Tag Archives: catalase

CHANGES IN GLUTATHIONE AND GLUTATHIONE REDUCTASE POSITIONING GLUTATHIONE-S-TRANSFERASE AS A FUNCTION OF CELL CONCENTRATION WITH ENZYME ACTIVITIES FOUND TO INFLUENCE BEHAVIOR.

Glutathione reductase (GSR, GR) locus in the chromosomal region 8p21.1, (EC 1.8.1.7)-(§, ) is a protein-S-glutathionylation, as a (human) Mitochondrial localization of hGSR and its associated enzymes cellular thiol/disulfides S-Glutathione reductase (GSR) which is the importance of significance in reversible thiol modifications which  regenerates reduced glutathione (GSH) and GSSG to the reduced form found in the obvious structural properties of glutathione reductase. The redox regulating enzymes relationship with TTase (thioltransferase) activity with the ratio of the activities of G3PD, as the mechanism (of cellular repair) ‘differs’ (gssg-g6pg) according to the type of reducing glutathionylated mixed disulfide, including protein-S-S-glutathione (PSSG), GSR reduces (PSSG) modified by thiolation to a normal level in human lens epithelial (HLE) cells. This may have implications in stress- and aging-related pathologies in astrocytes and granule cells, demonstrated by comparable mitochondria/cytosolic concentrations of its thiol proteins, where a mitochondrial leader sequence (cDNA) is present in the gene structure of human GSR and may be the Cytoplasmic Isoform (derivative or inhibitor formed) of  mitochondrial dysfunction that contains the catalytic cysteine revealing a possible therapeutic strategy/target, also indicating transiently accumulated inhibitor proteins modified by thiolation (cysteine catalytic subunits) compounds that inhibit these (re)activation processes (hGSR) with its structure-based prosthetic group (FAD) cofactor is common because of the levels of cysteine available; are mitochondria/cytosolic concentrations that the Glutathione reductases reversible thiol modifications which catalyzes the reduction of GSSG to GSH the natural GR substrate is dependent on the NADPH:GS-SG ratio.
PDB Id: 3DK9 Cys58 and Cys63 represent the enzyme’s results seen as the reductive (GSH) Cys-58 and oxidative (GSSG) Cys-63 is the relationship of these two enzymes, His467‘ is seen to interact with Cys63 more optimally and Cys-58 produces the second GSH intermediate molecule of the reaction is the reduced glutathione-to-oxidized glutathione ratio (GSH/GS-SG) when compared to the substrate free form correlated with (FAD) the flavin compounds, flow from NADPH to the substrate GSSG via flavin. The reducing equivalents needed for regeneration of GSH are provided by NADPH. The enzyme has affinity for flavin adenine dinucleotide (FAD) the prosthetic group of GR, and maintains high levels of reduced glutathione  (Cytoplasmic Isoform: Produced by alternative initiation of isoform Mitochondrial homodimer, derivative or inhibitor formed from the GSR Pyridine, dimerisation domain.) in the cytosol. Glutathione reductase (GR) plays a key role in maintaining either a thiol group or a nonprotein sulfhydryl group (NPS) form of GSH, and potential for thioredoxin and glutathione systems, as thioredoxin dose not require GSH and GR for catalytic activity. Glutathione reductase (GR) utilizes NADPH produced by G6PDH (glucose-6-phosphate dehydrogenase) enzyme activities, and enzyme glutathione reductase (GR) represents the erythrocyte glutathione-reducing system (GRS), of the GSH pathway to oxidation and inactivation in the activity of GSH peroxidase and GSH reductase. Expression of the regulatory subunit of gamma-glutamylcysteine synthetase/ligase (GCL) catalyzes the first and rate-limiting step in the production of the cellular (GSH) glutathione. Dietary riboflavin (Vitamin B2) intake produces its active essential coenzyme flavin forms, riboflavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) of glutathione reductase (GR), or the GR activity correlated with red-cell flavin compounds.When both GSSG and NADP(+) substrates and products are present, glutathione reductase (GR) is a enzyme required for the conversion in the presence and absence of flavin adenine dinucleotide (FAD), glutathione reductase (GR) is an obligatory FAD-containing homodimer. GSSG via glutathione reductase (GR) regenerates reduced glutathione which is essential for antioxidant defense. The flavoenzyme glutathione reductase (GR) reduces ‘oxidized glutathione’ (GSSG) back to GSH, also involving glutamate-cysteine ligase and modulatory (GCL)-can be upregulated ∉ as the cellular GSH system, indicating short-term and heritable tolerance of exposure to oxidative stress from/via numerous reporting ∈ mechanisms. NADPH is used by glutathione reductase for the reduction of oxidized glutathione (glutathione disulphide) GSSG to GSH-dependent peroxide metabolism. 4-Hydroxynonenal (HNE) is one of the major end products of lipid peroxidation which may lead to enhanced action of  the (GSR) oxygen radical, glutathione S-transferases (GSTs) are specifically suited to the detoxification and removal of 4-HNE (∋ or ∝) from cells which may provide a basis for selective cellular and/or subcellular distribution of mitochondrial and cytosolic to individual detoxifying gene inducer activities of glutathione reductase (GR), the cellular (GSH) glutathione. It was evident the enzyme glutathione reductase (GR) represents the erythrocyte glutathione-reducing system (GRS), of the GSH pathway to oxidation and the (∉ or ∝) inhibition constant for reversible inactivation in the activity of glutathione related antioxidant enzymes. And GSH reductase may be one of the factors that remained in focus that suggests its effects on the antioxidant system related to glutathione synthesis (GCL), degradation, and functions.
Biological Xenobiotics, Extracts, Applications of note In the presence of Glutathione reductase.:
Schisandrin (Schisandra chinensis), used in traditional Chinese medicine. PMID:21328628
Transketolase (TK) and transaldolase (TA)
Melatonin PMID:15571523, 19475625
Blackberry (Rubus sp.) cultivars, The ‘Hull Thornless’,  PMID:11087537
Glutathione dehydrogenase (ascorbate)-[dehydroascorbate reductase (DHAR), and glutathione reductase (GR). This enzyme participates in the glutathione metabolism the active metabolite of vitamin D3 increases glutathione levels.] PMID:11087537, 23770363
3H-1,2-dithiole-3-thione nutraceutical D3T potently induces the cellular GSH system, Anethole trithione is a drug used in the treatment of dry mouth, the Anethole trithione isomer is related to anethole (anise camphor) used as a flavoring substance. PMID:17206382*, 19408115,     19176875*, 15896789, 18408143*, Glutathione reductase
16946404*
Cassia fistula used in herbal medicine. PMID:19088944
Sanguinarine is extracted from some plants, including bloodroot and Mexican prickly poppy (Argemone mexicana) where argimone oil causes Epidemic dropsy. PMID:11260782
Vitamin E, PMID: 15672860
Tocotrienols are natural compounds members of the vitamin E family found in select vegetable oils are an essential nutrient for the body. PMID:21845802
Pyrrolizidine alkaloids are produced by plants as a defense mechanism against insect herbivores consumption of PAs is known as pyrrolizidine alkaloidosis. PMID:20144959
Apple extract (AE) PMID:20401791
Lipoic Acid an organic compound, forming a disulfide bond, available as a dietary supplement PMID:15246746, 21073761
Carnitine PMID:15246746, 10581232
Vitamin D upregulated expression of GCLC and GR. PMID:23770363
Vitamin D3_ PMID:12416023
Vitamin E_ PMID:10459841, 8360018, 18296478, 21845802, 15490422, 16885600, 7062348, 20729758, 21086752
Shidagonglao roots Mahonia fortunei (十大功劳 shi da gong lao) species contains the alkaloid berberine PMID:199382 18
Coenzyme Q10 (CoQ10) PMID:16621054
Trigonella foenum graecum seed powder (TSP) PMID:15026271
Boschniakia rossica, a ̱̱̱Traditional Chinese medicine. PMID:19352025
Aegle marmelos commonly known as bael is a species of tree. PMID:18830880
Scoparia dulcis A medicinal plant, dulcis. PMID:21905284
Fenugreek (Trigonella foenum-graecum)  is used as a herb. PMID:15026271
L-arginine (L-Arg) semiessential supplementation common natural amino acid. PMID:16038634
Hypericum perforatum (St. John’s Wort) PMID:18754092
Urtica dioica often called common nettle PMID:12834006
Usnea longissima, a medicinal lichen. PMID:16169175
Capparis decidua, a fruting tree also used in folk medicine and herbalism. PMID:22272107
Indole-3-carbinol found at relatively high levels in cruciferous vegetables such as broccoli
PMID:9512722, 14512388
Ascorbate Vitamin C. PMID:14512388
Sulforaphane It is obtained from cruciferous vegetables such as broccoli. PMID:12628444, 18607771*, 22303412
Andrographis paniculata, may shorten the duration and lessen the symptoms of common cold. PMID:11507728
Vitamin B-1 (thiamine) PMID:1132146, 10450194, 21308351*, 11514662*, 1270885
Vitamin B2 (riboflavin) PMID: 5822598, 5550591, 1201246, 5794396, 237845, 3677785, 3582603, 12194936, 2721660, 1261528, 5721130, 14608016, 4400882, 7883462, 844948, 7337797, 5881,12641409, 4393763, 3497609, 16883966…(№ 1244, OMIM.138300)
Vitamin B-6 (Pyridoxine) PMID:2721660, 3582603, 10450194, 15490422, 1270885, 7417521, 7337797, 7814235
Vitamin B9 (Folic acid)  PMID: 844947, 1270885
Aspartate transaminase (AST) or glutamic oxaloacetic transaminase (GOT) catalyzes the interconversion of aspartate an important enzyme in amino acid metabolism. PMID:1132146, 10450194, 1253408
β-Carotene is a strongly colored red-orange pigment abundant in plants and fruits. PMID:19957244
3-Hydroxykynurenine (3OHKyn) a metabolite of tryptophan. PMID:11273669
Ajoene ((E,Z)-4,5,9-trithiadodeca-1,6,11-triene 9-oxide), a garlic-derived natural compound. PMID:9986706 PDB: 1BWC
Propolis a product made by bees. PMID:19394397
Resveratrol produced naturally by several plants PMID:12797471
No CiTO relationships defined:


Brenneman, M. R.
Changes in glutathione and glutathione reductase
positioning glutathione-s-transferase as a function of cell concentration
with enzyme activities found to influence behavior. (2015).
URL http://vixra.org/abs/1506.0104.

http://www.citeulike.org/user/emissrto/article/13645622

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Thioredoxin reductase: Selenotetrapeptide sequences with specificity for thioredoxin and glutathione systems

  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, mitochondrialTR3 and TrxR2 (locus 22q11.21) where TrxR1 and TrxR2 are consdered as the respective cytosolic 1w1e MITOCHONDRIAL cytoplasmicand 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.


3qfbThe 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).3qfb-3h8q 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 1-2 and 3’s structures 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


Catalase, the antioxidant heme enzyme one of three subgroups related to catalase deficiency in humans modulating the normal catalase reaction dependent on NADPH-binding catalases for function.

Catalase (CAT) is converted by decomposition and intracellular localization relationships of the main cellular antioxidant enzyme system like superoxide dismutase (SOD), peroxiredoxins (Prdx), and glutathione peroxidase (GPX) are peroxisomal matrix enzymes in the cytoplasm, translocated to the peroxisomes to catalyze hydrogen peroxide H2O2 which is decomposed to oxygen and water, locus: 11p13 (§, ). Unlike catalase, the objective of this communication, SOD which prevents the formation of Hydroxyl radicals – (HRGT) determined from constant of O2.- dismutation, and generation of reversibly inactive (CAT)-compound II, Panax ginseng could induce both transcription factors. Catalase is  composed of four identical subunits each of the subunits binds one heme-containing active site, and produces two catalase compounds HPI and HPII (PDB: 1p80) is flipped 180 degrees » with respect to the orientation of the heme related to the « root mean square to the structure of catalase, (Mutation Location) from peroxisomal catalases inactive state in compound II NADP+(H) binding pockets inverted remains similar to the structure of the wild type (Val111, PDB:1A4E, KatG) orientation on the heme proximal (PDB: 1GGK) side, inactivate catalase can be prevented by melatonin. Catalase (CAT; EC 1.11.1.6) a  free radical scavenging enzyme (FRSE) is a scavenger of H2O2. Protoporphyrin – (ZnPPIX) (PDB: 1H6N), from a heme group of the ‘heme-pathway, which forms catalase,’ is a scavenger of antioxidant (HO-1-HMOX1) heme oxygenase, involving ROS. Catalase is part of the enzymatic defense system constituting the primary defense against ROS, zinc protoporphyrin IX (ZnPPIX) is an inhibitor of (HO-1) heme oxygenase. Catalase protects the cell from oxidative damage by the accumulation of cellular reactive oxygen species (ROS) generation systems, those peroxisomal enzymes that breaks down hydrogen peroxide after H(2)O(2) exposure, and thereby mitigates* (some contradictory* results) the toxic effects of hydrogen peroxide. In the process (The typical hydroperoxidases (CAT) known as Compound I) of the substrate of catalase, NADP+ (an inactive state, compound II) is replaced by another molecule of NADP(H) to provide protection of catalase against inactivation by (H2O2) hydrogen peroxide. Erythrocyte  [Human erythrocyte catalase (HEC), The NADPH-binding sites were empty – PDB: 1F4J, 1QQW] and plasma indices (enzymatic-antioxidants) initially implies the thiobarbituric acid-reacting substances (TBARS) based on reaction with hydroxyl radicals (OH) can release thiobarbituric acid, TBAR inhibition measures malondialdehyde (MDA – impact of coenzyme Q10) correlated (with MPO-myeloperoxidase activity -generating ROS) as co-variable, by which mulberry leaf polysaccharide (MLPII) via the decomposition of (certain) MDA, products of lipid peroxidation (LPO) were reduced. Comparisons were to specific activities of catalase (SNP) single nucleotide polymorphisms (CAT-C-262 (rs1001179) the low-risk allele) of genetic variants in both, promoter a common C/T polymorphism (262-C/T), and in nineexonic – regions and its boundaries, occur frequently associated distally in genomic mutations, similar to those of normal catalase demonstrating changes in catalase protein level targeted to the peroxisomal matrix. The 262-C/T CAT low-risk allele is hypothetically related to the lower risk variant allele CAT Tyr308 G to A point mutation ineducable in the Japanese acatalasemia allele. The common C/T polymorphism can be targeted by dietary and/or pharmacological antioxidants, and the endogenous antioxidant defense enzymes concentration can prevent cellular lipid (LPO) peroxidative reactions occurring. Catalase is a homotetramer complex of 4 identical monofunctional subunits. Catalase is located at the peroxisome of human cells associated with several (PBDs)-peroxisomal biogenesis disorders commonly caused by mutations in the PEX genes, peroxisomal targeting signal 1 (PTS1) protein affecting in peroxisomal biogenesis, the monomeric to homotetrameric transition in the forms of peroxisome biogenesis disorder. PBDs also include Acatalasemia the only disease known to be caused by the (CAT) gene. In human catalase, the antioxidant heme enzyme, is localized in the cytoplasm to the peroxisome, nucleus, or linked with mitochondria which in most cells lack catalase (Peroxisomes do not contain DNA), its mitochondrial fraction (microperoxisome), a secondary phenomena shows physiological decline, aging and age-related reactions in mitochondrial function and disfunction. NADPH is required for the prevention of forming an inactive state of the enzyme. Antioxidative defence mechanisms, capacity and redox cycle enzyme activities increasing with Tc treatment Tinospora cordifolia (Tc), T and B cells and antibody. Both RBCs and plasma were measured on parameters of oxidative stress. Syzygium cumini aqueous leaves extract (ASc) was able to remove oxidant species in a hyperglycemic state generated in red blood cells RBC-CAT levels. Catalase alone is unable to prevent in a hyperglycemic state. Macrophages recruit other types of immune cells such as lymphocytes white blood cells (WBCs).  Catalase is dependent on the family of NADPH-binding catalases for function, the prevention and reversal of inactivation by its toxic substrate (H2O2) hydrogen peroxide. Amyloid-beta binds catalase and inhibits (H2O2) hydrogen peroxide, a reactive oxygen species, breakdown through efficient dismutation, and malonaldelhyde (MDA) determined in plasma, as well as another member of the oxidoreductase family, myeloperoxidase (MPO (EC 1.11.1.7)) converting H(2)O(2), the reducing equivalents produces (HOCl) hypochlorous acid a mechanism of cell-mediated antimicrobial immune defense for monofunctional catalases one of three subgroups related to catalase deficiency in humans, in micro-organisms manganese-containing catalases (‘large catalases’) determining in part the bifunctional activity of (KatG, PDB:1X7U) represented by bifunctional (heme) catalase-peroxidase based Bacterial-resistance mechanisms. Peroxiredoxins (Prxs, EC 1.11.1.21), bifunctional catalase-peroxidases (KatGs) two organelle systems are antioxidant enzymes of the peroxiredoxin family that oxidize and reduce H(2)O(2) hydrogen peroxide thereby modulating the catalase reaction, KatGs are not found in plants and animals. Trx (thioredoxin) a redox-regulating protein also controls the antioxidant enzyme activity of the main cellular antioxidant enzymes (AOE) superoxide dismutase (SOD) and catalase.
The function of NADPH bound to Catalase.
catalaseThe cytosine to thymidine transition of nucleotide-262 (-262C>T) Computer analysis indicated that the two variants bound promoter the Ile  (-262 C/T) and (B) Ile-262 in the 5′-flanking region carrying the T allele best captured and characterized the generation of the hydroxyl radical site in (PDB: 1DGB), (CAT) -[GLU] 330C>T transition, is known also as -262C>T. The ‘T allele in comparison to the C allele’ is a common C/T polymorphism frequency in the promoter region association was observed between genotypes for locus11p13 risk alleles acatalasemia mutation Asp (37C>T in exon 9) was hypothetically related to the lower risk Japanese acatalasemia allele Tyr308 a single G to A (see: rs7947841  to evaluate the link to rs769214) point mutation ineducable or near exon 9 (TC, CC, TT) of the CAT gene to which variant changes in the promoter region C/T-262 polymorphism are more closely related to CAT T/C at codon 389 in exon 9 (rs769217) polymorphism did not differ significantly from those of healthy controls in both promoter (-262 C/T) and in exonic (ASP389 C/T) regions of the catalase (CAT). catalase Tyr 370 resolves the 25 A-long (hydrogen peroxide) channel a constriction or narrowing of the channel leading to the heme cavity (‘Parameters) situated in the entrance channel to a heme protoporphyrin (ZnPPIX) (PDB: 1H6N) from a heme group, capable of heme biosynthesis‘ in a wide range of organisms convert it into into heme b, protoporphyrin IX-heme. Two channels lead close to the distal side.  A third channel reaching the heme proximal side Tyr 370, Ile-262 is proposed as a the ‘PDB: 1DGB – variant with a substituted residue in the ASP 178 to the (Met) D181E variant PDB 1p80‘.  These differences include the structure of the variant protein Val111Ala (Saccharomyces cerevisiae) related supports the existence of the ‘Heme and NADP(H) binding pockets’. The omission of a 20-residue  PDB: 1F4J, (1QQW) segment corresponds to the N-terminal (blue) of catalase from human erythrocytes (HEC), or in a C-terminal (red) domain organized with an extra flavodoxin-like fold topology may provide with weak coordination the N- or C-terminal, that allows scrutiny of the origins (topology) in this report of what would otherwise remain speculative or determined with further verification.
 Biological Xenobiotic Extracts Applications of note In the presence of Catalase:
green tea polyphenol (-)-epigallocatechin-3-gallate (EGCG)
Yamamoto T, Lewis J, Wataha J, Dickinson D, Singh B, Bollag WB, Ueta E, OsakiT, Athar M, Schuster G, Hsu S. Roles of catalase and hydrogen peroxide in greentea polyphenol-induced chemopreventive effects. J Pharmacol Exp Ther. 2004Jan;308(1):317-23. Epub 2003 Oct 20. PubMed PMID: 14569057.Furukawa A, Oikawa S, Murata M, Hiraku Y, Kawanishi S. (-)-Epigallocatechingallate causes oxidative damage to isolated and cellular DNA. Biochem Pharmacol.2003 Nov 1;66(9):1769-78. PubMed PMID: 14563487.*
Trigonella (Fenugreek)
Mohammad S, Taha A, Bamezai RN, Basir SF, Baquer NZ. Lower doses of vanadatein combination with trigonella restore altered carbohydrate metabolism andantioxidant status in alloxan-diabetic rats. Clin Chim Acta. 2004Apr;342(1-2):105-14. Erratum in: Clin Chim Acta. 2010 Aug 5;411(15-16):1158.Mohamad, Sameer [corrected to Mohammad, Sameer]. PubMed PMID: 15026271.
Aegle marmelos
Khan TH, Sultana S. Antioxidant and hepatoprotective potential of Aeglemarmelos Correa. against CCl4-induced oxidative stress and early tumor events. JEnzyme Inhib Med Chem. 2009 Apr;24(2):320-7. doi: 10.1080/14756360802167754 .PubMed PMID: 18830880.
Centella asiatica
Flora SJ, Gupta R. Beneficial effects of Centella asiatica aqueous extractagainst arsenic-induced oxidative stress and essential metal status in rats.Phytother Res. 2007 Oct;21(10):980-8. PubMed PMID: 17600859.
Daidzein
Mishra P, Kar A, Kale RK. Prevention of chemically induced mammarytumorigenesis by daidzein in pre-pubertal rats: the role of peroxidative damageand antioxidative enzymes. Mol Cell Biochem. 2009 May;325(1-2):149-57. doi:10.1007/s11010-009-0029-1. Epub 2009 Feb 13. PubMed PMID: 19214712.
Capparis
Yadav P, Sarkar S, Bhatnagar D. Action of capparis decidua againstalloxan-induced oxidative stress and diabetes in rat tissues. Pharmacol Res. 1997Sep;36(3):221-8. PubMed PMID: 9367667.
Retinal
Kannan R, Jin M, Gamulescu MA, Hinton DR. Ceramide-induced apoptosis: role ofcatalase and hepatocyte growth factor. Free Radic Biol Med. 2004 Jul15;37(2):166-75. PubMed PMID: 15203188.
Retinol
Cemek M, Caksen H, Bayiroğlu F, Cemek F, Dede S. Oxidative stress andenzymic-non-enzymic antioxidant responses in children with acute pneumonia. CellBiochem Funct. 2006 May-Jun;24(3):269-73. PubMed PMID: 16634091.
Diallyl disulfide (Allicin)
Kalayarasan S, Prabhu PN, Sriram N, Manikandan R, Arumugam M, Sudhandiran G.Diallyl sulfide enhances antioxidants and inhibits inflammation through theactivation of Nrf2 against gentamicin-induced nephrotoxicity in Wistar rats. EurJ Pharmacol. 2009 Mar 15;606(1-3):162-71. doi: 10.1016/j.ejphar.2008.12.055. Epub2009 Jan 19. PubMed PMID: 19374873.
Leucas aspera (Catechin, EGCG)
Kripa KG, Chamundeeswari D, Thanka J, Uma Maheswara Reddy C. Modulation ofinflammatory markers by the ethanolic extract of Leucas aspera in adjuvantarthritis. J Ethnopharmacol. 2011 Apr 12;134(3):1024-7. doi:10.1016/j.jep.2011.01.010. Epub 2011 Jan 18. PubMed PMID: 21251972.
Urtica dioica (nettle suppliment)Ozen T, Korkmaz H. Modulatory effect of Urtica dioica L. (Urticaceae) leaf
extract on biotransformation enzyme systems, antioxidant enzymes, lactatedehydrogenase and lipid peroxidation in mice. Phytomedicine. 2003;10(5):405-15.PubMed PMID: 12834006.
Justicia adhatoda
Singh RP, Padmavathi B, Rao AR. Modulatory influence of Adhatoda vesica(Justicia adhatoda) leaf extract on the enzymes of xenobiotic metabolism,antioxidant status and lipid peroxidation in mice. Mol Cell Biochem. 2000Oct;213(1-2):99-109. PubMed PMID: 11129964.
Phyllanthus niruri L. (Euphorbiaceae) (P. niruri)
Bhattacharjee R, Sil PC. Protein isolate from the herb, Phyllanthus niruri L.(Euphorbiaceae), plays hepatoprotective role against carbon tetrachloride inducedliver damage via its antioxidant properties. Food Chem Toxicol. 2007May;45(5):817-26. Epub 2006 Nov 11. PubMed PMID: 17175085.
Tinospora cordifolia
Sharma V, Pandey D. Protective Role of Tinospora cordifolia againstLead-induced Hepatotoxicity. Toxicol Int. 2010 Jan;17(1):12-7. doi:10.4103/0971-6580.68343. PubMed PMID: 21042467; PubMed Central PMCID: PMC2964743.
Aher V, Kumar Wahi A. Biotechnological Approach to Evaluate theImmunomodulatory Activity of Ethanolic Extract of Tinospora cordifolia Stem(Mango Plant Climber). Iran J Pharm Res. 2012 Summer;11(3):863-72. PubMed PMID:24250513; PubMed Central PMCID: PMC3813135.
coenzyme Q10
Lee BJ, Lin YC, Huang YC, Ko YW, Hsia S, Lin PT. The relationship betweencoenzyme Q10, oxidative stress, and antioxidant enzymes activities and coronaryartery disease. ScientificWorldJournal. 2012;2012:792756. doi:10.1100/2012/792756. Epub 2012 May 3. PubMed PMID: 22645453; PubMed CentralPMCID: PMC3356738.
Dietary carotenoid-rich pequi oil
Miranda-Vilela AL, Akimoto AK, Alves PC, Pereira LC, Gonçalves CA,Klautau-Guimarães MN, Grisolia CK. Dietary carotenoid-rich pequi oil reducesplasma lipid peroxidation and DNA damage in runners and evidence for anassociation with MnSOD genetic variant -Val9Ala. Genet Mol Res. 2009 Dec15;8(4):1481-95. doi: 10.4238/vol8-4gmr684. PubMed PMID: 20082261.
Tinospora cordifolia  (Mango Plant Climber) extract from Tinospora known as Tinofend Aher V, Kumar Wahi A. Biotechnological Approach to Evaluate theImmunomodulatory Activity of Ethanolic Extract of Tinospora cordifolia Stem(Mango Plant Climber). Iran J Pharm Res. 2012 Summer;11(3):863-72. PubMed PMID:24250513; PubMed Central PMCID: PMC3813135.
 mulberry leaf polysaccharide (MLPII)
Ren C, Zhang Y, Cui W, Lu G, Wang Y, Gao H, Huang L, Mu Z. A polysaccharideextract of mulberry leaf ameliorates hepatic glucose metabolism and insulinsignaling in rats with type 2 diabetes induced by high fat-diet andstreptozotocin. Int J Biol Macromol. 2014 Oct 11. pii: S0141-8130(14)00674-6.doi: 10.1016/j.ijbiomac.2014.09.060. [Epub ahead of print] PubMed PMID: 25316427.
five widely studied medicinal plants (Protandim)
Nelson SK, Bose SK, Grunwald GK, Myhill P, McCord JM. The induction of humansuperoxide dismutase and catalase in vivo: a fundamentally new approach toantioxidant therapy. Free Radic Biol Med. 2006 Jan 15;40(2):341-7. PubMed PMID:16413416.
melatonin
Mayo JC, Tan DX, Sainz RM, Lopez-Burillo S, Reiter RJ. Oxidative damage tocatalase induced by peroxyl radicals: functional protection by melatonin andother antioxidants. Free Radic Res. 2003 May;37(5):543-53. PubMed PMID: 12797476.
Protective effect of harmaline
Kim DH, Jang YY, Han ES, Lee CS. Protective effect of harmaline and harmalolagainst dopamine- and 6-hydroxydopamine-induced oxidative damage of brainmitochondria and synaptosomes, and viability loss of PC12 cells. Eur J Neurosci.2001 May;13(10):1861-72. PubMed PMID: 11403679.
horseradish peroxidase (HRP)
Shen L, Hu N. Heme protein films with polyamidoamine dendrimer: directelectrochemistry and electrocatalysis. Biochim Biophys Acta. 2004 Jan30;1608(1):23-33. PubMed PMID: 14741582.
Selegiline (–)Deprenyl
Kitani K, Minami C, Isobe K, Maehara K, Kanai S, Ivy GO, Carrillo MC. Why(–)deprenyl prolongs survivals of experimental animals: increase of anti-oxidantenzymes in brain and other body tissues as well as mobilization of varioushumoral factors may lead to systemic anti-aging effects. Mech Ageing Dev. 2002Apr 30;123(8):1087-100. Review. PubMed PMID: 12044958.
Rhodiola rosea
Bayliak MM, Lushchak VI. The golden root, Rhodiola rosea, prolongs lifespanbut decreases oxidative stress resistance in yeast Saccharomyces cerevisiae.Phytomedicine. 2011 Nov 15;18(14):1262-8. doi: 10.1016/j.phymed.2011.06.010. Epub2011 Jul 30. PubMed PMID: 21802922.
Carnitine
Kiziltunc A, Coğalgil S, Cerrahoğlu L. Carnitine and antioxidants levels inpatients with rheumatoid arthritis. Scand J Rheumatol. 1998;27(6):441-5. PubMedPMID: 9855215.
 Syzygium cumini
 De Bona KS, Bellé LP, Sari MH, Thomé G, Schetinger MR, Morsch VM, Boligon A,
Athayde ML, Pigatto AS, Moretto MB. Syzygium cumini extract decrease adenosine
deaminase, 5’nucleotidase activities and oxidative damage in platelets of
diabetic patients. Cell Physiol Biochem. 2010;26(4-5):729-38. doi:
10.1159/000322340. Epub 2010 Oct 29. PubMed PMID: 21063110.