Thioredoxin reductase (EC 1.6.4.5) TXNRD1 (Alternate
Symbols: GRIM-12, TR, TRXR) chromosomal position 12q23.3-q24.1 (§, ‡) is a
homodimeric selenocysteine-containing enzyme. Secys a
selenocysteine residue is an essential TR isozyme component,
located near the C-terminus
region [cysteine (Cys)-497,Secys-498]
of the intracellular, redox
cellular environments center in the catalytically active
enzyme site, Gly-499 is the
actual C-terminal amino acid. In their N-terminal sequences Cys-59, Cys-64
links the thiol/disulfide
oxidoreductase dependent pathway reductases
from there to the flexible C-terminal
part (Secys) of the other sub cellular subunit by which Selenocystine
is efficiently reduced and induce RNR
(Ribonucleotide reductase) for replication
and repair,
where Trx reductase (TR) or oxidized GSH (GSSG) reductase
further supply electrons for RNR. The protein reversibly modulates
specific signal transduction cascades, to regulate multiple
downstream intracellular redox-sensitive proteins that links NADPH
and thiol-dependent
processes which catalyzes NADPH-dependent
reduction in the presence of the redox protein-Trx and
thioredoxin reductase (TR) maintain cysteine residues in numerous
proteins in the reduced state. There are three
TXNRD selenoproteins 5-prime end variants essential
for mammals, one V3
(TXNRD1) encodes an N-terminal
glutaredoxin (GRX) these variants code for thioredoxin glutathione
reductases (TGR). V3 associates with and triggers formation of Filopodia
(cytoplasmic filaments) can guide actin in
migrating cells, the emerging protrusions
of cell membrane restructuring involved is in 'deglutathionylation
values" for mitochondrial and cytosolic thioredoxin reductase (TR)
domains. Characterization of the TR native Thioredoxin and glutathione
systems (TGR) suggests that the lifecycle of E. granulosus
and Schistosoma
mansoni a phylum of Platyhelmintha,
involves the TXNRD1_v3 isoform containing a fused (Grx)
glutaredoxin domain which is abolished by deglutathionylation'
targeted to either mitochondria or the nucleus in the reduction of
glutathionylated substrates, in leishmaniasis
(disease) glutathione reductase system (TGR) is replaced by the trypanothione
reductase (TcTR) system in mammalian cells, essential as these TR3
are significant as a recognized drug target
of these (TcTR)
human protozoan parasites. Cytosolic TR1, mitochondrial
- TR3
and TrxR2
(locus 22q11.21)
where TrxR1
and TrxR2 are consdered as the respective cytosolic
and mitochondrial
thioredoxin reductases, plus the thioredoxin glutathione
reductases-TGR systems
most likely can reduce (Trx) by fusion of the TR and an N-terminal
glutaredoxin domains. As a pyridine
nucleotide disulfide oxidoreductase of the oxidized GSH and GSSG
(selenodiglutathione) reductase TGR
structures enzyme stability, are linked to the previously
characterized two thioredoxin reductases cytosolic TR1 and TR3, and one
mitochondrial variant. Selenols
are key metabolites at mammalian TXNRD1's active (SeCys
498) site. Thioredoxin undergoes NADPH-dependent
reduction (NTRs)
and reduce oxidized cysteine groups on mitochondrial TXNRD1 proteins similar to the cytosolic enzyme, from the FAD binding
domain where the active cystines
and the NADPH binding domain are contained, plus an interface
domain (ID)
of the C-terminal interface homologous to glutathione reductase identifies a mechanism of p53
mediated cell death regulation involving (TrxR) enzymes of redox homeostasis
reactions to overcome the oxidative
stress generating
reactive oxygen species (ROS) on a complex
combination of decreased apoptosis to prevent permanent cell
damage and cell death that tumor cells use to evade the
redox-sensitive signaling factors, or resistance
to therapy. End products of lipid-peroxidation,
4-HNE-(4-Hydroxynonenal) can induce oxidative stress,
other isoforms are more water-soluble adducts detoxifying such a
buildup, peroxidation might be limiting
their (selenoproteins) proper expression. Thioredoxin reductase
(TrxR) is the homodimeric flavoenzyme
that catalyzes reduction of thioredoxin disulfide (Trx) one of the
major redox control systems,
involving a second interaction between NAD(P)H and/or
(quinone reductase) NQO1 via
the FAD-containing enzyme (TR),
thioredoxin reductase forms an oxidoreductase system. TrxRs are
able to reduce a number of substrate proteins other than Trx.
The 3' UTR of selenocysteine-containing genes have a common
stem-loop structure, the sec insertion sequence
(selenocystine-SECIS, PDB: 2ZZ0),
that is necessary for the recognition of a catalytically
active Sec codon rather in the values for mitochondrial and
cytosolic thioredoxins reductase (TR) domains. The Sec residue is
protonated at a different pka than in comparison to that of Cysteine. Cys59-Cys64 two cysteines pair also was oxidized in the N-terminal FAD domain essential for thioredoxin-reducing activity, and the need for Sec-498 (PDB: 2J3N)
to be in complex with the FAD and NADP(+)
during catalysis to the N-terminal active site cysteine residues
Cys59-Cys64 and from there to the C-terminal part of the other subunit which
have selenotetrapeptide
sequences from the other module (PDB: 2J3N).
Secys498 forms, (Human PDB 3QFB,) can both be identified at
active site of the enzyme Gly-499 of the
subunits active Cys-497-TRXR1 (the TR1
structure PDB: 3QFB) are the mechanism(s) for the incorporation of
Se into
TrxRs as the amino acid selenocysteine (Sec), as well as for
delivery to a variety of secondary substrates or TRX (PDB: 3QFB) in nuclei provide means to quantify glutathione (GSH) (PDB: 3H8Q)
conditions of the active GRX functonally and structurally analogus to
TGR (selenodiglutathione) reductase. These two were modeled parts of TGR
were linked to V3 (_TXNRD1) encodes an N-terminal inter-specific
glutaredoxin
(PDB: 1JHB).
From the FAD
binding domain-(PDB: 1ZKQ ) active cystines and the NADPH binding
domain where they are contained, plus an interface domain (ID) of the
C-terminal ID in complex with its substrate thioredoxin
(Trx-PDB: 1TRX,
TXNRD1-3QFB) bringing Cys32
in Trx1 close to Cys497 in 3H8Q to quantify glutathione (GSH) that
helped in characterizing what was separately modeled as the Thioredoxin
reductase (TXNRD1) domain which are consdered as the respective
cytosolic and mitochondrial thioredoxin reductases units with a model
obeying standard geometry that is conceivable of human thioredoxin
reductase 3's structure glutaredoxin domain 3H8Q in complex with the
FAD and NADP(H), when replaced by the TcTR (PDB: 2W0H) trypanothione/trypanothione reductase system involves a
phylum of Platyhelmintha, where a glutathione (GSH) isoform containing a
fused (Grx)
glutaredoxin domain (PDB: 1JHB) is essential for the parasite
survival. The intricate substrate specificities for the thioredoxin
(Trx) system which consists of native Trx and the respective cytosolic
mitochondrial thioredoxin reductase (TrxR) enzymes are likely to be of
central importance to these observations as a determinant of TrxR
function in general, each (the thioredoxin reductase/thioredoxin
pathway) can reduce a number of different types of substrates or
cross-reactive-bound enzyme fractions as active with thioredoxin.
and mitochondrial
thioredoxin reductases, plus the thioredoxin glutathione
reductases-TGR systems
most likely can reduce (Trx) by fusion of the TR and an N-terminal
glutaredoxin domains. As a pyridine
nucleotide disulfide oxidoreductase of the oxidized GSH and GSSG
(selenodiglutathione) reductase TGR
structures enzyme stability, are linked to the previously
characterized two thioredoxin reductases cytosolic TR1 and TR3, and one
mitochondrial variant. Selenols
are key metabolites at mammalian TXNRD1's active (SeCys
498) site. Thioredoxin undergoes NADPH-dependent
reduction (NTRs)
and reduce oxidized cysteine groups on mitochondrial TXNRD1 proteins similar to the cytosolic enzyme, from the FAD binding
domain where the active cystines
and the NADPH binding domain are contained, plus an interface
domain (ID)
of the C-terminal interface homologous to glutathione reductase identifies a mechanism of p53
mediated cell death regulation involving (TrxR) enzymes of redox homeostasis
reactions to overcome the oxidative
stress generating
reactive oxygen species (ROS) on a complex
combination of decreased apoptosis to prevent permanent cell
damage and cell death that tumor cells use to evade the
redox-sensitive signaling factors, or resistance
to therapy. End products of lipid-peroxidation,
4-HNE-(4-Hydroxynonenal) can induce oxidative stress,
other isoforms are more water-soluble adducts detoxifying such a
buildup, peroxidation might be limiting
their (selenoproteins) proper expression. Thioredoxin reductase
(TrxR) is the homodimeric flavoenzyme
that catalyzes reduction of thioredoxin disulfide (Trx) one of the
major redox control systems,
involving a second interaction between NAD(P)H and/or
(quinone reductase) NQO1 via
the FAD-containing enzyme (TR),
thioredoxin reductase forms an oxidoreductase system. TrxRs are
able to reduce a number of substrate proteins other than Trx.The 3' UTR of selenocysteine-containing genes have a common
stem-loop structure, the sec insertion sequence
(selenocystine-SECIS, PDB: 2ZZ0),
that is necessary for the recognition of a catalytically
active Sec codon rather in the values for mitochondrial and
cytosolic thioredoxins reductase (TR) domains. The Sec residue is
protonated at a different pka than in comparison to that of Cysteine. Cys59-Cys64 two cysteines pair also was oxidized in the N-terminal FAD domain essential for thioredoxin-reducing activity, and the need for Sec-498 (PDB: 2J3N)
to be in complex with the FAD and NADP(+)
during catalysis to the N-terminal active site cysteine residues
Cys59-Cys64 and from there to the C-terminal part of the other subunit which
have selenotetrapeptide
sequences from the other module (PDB: 2J3N).
Secys498 forms, (Human PDB 3QFB,) can both be identified at
active site of the enzyme Gly-499 of the
subunits active Cys-497-TRXR1 (the TR1
structure PDB: 3QFB) are the mechanism(s) for the incorporation of
Se into
TrxRs as the amino acid selenocysteine (Sec), as well as for
delivery to a variety of secondary substrates or TRX (PDB: 3QFB) in nuclei provide means to quantify glutathione (GSH) (PDB: 3H8Q)
conditions of the active GRX functonally and structurally analogus to
TGR (selenodiglutathione) reductase. These two were modeled parts of TGR
were linked to V3 (_TXNRD1) encodes an N-terminal inter-specific
glutaredoxin
(PDB: 1JHB).
From the FAD
binding domain-(PDB: 1ZKQ ) active cystines and the NADPH binding
domain where they are contained, plus an interface domain (ID) of the
C-terminal ID in complex with its substrate thioredoxin
(Trx-PDB: 1TRX,
TXNRD1-3QFB) bringing Cys32
in Trx1 close to Cys497 in 3H8Q to quantify glutathione (GSH) that
helped in characterizing what was separately modeled as the Thioredoxin
reductase (TXNRD1) domain which are consdered as the respective
cytosolic and mitochondrial thioredoxin reductases units with a model
obeying standard geometry that is conceivable of human thioredoxin
reductase 3's structure glutaredoxin domain 3H8Q in complex with the
FAD and NADP(H), when replaced by the TcTR (PDB: 2W0H) trypanothione/trypanothione reductase system involves a
phylum of Platyhelmintha, where a glutathione (GSH) isoform containing a
fused (Grx)
glutaredoxin domain (PDB: 1JHB) is essential for the parasite
survival. The intricate substrate specificities for the thioredoxin
(Trx) system which consists of native Trx and the respective cytosolic
mitochondrial thioredoxin reductase (TrxR) enzymes are likely to be of
central importance to these observations as a determinant of TrxR
function in general, each (the thioredoxin reductase/thioredoxin
pathway) can reduce a number of different types of substrates or
cross-reactive-bound enzyme fractions as active with thioredoxin.
[1.] Selenium yeast: seleno yeast PMID: 16857846
[2.] Sulforaphane From Broccoli PMID: 16377050, 12742546, 20204301, 12949356, 19595745, 17150329, 15740016, 12663510, 15998110, 17300148
[3.] Chlorella vulgaris: corresponding to a chloroplast NADPH-dependent thioredoxin reductase gene (NTR-C), in Chlorella PMID: 18029787
[4.] Scutellarin: It can be found in Scutellaria barbata and S. lateriflora. PMID: 15131321
[5.] Curcumin (TURMERIC plant of the ginger family): PMID: 21782934, 20160040, ~15879598
[6.] Experiments in E. huxleyi genus phytoplankton PMID: 20032866
[7.] Gambogic Acid pigment of gambooge resin from tree species Garcinia gummi-gutta. PMID: 24407164
[8.] Shikonin an antioxidant (no longer approved for use,: targets the Sec residue [13.] in TrxR1 to inhibit its physiological function. see: (Methane-) methylseleninic acid (MSA)) obtained from the extracts of plant [9.] Lithospermum erythrorhizon. PMID: 24583460
[10.] Black tea extract (BTE) theaflavin (TF) PMID: 19059456
[11.] Green tea extract-epigallocatechin-3-gallate (EGCG) PMID: 19020731
[12.] Eicosatetraenoic acid, (Mortierella Alpina Oil) Arachidonic acid (AA) all-cis-5,8,11,14-eicosatetraenoic acid, 5-Hydroxyicosatetraenoic_acid_and_5-oxo-eicosatetraenoic_acid PMID: 15123685
[13.] Juglone: In the food industry known as C.I. Natural Brown 7 and C.I. 75500. (DTNB assay, a synthetic approach for Cys and Sec residues.) PMID: 21172426, 11170645, 18382651 ... a 5,5'-[dithiobis Pyritinol: analogue, Sulbutiamine]
[14.] The antioxidant ubiquinol-10 (Q10) PMID: 12435734
[15.] Rottlerin, conductance potassium channel (BKCa++) opener, source the Kamala tree. PMID: 17581112
[16.] Ajoene a chemical compound available from garlic. PMID: 9986706
No CiTO relationships defined
http://vixra.org/abs/1502.0252
http://www.citeulike.org/user/emissrto/article/13530556
[2.] Sulforaphane From Broccoli PMID: 16377050, 12742546, 20204301, 12949356, 19595745, 17150329, 15740016, 12663510, 15998110, 17300148
[3.] Chlorella vulgaris: corresponding to a chloroplast NADPH-dependent thioredoxin reductase gene (NTR-C), in Chlorella PMID: 18029787
[4.] Scutellarin: It can be found in Scutellaria barbata and S. lateriflora. PMID: 15131321
[5.] Curcumin (TURMERIC plant of the ginger family): PMID: 21782934, 20160040, ~15879598
[6.] Experiments in E. huxleyi genus phytoplankton PMID: 20032866
[7.] Gambogic Acid pigment of gambooge resin from tree species Garcinia gummi-gutta. PMID: 24407164
[8.] Shikonin an antioxidant (no longer approved for use,: targets the Sec residue [13.] in TrxR1 to inhibit its physiological function. see: (Methane-) methylseleninic acid (MSA)) obtained from the extracts of plant [9.] Lithospermum erythrorhizon. PMID: 24583460
[10.] Black tea extract (BTE) theaflavin (TF) PMID: 19059456
[11.] Green tea extract-epigallocatechin-3-gallate (EGCG) PMID: 19020731
[12.] Eicosatetraenoic acid, (Mortierella Alpina Oil) Arachidonic acid (AA) all-cis-5,8,11,14-eicosatetraenoic acid, 5-Hydroxyicosatetraenoic_acid_and_5-oxo-eicosatetraenoic_acid PMID: 15123685
[13.] Juglone: In the food industry known as C.I. Natural Brown 7 and C.I. 75500. (DTNB assay, a synthetic approach for Cys and Sec residues.) PMID: 21172426, 11170645, 18382651 ... a 5,5'-[dithiobis Pyritinol: analogue, Sulbutiamine]
[14.] The antioxidant ubiquinol-10 (Q10) PMID: 12435734
[15.] Rottlerin, conductance potassium channel (BKCa++) opener, source the Kamala tree. PMID: 17581112
[16.] Ajoene a chemical compound available from garlic. PMID: 9986706
No CiTO relationships defined
http://vixra.org/abs/1502.0252
http://www.citeulike.org/user/emissrto/article/13530556
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