, J.; Luo, G.

Int. J. Biochem. Cell Biol.

40

2090-2097

687454

18182386

Selenite assimilation into formate dehydrogenase H depends on thioredoxin reductase in Escherichia coli

2008

Takahata, M.; Tamura, T.; Abe, K.; Mihara, H.; Kurokawa, S.; Yamamoto, Y.; Nakano, R.; Esaki, N.; Inagaki, K.

J. Biochem.

143

467-473

687730

18408002

Platyhelminth mitochondrial and cytosolic redox homeostasis is controlled by a single thioredoxin glutathione reductase and dependent on selenium and glutathione

2008

Bonilla, M.; Denicola, A.; Novoselov, S.V.; Turanov, A.A.; Protasio, A.; Izmendi, D.; Gladyshev, V.N.; Salinas, G.

J. Biol. Chem.

283

17898-17907

688886

11985869

The disulfide redox system of Schistosoma mansoni and the importance of a multifunctional enzyme, thioredoxin glutathione reductase

2002

Alger, H.M.; Williams, D.L.

Mol. Biochem. Parasitol.

121

129-139

689708

17971875

Targeting thioredoxin reductase 1 reduction in cancer cells inhibits self-sufficient growth and DNA replication

2007

Yoo, M.H.; Xu, X.M.; Carlson, B.A.; Patterson, A.D.; Gladyshev, V.N.; Hatfield, D.L.

PLoS ONE

2

e1112

690043

17558897

Elevated plasma glutathione peroxidase concentration in acute severe asthma: comparison with plasma glutathione peroxidase activity, selenium and malondialdehyde

2007

Jacobson, G.A.; Yee, K.C.; Ng, C.H.

Scand. J. Clin. Lab. Invest.

67

423-430

690120

17964641

Localization and characterization of glutathione peroxidase (GPx) in boar accessory sex glands, seminal plasma, and spermatozoa and activity of GPx in boar semen

2008

Jelezarsky, L.; Vaisberg, C.h.; Chaushev, T.; Sapundjiev, E.

Theriogenology

69

139-145

690290

18540050

Structure of an N-terminally truncated selenophosphate synthetase from Aquifex aeolicus

2008

Matsumoto, E.; Sekine, S.; Akasaka, R.; Otta, Y.; Katsura, K.; Inoue, M.; Kaminishi, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.

Acta Crystallogr. Sect. F

F64

453-458

691179

17916946

New developments in selenium biochemistry: selenocysteine biosynthesis in eukaryotes and archaea

2007

Xu, X.M.; Carlson, B.A.; Zhang, Y.; Mix, H.; Kryukov, G.V.; Glass, R.S.; Berry, M.J.; Gladyshev, V.N.; Hatfield, D.L.

Biol. Trace Elem. Res.

119

234-241

691196

-

Functional analysis of two homologous mouse selenophosphate synthetases

2008

Abe, K.; Mihara, H.; Nishijima, Y.; Kurokawa, S.; Esaki, N.

Biomed. Res. Trace Elem.

19

76-79

691493

18510720

In silico identification of genes involved in selenium metabolism: evidence for a third selenium utilization trait

2008

Zhang, Y.; Turanov, A.A.; Hatfield, D.L.; Gladyshev, V.N.

BMC Genomics

9

251

693677

18773910

Structure of selenophosphate synthetase essential for selenium incorporation into proteins and RNAs

2008

Itoh, Y.; Sekine, S.I.; Matsumoto, E.; Akasaka, R.; Takemoto, C.; Shirouzu, M.; Yokoyama, S.

J. Mol. Biol.

385

1456-1469

694071

18812192

Selenocysteine incorporation in kinetoplastid: selenophosphate synthetase (SELD) from Leishmania major and Trypanosoma brucei

2008

Sculaccio, S.A.; Rodrigues, E.M.; Cordeiro, A.T.; Magalhaes, A.; Braga, A.L.; Alberto, E.E.; Thiemann, O.H.

Mol. Biochem. Parasitol.

162

165-171

694096

17712607

Active bovine selenophosphate synthetase 2, not having selenocysteine

2007

Furumiya, K.; Kanaya, K.; Tanabe, K.; Tanaka, Y.; Mizutani, T.

Mol. Biol. Rep.

35

541-549

694794

-

Biosynthesis of selenocysteine on its tRNA in eukaryotes

2007

Xu, X.; Carlson, B.A.; Mix, H.; Zhang, Y.; Saira, K.; Glass, R.S.; Berry, M.J.; Gladyshev, V.N.; Hatfield, D.L.

PLoS Biol.

5

96-105

695650

7747941

The hydrogenases and formate dehydrogenases of Escherichia coli

1994

Sawers, G.

Antonie van Leeuwenhoek

66

57-88

696173

19538123

Enzymatic properties of a recombinant phospholipid hydroperoxide glutathione peroxidase from Momordica charantia and its complementation function in yeast

2009

Dong, C.J.; Yang, X.D.; Liu, J.Y.

Biochemistry (Moscow)

74

502-508

696191

9521673

Selenium-containing formate dehydrogenase H from Escherichia coli: A molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer

1998

Khangulov, S.V.; Gladyshev, V.N.; Dismukes, G.C.; Stadtman, T.C.

Biochemistry

37

3518-3528

696235

18986163

Selenium in thioredoxin reductase: a mechanistic perspective

2008

Lacey, B.M.; Eckenroth, B.E.; Flemer, S.; Hondal, R.J.

Biochemistry

47

12810-12821

696435

19433132

Transgenic mouse models for the vital selenoenzymes cytosolic thioredoxin reductase, mitochondrial thioredoxin reductase and glutathione peroxidase 4

2009

Conrad, M.

Biochim. Biophys. Acta

1790

1575-1585

696439

19364476

Focus on mammalian thioredoxin reductases--important selenoproteins with versatile functions

2009

Arner, E.S.

Biochim. Biophys. Acta

1790

495-526

696560

19182374

Effects of selenium deficiency on aldehyde oxidase 1 in rats

2009

Itoh, K.; Adachi, M.; Sato, J.; Shouji, K.; Fukiya, K.; Fujii, K.; Tanaka, Y.

Biol. Pharm. Bull.

32

190-194

696578

18227976

Selenium induces manganese-dependent peroxidase production by the white-rot fungus Bjerkandera adusta (Willdenow) P. Karsten

2008

Catal, T.; Liu, H.; Bermek, H.

Biol. Trace Elem. Res.

123

211-217

696580

18972070

Differential effects of sodium selenite and nano-Se on growth performance, tissue Se distribution, and glutathione peroxidase activity of avian broiler

2009

Wang, Y.

Biol. Trace Elem. Res.

128

184-190

697468

19808099

Molecular characterization of a phospholipid-hydroperoxide glutathione peroxidase from the bumblebee Bombus ignitus

2010

Hu, Z.; Lee, K.S.; Choo, Y.M.; Yoon, H.J.; Kim, I.; Wei, Y.D.; Gui, Z.Z.; Zhang, G.Z.; Sohn, H.D.; Jin, B.R.

Comp. Biochem. Physiol. B

155

54-61

697470

19345279

Identification of two phospholipid hydroperoxide glutathione peroxidase (gpx4) genes in common carp

2009

Hermesz, E.; Ferencz, A.

Comp. Biochem. Physiol. C

150

101-106

698045

18215741

Suppression of atherogenesis by overexpression of glutathione peroxidase-4 in apolipoprotein E-deficient mice

2008

Guo, Z.; Ran, Q.; Roberts, L.J.; Zhou, L.; Richardson, A.; Sharan, C.; Wu, D.; Yang, H.

Free Radic. Biol. Med.

44

343-352

698053

19146949

Highly active dimeric and low-activity tetrameric forms of selenium-containing rat thioredoxin reductase 1

2009

Rengby, O.; Cheng, Q.; Vahter, M.; Joernvall, H.; Arner, E.S.

Free Radic. Biol. Med.

46

893-904

698681

1099093

The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli

1975

Enoch, H.G.; Lester, R.L.

J. Biol. Chem.

250

6693-7705

698686

2211698

Escherichia coli formate-hydrogen lyase. Purification and properties of the selenium-dependent formate dehydrogenase component

1990

Axley, M.J.; Grahame, D.A.; Stadtman, T.C.

J. Biol. Chem.

265

18213-18218

698689

1834670

Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. II. Evidence that a mRNA stem-loop structure is essential for decoding opal (UGA) as selenocysteine

1991

Berg, B.L.; Baron, C.; Stewart, V.

J. Biol. Chem.

266

22386-22391

698704

8626495

Characterization of crystalline formate dehydrogenase H from Escherichia coli

1996

Gladyshev, V.N.; Boyington, J.C.; Khangulov, S.V.; Grahame, D.A.; Stadtman, T.C.; Sun, P.D.

J. Biol. Chem.

271

8095-8100

698965

19054767

Crystal structure and catalysis of the selenoprotein thioredoxin reductase 1

2009

Cheng, Q.; Sandalova, T.; Lindqvist, Y.; Arner, E.S.

J. Biol. Chem.

284

3998-4008

700072

19733578

Aging decreases expression and activity of glutathione peroxidase-1 in human endothelial progenitor cells

2009

He, T.; Joyner, M.J.; Katusic, Z.S.

Microvasc. Res.

78

447-452

700153

18426912

Hepatocyte nuclear factor 4alpha contributes to thyroid hormone homeostasis by cooperatively regulating the type 1 iodothyronine deiodinase gene with GATA4 and Kruppel-like transcription factor 9

2008

Ohguchi, H.; Tanaka, T.; Uchida, A.; Magoori, K.; Kudo, H.; Kim, I.; Daigo, K.; Sakakibara, I.; Okamura, M.; Harigae, H.; Sasaki, T.; Osborne, T.F.; Gonzalez, F.J.; Hamakubo, T.; Kodama, T.; Sakai, J.

Mol. Cell. Biol.

28

3917-3931

700262

1533438

Overproduction of a selenocysteine-containing polypeptide in Escherichia coli: the fdhFgene product

1992

Chen, G.T.; Axley, M.J.; Hacia, J.; Inouye, M.

Mol. Microbiol.

6

781-785

701021

2941757

Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli

1986

Zinoni, F.; Birkmann, A.; Stadtman, T.C.; Böck, A.

Proc. Natl. Acad. Sci. USA

83

4650-4654

701023

1924303

Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium

1991

Axley, M.J.; Böck, A.; Stadtman, T.C.

Proc. Natl. Acad. Sci. USA

88

8450-8454

701024

8052647

Coordination of selenium to molybdenum in formate dehydrogenase H from Escherichia coli

1994

Gladyshev, V.N.; Khangulov, S.V.; Axley, M.J.; Stadtman, T.C.

Proc. Natl. Acad. Sci. USA

91

7708-7711

701039

19623542

Correlation between selenium concentrations and glutathione peroxidase activity in serum and human prostate tissue

2009

Takata, Y.; Morris, J.S.; King, I.B.; Kristal, A.R.; Lin, D.W.; Peters, U.

Prostate

69

1635-1642

701130

18767149

The selenoproteome of Clostridium sp. OhILAs: characterization of anaerobic bacterial selenoprotein methionine sulfoxide reductase A

2009

Kim, H.Y.; Zhang, Y.; Lee, B.C.; Kim, J.R.; Gladyshev, V.N.

Proteins

74

1008-1017

701138

19714775

Combining crystallography and molecular dynamics: The case of Schistosoma mansoni phospholipid glutathione peroxidase

2009

Dimastrogiovanni, D.; Anselmi, M.; Miele, A.E.; Boumis, G.; Petersson, L.; Angelucci, F.; Nola, A.D.; Brunori, M.; Bellelli, A.

Proteins

78

259-270

701272

19345404

Phospholipid hydroperoxide glutathione peroxidase in bull spermatozoa provides a unique marker in the quest for semen quality analysis

2009

Stradaioli, G.; Sylla, L.; Monaci, M.; Maiorino, M.

Theriogenology

72

91-98

701298

19534619

Disturbed expression of type 1 iodothyronine deiodinase splice variants in human renal cancer

2009

Piekielko-Witkowska, A.; Master, A.; Wojcicka, A.; Boguslawska, J.; Brozda, I.; Tanski, Z.; Nauman, A.

Thyroid

19

1105-1113

702092

19944066

O-GlcNAcylation regulates hyperglycemia-induced GPX1 activation

2010

Yang, W.H.; Park, S.Y.; Ji, S.; Kang, J.G.; Kim, J.-E.; Song, H.; Mook-Jung, I.; Choe, K.-M.; Cho, J.W.

Biochem. Biophys. Res. Commun.

391

756-761

702181

19817692

Binding of ATP and its derivatives to selenophosphate synthetase from Escherichia coli

2009

Preabrazhenskaya, Y.V.; Kim, I.Y.; Stadtman, T.C.

Biochemistry (Moscow)

74

910-916

704162

18781742

The difference a Se makes? Oxygen-tolerant hydrogen production by the [NiFeSe]-hydrogenase from Desulfomicrobium baculatum

2008

Parkin, A.; Goldet, G.; Cavazza, C.; Fontecilla-Camps, J.C.; Armstrong, F.A.

J. Am. Chem. Soc.

130

13410-13416

705151

19477186

Crystal structures of catalytic intermediates of human selenophosphate synthetase 1

2009

Wang, K.T.; Wang, J.; Li, L.F.; Su, X.D.

J. Mol. Biol.

390

747-759

710835

20397034

Differing views of the role of selenium in thioredoxin reductase

2011

Hondal, R.J.; Ruggles, E.L.

Amino Acids

41

73-89

710848

20167203

Determination of the specific activities of methionine sulfoxide reductase A and B by capillary electrophoresis

2010

Uthus, E.O.

Anal. Biochem.

401

68-73

711101

20494123

Thioredoxin and thioredoxin reductase: current research with special reference to human disease

2010

Holmgren, A.; Lu, J.

Biochem. Biophys. Res. Commun.

396

120-124

711146

20536427

Mammalian thioredoxin reductase 1: roles in redox homoeostasis and characterization of cellular targets

2010

Turanov, A.A.; Kehr, S.; Marino, S.M.; Yoo, M.H.; Carlson, B.A.; Hatfield, D.L.; Gladyshev, V.N.

Biochem. J.

430

285-293

713184

20495929

Substrate specificity of the mitochondrial thioredoxin reductase of the parasitic nematode Haemonchus contortus

2010

Hudson, A.L.; Sotirchos, I.M.; Davey, M.W.

Parasitol. Res.

107

487-493

715377

21257770

A selenium-dependent xanthine dehydrogenase triggers biofilm proliferation in Enterococcus faecalis through oxidant production

2011

Srivastava, M.; Mallard, C.; Barke, T.; Hancock, L.E.; Self, W.T.

J. Bacteriol.

193

1643-1652

716049

-

Radiometric enzyme assays: development of methods for extremely sensitive determination of types 1, 2 and 3 iodothyronine deiodinase enzyme activities

2010

Pavelka, S.

J. Radioanal. Nucl. Chem.

286

861-865

720145

-

Steady-state fluorescence properties of S. solfataricus alcohol dehydrogenase and its selenomethionyl derivative

2003

Giordano, A.; Raia, C.A.

J. Fluoresc.

13

17-24

720330

15253444

Highly UV-absorbing complex in selenomethionine-substituted alcohol dehydrogenase from Sulfolobus solfataricus

2004

Giordano, A.; Russo, C.; Raia, C.A.; Kuznetsova, I.M.; Stepanenko, O.V.; Turoverov, K.K.

J. Proteome Res.

3

613-620

721940

21864351

Drosophila selenophosphate synthetase 1 regulates vitamin B6 metabolism: prediction and confirmation

2011

Lee, K.H.; Shim, M.S.; Kim, J.Y.; Jung, H.K.; Lee, E.; Carlson, B.A.; Xu, X.M.; Park, J.M.; Hatfield, D.L.; Park, T.; Lee, B.J.

BMC Genomics

12

426

722096

21664929

Identification and cloning of a selenophosphate synthetase (SPS) from tiger shrimp, Penaeus monodon, and its transcription in relation to molt stages and following pathogen infection

2012

Yeh, M.S.; Huang, C.J.; Guo, C.H.; Liu, K.F.; Tsai, I.H.; Cheng, W.

Dev. Comp. Immunol.

36

21-30

722547

22081394

Structural insights into the catalytic mechanism of Escherichia coli selenophosphate synthetase

2012

Noinaj, N.; Wattanasak, R.; Lee, D.Y.; Wally, J.L.; Piszczek, G.; Chock, P.B.; Stadtman, T.C.; Buchanan, S.K.

J. Bacteriol.

194

499-508

723898

-

Enhanced glutathione peroxidases (GPx) activity in young barley seedlings enriched with selenium

2011

Liu, K.; Zhao, Y.; Chen, F.; Gu, Z.; Bu, G.

Afr. J. Biotechnol.

10

11483-11487

724798

21983335

Identification and mRNA expression of pi-class glutathione S-transferase and selenium-dependent glutathione peroxidase in the gudgeon Gobio gobio exposed to PCB 77

2012

Doyen, P.; Rodius, F.; Lhoste, L.; Hoffmann, L.; Cauchie, H.M.

Comp. Biochem. Physiol. C

155

300-306

725048

21821133

Transcriptional regulation of selenium-dependent glutathione peroxidase from Venerupis philippinarum in response to pathogen and contaminants challenge

2011

Zhang, L.; Liu, X.; Chen, L.; You, L.; Pei, D.; Cong, M.; Zhao, J.; Li, C.; Liu, D.; Yu, J.; Wu, H.

Fish Shellfish Immunol.

31

831-837

725392

20178978

Kinetic and spectroscopic studies of the molybdenum-copper CO dehydrogenase from Oligotropha carboxidovorans

2010

Zhang, B.; Hemann, C.F.; Hille, R.

J. Biol. Chem.

285

12571-12578

727803

7451465

Selenium-dependent and selenium-independent formate dehydrogenases of Methanococcus vannielii. Separation of the two forms and characterization of the purified selenium-independent form

1981

Jones, J.B.; Stadtman, T.C.

J. Biol. Chem.

256

656-663

728320

19919669

In vivo requirement of selenophosphate for selenoprotein synthesis in archaea

2010

Stock, T.; Selzer, M.; Rother, M.

Mol. Microbiol.

75

149-160

736397

10636886

Binding of flavin adenine dinucleotide to molybdenum-containing carbon monoxide dehydrogenase from Oligotropha carboxidovorans. Structural and functional analysis of a carbon monoxide dehydrogenase species in which the native flavoprotein has been replaced by its recombinant counterpart produced in Escherichia coli

2000

Gremer, L.; Kellner, S.; Dobbek, H.; Huber, R.; Meyer, O.

J. Biol. Chem.

275

1864-1872

737371

23908029

Crystallization and preliminary X-ray diffraction analysis of selenophosphate synthetases from Trypanosoma brucei and Leishmania major

2013

Faim, L.M.; Rosa e Silva, I.; Bertacine Dias, M.V.; DMuniz Pereira, H.; Brandao-Neto, J.; Alves da Silva, M.T.; Thiemann, O.H.

Acta Crystallogr. Sect. F

69

864-867

737653

27208177

Selenophosphate synthetase 1 is an essential protein with roles in regulation of redox homoeostasis in mammals

2016

Tobe, R.; Carlson, B.A.; Huh, J.H.; Castro, N.P.; Xu, X.M.; Tsuji, P.A.; Lee, S.G.; Bang, J.; Na, J.W.; Kong, Y.Y.; Beaglehole, D.; Southon, E.; Seifried, H.; Tessarollo, L.; Salomon, D.S.; Schweizer, U.; Gladyshev, V.N.; Hatfield, D.L.; Lee, B.J.

Biochem. J.

473

2141-2154

737876

27405844

A non-radioactive assay for selenophosphate synthetase activity using recombinant pyruvate pyrophosphate dikinase from Thermus thermophilus HB8

2016

Kamada, S.; Okugochi, T.; Asano, K.; Tobe, R.; Mihara, H.; Nemoto, M.; Inagaki, K.; Tamura, T.

Biosci. Biotechnol. Biochem.

80

1970-1972

738336

26194102

Evolution of selenophosphate synthetases: emergence and relocation of function through independent duplications and recurrent subfunctionalization

2015

Mariotti, M.; Santesmasses, D.; Capella-Gutierrez, S.; Mateo, A.; Arnan, C.; Johnson, R.; D'Aniello, S.; Yim, S.H.; Gladyshev, V.N.; Serras, F.; Corominas, M.; Gabaldon, T.; Guigo, R.

Genome Res.

25

1256-1267

738466

24719756

Binding stoichiometry of a recombinant selenophosphate synthetase with one synonymic substitution E197D to a fluorescent nucleotide analog of ATP, TNP-ATP

2013

Preobrazhenskaya, Y.V.; Stenko, A.I.; Shvarts, M.V.; Lugovtsev, V.Y.

J. Amino Acids

2013

983565

742568

25488369

Characterization of recombinant human gastrointestinal glutathione peroxidase mutant produced in Escherichia coli

2015

Guo, X.; Song, J.; Guan, T.; Wang, S.; Wang, Y.; Meng, Y.; Guo, J.; Li, T.; Ma, C.; Wei, J.

Free Radic. Res.

49

228-235

742715

-

Heterologous expression and characterization of human cellular glutathione peroxidase mutants

2014

Guo, X.; Yu, Y.; Liu, X.; Zhang, Y.; Guan, T.; Xie, G.; Wei, J.

IUBMB Life

66

212-219

760584

28414460

Analysis of Novel interactions between components of the selenocysteine biosynthesis pathway, SEPHS1, SEPHS2, SEPSECS, and SECp43

2017

Oudouhou, F.; Casu, B.; Dopgwa Puemi, A.S.; Sygusch, J.; Baron, C.

Biochemistry

56

2261-2270

761117

28189853

Synthesis of L-cysteine derivatives containing stable sulfur isotopes and application of this synthesis to reactive sulfur metabolome

2017

Ono, K.; Jung, M.; Zhang, T.; Tsutsuki, H.; Sezaki, H.; Ihara, H.; Wei, F.; Tomizawa, K.; Akaike, T.; Sawa, T.

Free Radic. Biol. Med.

106

69-79

761118

29715549

Selenophosphate synthetase 1 and its role in redox homeostasis, defense and proliferation

2018

Na, J.; Jung, J.; Bang, J.; Lu, Q.; Carlson, B.A.; Guo, X.; Gladyshev, V.N.; Kim, J.; Hatfield, D.L.; Lee, B.J.

Free Radic. Biol. Med.

127

190-197

761271

32275991

Initial steps in selenocysteine biosynthesis The interaction between selenocysteine lyase and selenophosphate synthetase

2020

Scortecci, J.F.; Serrao, V.H.B.; Fernandes, A.F.; Basso, L.G.M.; Gutierrez, R.F.; Araujo, A.P.U.; Neto, M.O.; Thiemann, O.H.

Int. J. Biol. Macromol.

156

18-26

762427

29116155

Using CRISPR-Cas9-mediated genome editing to generate C. difficile mutants defective in selenoproteins synthesis

2017

McAllister, K.N.; Bouillaut, L.; Kahn, J.N.; Self, W.T.; Sorg, J.A.

Sci. Rep.

7

14672

Links to other databases for selenium

top print hide

Show Links (1 entry)

ChEBI

PubChem

-