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 nine - exonic - 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.
The 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 (ASP-389 C/T) regions of the catalase (CAT).  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.

Gluathione peroxidase (GSH-Px1-GPX1) a extracellular selenoenzyme expression modulates xenobiotic metabolising enzymes.

     Glutathione peroxidase (EC 1.11.1.9) protects against oxidative damage via the chemoprotective action of nitric-oxide mediated lipid peroxidation and anti oxidative defense by gluathione (GSH-Px1-GPX1) a extracellular selenoenzyme, extracellular glutathione peroxidase (E-GPx) and cellular (C-GPx) detoxifies hydroperoxides. Other antioxidant genes (AOX) as Gpx1, is located in the cytosol and in (mt) mitochondria. Epithelial antioxidative enzymes (AOEs) are activities of GSH-Px1 (gluathione peroxidase), (SOD) superoxide dismutase, and thioredoxine reductase (TXNRD1) by itself or with thioredoxin (Trx) are antioxidant enzymes. Glutaredoxin (Grx) are reduced by the oxidation of glutathione an antioxidant, (The effect of iridoid  glucosides such as oleuropein an antioxidant, can often be bound to glucose.) phenolic compound isothiocyanate sulforaphane found in olive leaf, increased cell-lysate NAD(P)H:quinone oxidoreductase (NQO1) phase II activities reduction reactions, catalyzed such as by glutathione-S-transferase (GST) can catalyze the conjugation back to the thiol group and other GPx mimics (converted into selenocysteine), to the reaction site of glutathione (GSH) and antioxidants, implying (GR) reduction reactions back to glutathione, are an evolutionary relationship between GST and GPx/glutathione system defense in oxidative stress. "Glutathione" peroxidase (Gpx) content, and glutathione reductase (GR) components compose the glutathione (GSH) system, this contains Selenocysteine (Sec), the 21st amino acid at the active GPX site (Homo sapiens chromosome 3, GRCh37 primary reference: rs644261)- TGA  => UGA (selenocysteine, which occurs at the active site of  glutathione peroxidase GPX1 is coded by UGA, isoform 1 NM_201397.1-variant 1 represents the shorter transcript that  encodes the longer isoform 1, as compared to isoform 2- NM_000581.2 variant 2); (rs1050450) is intronless and has a shorter C-terminus. They represent the cDNA as a molecular mechanism (TGA) for down-regulation of mRNA expression and transcriptional code is a regulatory switch at the translational-step delivered to the ribosome in genes similar to Glutathione peroxidase 1 (GP, Gpx1, GSHPX1): locus 3p13-q12 (§, ‡,). GSH-Px is an essential nutrient selenium dependent GPX, by which mRNA translational repression of selenium-binding protein (SBP1) is accomplished when GPX1 increased in human plasma, if selenium-deficient, while independent of Se values in leukocyte (White blood cells) from correspondingly damaged DNA. In fibroblast activity, GPx1 was effective through the prevention or repair of DNA damage. The reductive detoxification of peroxides in cells modulates xenobiotic metabolising enzymes via anticarcinogen supplementation, e.g. selenium-yeast  in human plasma. GPX in turn, can lead to carcinogenesis. The heterozygote has an intraerythrocytic environment (red blood cell) with the favorable higher peroxidase activities role in malarial resistance. An in-frame GCG trinucleotide repeat was homozygous for the pseudogene GPX1 Pro197Leu-like two alleles associated with 6 GCG repeats coding for a polyalanine tract. CuZn-SOD (copper/zinc-superoxide dismutase) and other oxidoreductases contribute to the cellular defenses, repair of oxidative damage to DNA. Chronic hyperglycemia (excessive blood sugar) causes oxidative stress, 'Extract silymarin and Berberine-'may' overcome insulin resistance. And for diabetes Astragalus membranaceus  can improve the protective effect, an extract from Shidagonglao roots (Mahonia fortunei)  or the effects of Berberine from the main alkaloid of Coptis chinensis  are agents for preventing sepsis and its lipopolysaccharide (LPS) complications in human microvascular endothelial cells. GPX is down-regulated and peroxiredoxin (PRX) is up-regulated. Both use thioredoxin (Gpx and Prx, suppress Trx, a cysteine-based thioredoxin-specific GPx-Txn expression.) to recharge after reducing hydrogen peroxide (H2O2) along with other cellular molecules. Also found in transcripts in ocular tissues from oxidative anterior damaged cells,  GSH-dependent recombinant human lens thioltransferase (RHLT)* being  its repair systems. GPX1 could supress staurosporine-induced late generation of ROS, corresponding to reduction in visual loss.  Its role in pathogenesis of  (inflammatory disorders of blood antioxidant enzyme system) as an autoimmune disease background, appears to be the hydroperoxide metabolism in diverse pathogens*, an enzyme by single administration streptozotocin  (60 mg/kg) of negative implication, oxidative damage or antioxidant status when examined in contrast as metabolic syndrome through the GPX down-regulation are comparable, with reduced-enzyme-activity to the T allele of the GPx-1 genetic leucine/proline polymorphism at codon 198  approximately 70% for pro197 and 30% for leu197 named Pro198Leu (rs1050450). The leucine-containing allele was less responsive to GPx-1 enzyme activity. Thioltransferase (TTase) with GPx the dethiolating enzyme, thiol* catalysis glutaredoxin thioltransferase (Grx) content and activity to the thiol status produced by the oxidation of glutathione: a seleno-organic compound ebselen  (2-phenyl-1,2-benzisoselenazol-3(2H)-one) catalyzed in vitro, has been reported to '« mimic » development of small-molecule selenium compounds' ('synthetic antioxidant' GPX)  required for, a diphenyl diselenide PhSe group 'in the catalytic activities' is introduced by reaction (a monocyte-derived soluble protein (M-DSP/Gpx1) with 5-LO, (5-lipoxygenase ) activity this 'recovered (M-DSP)-GPx inactivation'. In which Serum Malondialdehyde (MDA) a marker (oxidative activity) generated from, reactive oxygen species (ROS) is thought to cause DNA damage with various antioxidants usually homeostatically controlled by endogenous superoxide dismutase (SOD), as a by-product and the oxygen-sensor neuroglobin (Nb), GSHPx reactive neurons or in brief neuronal damage (apoptosis) after ischemia. Antioxidant enzymes such as Cu/Zn-superoxide dismutase (SOD) and a 21-kD protein (involved in neuroprotection) GPx1 both in the free radical chain, protects neurons and Microglial cells. Microglial cells are, sensitive to small changes from Reactive oxygen species (ROS), free radical scavenging enzymes-mediated apoptosis. Neuronal loss and deteriorating CNS function: is linked to the pentose phosphate shunt, the (PPP) pentose phosphate pathway, has a relatively low content of enzymatic antioxidants, in a higher cellular ROS level to oxidative stress. A candidate (SePP1) selenoprotein (P-plasma) or  genetic variations homologous to GPX1 are rapidly degraded at relative low selenium concentrations. Microsomal (reconstituted fraction) glutathione transferase-1 (hGSTP1) decreased cytotoxicity ( cartilage degradation and regeneration [Leucas aspera] to mitochondria damage, directed to citrulline- containing proteins) by effects of hydrogen peroxide 'H(2)O(2), which causes lipid peroxidation (LPO) in the (ER) endoplasmic reticulum. In which LPO product Malondialdehyde and other Thiobarbituric acid reactive substances - TBARS - are formed as a byproduct, when the effects of GPX1 ( glutathione peroxidase 1)' is measured, the effects of Centella asiatica  extract detoxifies. Antioxidants and detoxication agents as antigenotoxic* agents (isoflavones via dietary intake) were also observed as cytogenetic end-points* of carcinogenesis. Over-expression could drain the  reduced glutathione ( hepatic and GSH dependent enzymes), cellular glutathione (GSH) levels, GSH acts as a feedback rate-limiting inhibitor of its synthesizing enzyme GCL (gamma-glutamyl-cysteine synthetase) activity,  Diosgenin  is a useful Marker degradation-compound of Low-density lipoprotein (LDL) and high-density lipoprotein (HDL) against oxidation. The compound buthionine sulfoximine (BSO) inhibits the first step of glutathione synthesis, concerning the mechanism of GSH depletion. Gpx suppresses (thioredoxin) Trx - expression, which augments Anti-clastogenic (mutagenic agents), potential DNA-binding (heritable multigenerational/evolutionary tolerance), in a cDNA open reading frame (ORF) GPx1 is a small inversion (~pericentric), incorporating the co-translational selenocysteine which may be unique to the insertion sequence elements.

(Click on image to zoom)

---

      Biological Assembly GPx-1 tetrameric structure with an altered carcinogen metabolism and reduce oxygen tension to explain the anti-carcinogenic effects, the redox donor (hTXN-oxidoreductase Figure 4) status  (Figure 2) of one oxygen atom limited to only two regions may carry missense variant (rasmol_php_C and _D) a reaction incorporated into the overall tetrameric structures instability potentially in humans through modulation of biosynthetic and genetically modified GSH enzymes binding the selenocysteine insertion sequence elements. The specific activity of the enzyme Sec suggest how the molecular pathway might work, as the glutathione pathway may influence the enzyme Sec reaction site incorporation sequence in the 3'-untranslated region UTR of glutathione (GSH) may further reveal a signaling pathway that is activated. The differing and interacting roles of GPX1 and (Sec.) Selenocysteine Synthase [doi: 10.2210/rcsb_pdb/mom_2008_8] both vectorstogether with glutathione (HUMAN GLUTATHIONE TRANSFERASE (HGST) PDB ID: 1LJR ligand component GSH: C10 H17 N3 O6 S, molecules colored: aquamarine) did; activates two multiple signaling pathways in one of the Gpx1 variants 1 or 2 nucleotide, the nonsense codon, UGA has both, related to the antioxidative pathway vectors together PDB ID: 1gp1 (2-AMINO-3-SELENINO-PROPIONIC ACID: ALANINE  molecule colored: purple), is located near the selenocysteine insertion sequence element PDB ID: 2F8A (rainbow colored: ribbons) mutant of  GPX1. Interrogation of data based on experimentally determined models are limited but revealed network structures that dynamically conveyed information from the antioxidant enzymes that share a common pathway considered most important in the selenocysteine synthesis pathway from the information suggested, and they implicate at least one selenoprotein (GPx-1) in the process.

Nrf2 (NFE2L2) transport upregulation of HO-1 expression into the nucleus

Crystal structure of human heme oxygenase 1 (ho-1) in complex with its substrate heme, crystal form b
Because of the absence of the heme, the distal and proximal helices that bracket the heme plane in the holo structure move farther apart in the apo structure, thus increasing the size of the active-site pocket. PDB Structure: 1n3u the apo structure compared with the holo structure 1ni

Heme oxygenase occurs as 2 isozymes (HMOX1-2) locus: 22q12 [§§], to form biliverdin which is which is immediately reduced to/or converted to bilirubin  a intracellular source of  the essential nutrient iron, and biologic gases (O2, CO, NO, and H2S) carbon monoxide and eventually releasing iron as parts of the heme breakdown. Activator protein-1 (AP-1) is shown in other systems to regulate HO-1 expression. Biliverdin reductase (BVR) reduces heme oxygenase (HO), to bilirubin, the activity, TGF-beta has been implicated in, a variety of renal diseases. Heme oxygenase is highest in the spleen where HO-1 senescent erythrocytes support siRNA inducible apoptosis in some cancer cells the major polyphenol found in green tea, exerts antiproliferative and proapoptotic effects in many cancer cells, oxidative injury that can be ameliorated (cytoprotection) by vitamin C to pro-oxidative and pro-inflammatory insults. Curcumin by itself is a potent inducer of HO-1. Biliverdin reductase (BVR) contains a bZip domain, inhibition of HO activity by zinc protoporphyrin (ZnPP) or (inhibitors and activators) Tin-protoporphyrin (SnPP) prevented hemin-induced expression of [monocyte chemoattractant protein-1] MCP-1. Heme oxygenase HO-1 gene is quite similar in the spectrum of metal response and Iron induction kinetics to  the spectrum of  the heat shock protein 70 (HSP70) to heat shock protein HSP32 expression of human heme oxygenase-1. Andrographis paniculata increased the rate of nuclear translocation of Nrf2. A nuclear factor dimer of mammalian nuclear factor-erythroid 2-related factor 2 Nrf2 (NFE2L2) transport was shown as upregulation of HO-1 expression into the nucleus (Bach1  localized in the cytoplasm, but Nrf2 was localized in the nuclei.) and binding to a human HO-1 antioxidant response element (ARE), whereas laminar flow and high fluid shear stress are athero-protective. Atf4 an activating transcription factor bound a stress response element (StRE) sequence from Ho1, contains antioxidant-response elements that can bind the Nrf2 target gene in the signaling pathway anisotropy reveals observed in fetal transcription factors ( lipopolysaccharide (LPS) where COX-2 (include etiologic agents), plays important roles that influence suppression or overexpression of HO isoforms, an endotoxin produced by Gram negative bacteria) leading to HO-1 up-regulation and hydrogen peroxide H(2)O(2) that catalyzes the degradation of heme O(2)(*-) accumulation, leads to the shear-induced nuclear translocation of Nrf2-regulated genes such as by HO-1 and SQSTM1, upstream of MT-III. Bach1 is a basic leucine zipper protein.

Nampt restored the normal kinetics of apoptosis as an institutional isomorphism

Inhibition of NAMPT the Visfatin Gene (PBEF1) locus 7q22.2; [§§], promotes oscillation of the clock gene Per2 by releasing ‘CLOCK:BMAL1’ from suppression by SIRT1. There is a functional equivalent of PNC1 in mammals called NAMPT a longevity protein that adds stress-resistant life to the function of SIRT1. From suppression by SIRT1 in turn, the circadian transcription factor CLOCK binds to and upregulates Nampt also known as pre-B cell colony enhancing factor, thus completing a feedback loop* involving NAMPT/NAD+ and SIRT1/CLOCK:BMAL1. PBEF1 another recently characterized adipocytokine is an inflammatory cytokine that plays a requisite role in the delayed neutrophil apoptosis of sepsis. White fat comprises adipocytes and adipokines, seem to play a pro-inflammatory role in arthritis. Visfatin and apelin are novel adipocytokines elevated visfatin may be due to renal failure (per se is associated with chronic kidney disease (CKD)) and/or inflammation and induces oxidative stress, damages the blood brain barrier. Prevention of PBEF1 pre-B cell colony-enhancing factor NAMPT translation (insulin-mimetic effects) abrogated the reproducible phagocytic activity model NAMPT as the rate-limiting component (an interlocked transcriptional-enzymatic feedback loop* (NAMPT, EC 2.4.2.12) catalyzes) in the mammalian NAD (nicotinamide adenine dinucleotide) of Nampt restored the normal kinetics of apoptosis in septic polymorphonuclear Europhiles (as an institutional isomorphism [† PMID: 18272217] and Protects Them from Apoptosis) and confers resistance to oxidative stress via SIRT1-dependent “emergency” granulopoiesis axonal degeneration is an early event in the disease process Nampt activity may thus be beneficial in this chronic, aging-related condition in the salvage pathway of NAD metabolism in mammalian cells. NAMPT (visfatin), is insensitive to the physiological concentration of NAD (nicotinamide adenine dinucleotide) thus SIRT1 (sirtuin 1, silent mating type information regulation 2) activity was found to be exquisitely dependent on NAD, to prevent oxidative stress of the cells NAPRT (nicotinate phosphoribosyltransferase domain containing 1) decreased cytotoxicity by H(2)O(2). Inhibition of apoptosis by PBEF is associated with reduced activity of caspases-8 and -3, but not caspase-9, PBEF is a highly conserved 52-kDa protein is linked to the biology of visceral white adipose tissue (WAT) also aromatizes androgens to estrogens. Vistafin originally identified as a growth factor isolated from a human peripheral blood lymphocyte for early stage B cells is a new hypoxia-inducible gene (HIGD1A), two hypoxia mimetic compounds (two functional HIF responsive elements (HREs) believed to regulate seasonal physiology by decoding changes in nocturnal melatonin secretion). The expression of this gene is induced by pokeweed mitogen (PWM) and superinduced by cycloheximide, also increased visfatin mRNA levels, circulating visfatin is increased with progressive beta-cell deterioration, studied longitudinally. The lowest metazoan phylum can recognize self/nonself molecules. PBEF itself had no activity but synergized the pre-B-cell colony formation mainly transcribed in human bone marrow, liver tissue, and muscle, infected RBCs (red blood cells and other white blood cells) can make NAD biosynthetic pathways from (NA) nicotinamide. Glucose-induced elevation of visfatin was prevented by co-infusion of insulin or somatostatin. This hormone is found in the cytoplasm as well as the nucleus of cells and has been identified in many tissues and organs. Fetal development is thought to be gender specific for adiposity but not adipokinemia with slow (auto)immune attack (speculates on the existence of a maternal-placental regulatory loop (OR) values of PCOS polycystic ovary syndrome PWM prototype HNF-6/OC-1 steps required NAM for promoter chromatin remodeling) and metabolic parameters in neonates the common rs9939609 (SNP) is associated in the early stages of fat accretion in humans, as judged by serum visfatin.

Using intense methods to decrease the effect annotated SucA.

[N]eo[C]on could explain the "catch up" phenomenon in neonates and control values in several ultrastructural parameters. The quaternary structure of citrate synthase from acetate-grown Escherichia coli K12 3000. [1975]»» The dimer was the major product of an active site which was functioning as two open branches for sucA and sucB the putative E1 component Elo of KDH, instead encodes E2o components of Escherichia coli K12. single minichaperones normally requires GroEL, its co-chaperonin GroES refolded MDH in vitro, by two genes, sucC (beta subunit) and sucD (alpha subunit), which are distal genes in the sucABCD operon. Oxidizing conditions impair the chaperone activity of Hsp90 toward citrate synthase. Using a intense electrical stimulation (ES) protocol and of the following major antioxidant PRDX3 enzymes: in expression of Mn-SOD this same citrate synthase (CS) (EC 4.1.3.28) citrate synthase or glutaminase can be replaced, at least in part, by two mitogens possibly the two isozymic systems [lactate dehydrogenase (LDH) and myosin] or using a Michaelis-Menten equation, the monocarboxylate transporter proteins (MCT)-1 expression with two published subcellular subfractionation techniques, The activities of these two enzymes did not correlate with citrate synthase to those linking ATP-citrate lyase to the cholinergic system in the brain taken into account evaluated in non-synaptic (free) and synaptic mitochondria isoforms DNA enzyme activities behave quite similarly in both areas in any pharmacological study on these systems. In splenocytes this mitogen isoforms prevented much of the decrease in hexokinase activity and an increase in the production of labelled CO(2) from the oxidation of [U-(14)C]-glucose is not due to a limited H2O2 production by these isoform organelles electrons are transferred directly to molecular O2 to perform RNase protection assays on the concomitant with the enhancement of the Krebs cycle enzyme, and an increase in the activity of citrate synthase (10.1 per cent). A superficial portion of M. gastrocnemius tissue obtained before and after the diet period were analyzed to determine the activities, mixed fibre-type gastrocnemius did not affect, or was not paralleled by an increase in the ACBP [diazepam binding inhibitor] content. Exercise significantly increased oxidative capacity. Furthermore, the activities of creatine kinase, citrate synthase, cytochrome c oxidase and hexokinase were significantly higher in bioenergetics. And phosphofructokinase L the most significant changes in PGK phosphoglycerate kinase immunoreceptor loci and Germinal centers with nonrelevant specificities as Krebs-Ringer buffer especially affected the activities in glycolysis (phosphofructokinase [PFK]) from E(2) and P groups, as well as CO(2) hydration, and HK hexokinase (EC 2.7.1.1) were all elevated in term newborns suggesting the persistence of a relatively young red cell population throughout the first year of life. Similarly, CS activity was decreased, but only in olfactory bulb, these enzymes may have pathophysiological implications (e.g., decreased in energy metabolism) in childhood diseases (e.g., sudden infant death syndrome) in which hypoxia plays a role. The resulting mixture of chelated and unchelated nucleotides and tribasic acids effected coordinated control of citrate synthase, aconitase [ACO2]. The genome sequence of Mtb H37Rv , aconitase (ACO2) predicts the presence of citrate synthase has adapted its metabolism for persistence annotated as encoding SucA, maturational differences in the proximal tubule, other than Na/citrate [Cs] [renal stones] as cotransport [K+] plasma in significantly mitochondrial aconitase (m-aconitase) activity, that directly affect SLC25A1 [citrate transport]. Which may in turn favor better muscle pH regulation. Involved the mechanism for hexokinase (HK) deinhibition, fatty acyl-CoA synthetase showed also for 48 h [1975]«« should also raise cytosolic LC-CoA showed a moderate to marked increment and the kinase remained at the control values. . Major changes in the expression of CS, LDH, proteasome, caspase 3, plasminogen activators (PAs), and matrix metalloproteinase 2-9 (MMP2-9) had any effect on CS or structurally related compounds on glutamate dehydrogenase [GDH] activity were observed upon serum stimulation, that MMP+ may represent an additional mechanism contributing to mitochondrial dysfunction, but no age-related difference was noted.

From Minichaperone to GroEL 2: Importance of Avidity of the Multisite Ring Structure,

by: Jean Chatellier, Fergal Hill, Alan R Fersht,

Journal of Molecular Biology pp. 304, 883 (2000). info pmid/11124034 | info doi:10.1006/jmbi.2000.4277 | [§§].

The YFH1-delta iron sulphur center divalent metal transporter domains.

E. coli, assembles into a stable homopolymer (a common theme) that can bind approximately 10 atoms of iron per molecule of (FRDA GENE X25 OMIM-606829 locus 9q13) frataxin transformation suggested by others to be a mitochondrial ferritin induced by ROS [1.] reactive oxygen species divalent metal transporters in at least 2 cell types proportional to the size of the smaller GAA repeat allele. Iron accumulation in FRDA mitochondria appeared to be a late consequence in Fe/S proteins apoptosis pathway yeast maturation components in most Eukarya suggests similar cytosolic iron-regulatory transporter protein mechanisms for cytosolic ISC biogenesis in the role of oxidative stress associated with FRDA frataxin deficiency (ISC) biosynthetic pathway involved in the Fas/TNF/INF apoptosis (yeast frataxin homolog, YFH1 reduces function) YHF1 (606829.0005) assembly of regular spherical homopolymer multimerscan sequester more than 3,000 atoms of iron mutation; affected protein processing resulted in severe mature frataxin deficiency in mammalian or yeast mitochondrial iron accumulation does not induce oxidative stress. Testing the clear cell cAMP bacterial resistance cofactor MPP(+) caused I151F (606829.0004) and G127V (606829.0005), to modulate interaction with MPP-beta to the Fe-S cluster scaffold protein to form large molecular assemblies that store Fe(III) as physiologically relevant form(s) and ferrochelatase (see 177000) deficiency in delta-yfh1 cells and (iii) the glutathione peroxidase gene [1.] that prevents an increase in mutation rates, which is cleaved by the reconstituted MPP heterodimer resulting in a slower maturation process and enhanced (ACO2; 100850) resistance to H2O2 exposure. The second cleaved domain I or (domain II), consisting of YFH1 protein failed to attain appreciable steady-state amounts in mitochondria of the YFH1-delta mutant, the absence of frataxin in yeast leads to nuclear damage the gene (GPX1; 138320) [1.] that prevents an increase in mutation rates, biosynthesis of cellular Fe/S proteins (iron-sulphur centres) an iron-starvation cofactor (in non photochemical quenching NPQ in domains III, II, and I can up-regulate MMP-2 [Mmp2] mTOR synthesis as an Fe in an S mode footprint [3Fe-4S](+)) which excluded most of the previously suggested functions (30 PubMed Neighbors) which may be seen as secondary to defects. Suggest that frataxin can use different molecular forms of oxidatively inactivated [3Fe-4S] to accomplish its functions.

Yfh1 mediates iron use by ferrochelatase(+) (see 177000) representative of the disease state in the FXN gene Friedreich ataxia mitochondrial 'petite' phenotype mutants mtDNA as a result of of two hypervariable regions however, predicted it aids ferrochelatase transcriptional repression by the expansion of a polymorphic and unstable GAA triplet repeat effects in Delta-yfh1 mutational cellular antioxidant defense rates, triggered associated with a decrease found that lower aconitase (100850) activity can undergo conversion to the active [4Fe-4S]2+ form of the protein in complexes I, II and III, and the number of GAA repeats (and particularly that of the smaller of each pair of alleles) different from that found with STM7 exon pseudogenes other triplet diseases to be identified STM7 (with a questionable role in FXN) in the X25 gene for a G130V missense mutation. Related to the size of the expanded repeat: the smaller of the 2 expanded alleles in the X25/exon 1 from the 3-prime end of STM7/exon 16 fulfilled the requirents for the untranslated (177000) ataxia-telangiectasia gene (607585) IscU- AMELX-Fas deficient cells, only rescues cells non-committed (GPX1; 138320) to the neuronal lineage footprinting, and are alleviated by and related to free radical independent signaling pathways.

Supramolecular Assemblies of Human Frataxin are Formed via Subunit–Subunit Interactions Mediated by a Non-conserved Amino-terminal Region.

Heather O'Neill, Oleksandr Gakh, and Grazia Isaya

Journal of Molecular Biology 345 (3), 433-9 (21 Jan 2005)

info:pmid/15581888 | info:doi/10.1016/j.jmb.2004.10.074; [§§]:|:[§§].