Apoprotein can refer to Apoenzyme , the protein part of an enzyme without its characteristic prosthetic group . Apolipoprotein , a lipid binding protein that is a constituent of the plasma lipoprotein . disambig ja ... more details
Familial apoprotein CII deficiency is a condition caused by a lack of lipoprotein lipase activator. ref name Andrews cite book author James, William D. Berger, Timothy G. et al. title Andrews Diseases of the Skin clinical Dermatology publisher Saunders Elsevier location year 2006 pages isbn 0 7216 2921 0 oclc doi accessdate ref rp 533 See also Primary hyperlipoproteinemia Lipoprotein lipase deficiency Skin lesion References reflist Lipid metabolism disorders Cutaneous condition stub Category Skin conditions resulting from errors in metabolism ... more details
APOE may refer to Apolipoprotein E , a main apoprotein of the chylomicron. Professional Oklahoma Educators , an organization in Oklahoma formerly known as the Association of Professional Oklahoma Educators or APOE. disambig ... more details
Unreferenced stub auto yes date December 2009 Orphan date December 2009 Holoprotein is an apoprotein combined with its prosthetic group . Category Proteins Protein stub es Holoprote na fr Holoprot ine pt Holoprote na ... more details
Familial hypertriglyceridemia is an autosomal dominant condition occurring in 1 2 of the population. Triglyceride levels, but not cholesterol, are elevated as a result of excess hepatic production of VLDL or heterozygous LPL deficiency. Unlike familial hypercholesterolemia, there is no association with premature coronary disease. However, affected individuals are at risk for chylomicronemia syndrome, characterized by elevated chylomicrons in the blood. See also Primary hyperlipoproteinemia Familial apoprotein CII deficiency Skin lesion References reflist Lipid metabolism disorders Cutaneous condition stub Category Skin conditions resulting from errors in metabolism ... more details
Infobox disease Name Chylomicron retention disease Image Caption DiseasesDB 33188 ICD10 ICD9 ICDO OMIM 246700 MedlinePlus eMedicineSubj eMedicineTopic MeshID Chylomicron retention disease is a disorder of fat absorption. ref name pmid3792776 cite journal author Roy CC, Levy E, Green PH, et al. title Malabsorption, hypocholesterolemia, and fat filled enterocytes with increased intestinal apoprotein B. Chylomicron retention disease journal Gastroenterology volume 92 issue 2 pages 390 9 year 1987 month February pmid 3792776 doi url ref It is associated with SAR1B . ref name pmid12692552 cite journal author Jones B, Jones EL, Bonney SA, et al. title Mutations in a Sar1 GTPase of COPII vesicles are associated with lipid absorption disorders journal Nat. Genet. volume 34 issue 1 pages 29 31 year 2003 month May pmid 12692552 doi 10.1038 ng1145 ref References reflist Category Diseases and disorders medicine stub Deficiencies of intracellular signaling peptides and proteins pl Zesp chylomikronemii ... more details
drugs statins , niacin ,and fibric acids . Apo B is an integral apoprotein whereas the others are peripheral apoproteins. See also Apolipoprotein L Apoprotein External links http www.ncbi.nlm.nih.gov ... more details
Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin the flavin adenine dinucleotide FAD or flavin mononucleotide FMN . Flavoproteins are involved in a wide array of biological processes, including, but by no means limited to, bioluminescence , removal of Radical chemistry radicals contributing to oxidative stress, photosynthesis , DNA repair , and apoptosis . The spectroscopic properties of the Flavin group flavin cofactor make it a natural reporter for changes occurring within the active site this makes flavoproteins one of the most studied enzyme families. Discovery The first mention of a flavoprotein in the scientific literature dates back to 1879, when the work on the composition of cow s milk resulted in the isolation of a bright yellow pigment , that we now know as Flavin group flavin , but termed lactochrome at the time. By the early 1930s, this same pigment had been isolated from a range of sources, and recognised as a component of the vitamin B complex . Its structure was determined almost simultaneously by two groups in 1934, and given the name riboflavin , derived from the ribityl side chain and yellow colour of the conjugated ring system. ref name Massey Massey, V. 2000 The chemical and biological versatility of riboflavin, Biochem. Soc. Trans. 28, 283 296. ref The first evidence for the requirement of Flavin group flavin as an enzyme cofactor biochemistry cofactor came in 1935. Hugo Theorell and coworkers showed that a bright yellow coloured yeast protein , identified previously as essential for cellular respiration , could be separated into apoprotein and a bright yellow pigment. Neither apoprotein nor pigment alone could catalyse the oxidation of NADH , but mixing of the two restored the enzyme activity. However, replacing the isolated pigment with riboflavin did not restore enzyme activity, despite their being indistinguishable under spectroscopy . This led to the discovery that the protein studied required not riboflavin ... more details
acid apoprotein to which the chromophore is tightly and non covalent bond covalently bound with high ... labile and the role of the apoprotein is to protect it and release it to the target DNA. Opening ... more details
Infobox Disease Name PAGENAME Image Caption DiseasesDB 4697 ICD10 ICD10 E 78 e 78 ICD9 ICDO OMIM 238600 MedlinePlus 000408 eMedicineSubj eMedicineTopic MeshID D008072 Lipoprotein lipase deficiency also known as chylomicronemia, ref name Andrews and chylomicronemia syndrome ref name Bolognia cite book author Rapini, Ronald P. Bolognia, Jean L. Jorizzo, Joseph L. title Dermatology 2 Volume Set publisher Mosby location St. Louis year 2007 pages isbn 1 4160 2999 0 oclc doi accessdate ref is caused by a mutation in the gene which codes lipoprotein lipase . ref name Andrews cite book author James, William D. Berger, Timothy G. et al. title Andrews Diseases of the Skin clinical Dermatology publisher Saunders Elsevier location year 2006 pages isbn 0 7216 2921 0 oclc doi accessdate ref rp 533 . As a result, afflicted individuals lack the ability to produce lipoprotein lipase enzymes necessary for effective breakdown of fatty acids. See also Primary hyperlipoproteinemia Familial apoprotein CII deficiency List of cutaneous conditions References reflist External links http www.genetests.org profiles lpl index.html GeneReviews Familial Lipoprotein Lipase Deficiency http ghr.nlm.nih.gov condition familiallipoproteinlipasedeficiency Genetic Home Reference Lipid metabolism disorders disease stub Category Cardiology Category Lipid disorders Category Skin conditions resulting from errors in metabolism nl Lipoprote ne lipase defici ntie ... more details
Leghemoglobin also leghaemoglobin or legoglobin is an nitrogen or oxygen carrier, because naturally occurring oxygen and nitrogen look the same to this protein and a hemoprotein found in the Nitrogen fixation nitrogen fixing root nodules of legume leguminous plants. But nitrogen is need for the cycle to occur. It is produced by legumes in response to the roots being infected by nitrogen fixing bacteria, called rhizobia , as part of the symbiosis symbiotic interaction between plant and bacterium roots uninfected with Rhizobium do not synthesise leghemoglobin. Leghemoglobin has close chemical and structural similarities to hemoglobin , and, like hemoglobin, is red in colour. The protein was believed to be a product of both plant and the bacterium in which the apoprotein is produced by the plant and the heme an iron atom bound in a porphyrin ring is produced by the bacterium . ref cite journal author O Brian, M. R., Kirshbom, P. M., & Maier, R. J. title Bacterial heme synthesis is required for expression of the leghemoglobin holoprotein but not the apoprotein in soybean root nodules journal Proc. Nat. Acad. Sci. USA volume 84 issue 23 pages 8390&ndash 8393 year 1987 url http www.pnas.org content 84 23 8390 doi 10.1073 pnas.84.23.8390 pmid 3479799 pmc 299548 ref Newer findings however, indicate that the heme moiety is also produced by the plant. ref cite journal author Santana, M. A., Pihakaski Maunsbach, K., Sandal, N., Marcker, K. A., & Smith, A. G. title Evidence that the plant host synthesizes the heme moiety of leghemoglobin in root nodules journal Plant Physiol. volume 116 issue 4 pages 1259&ndash 1269 year 1998 url http www.plantphysiol.org cgi content full 116 4 1259 doi 10.1104 pp.116.4.1259 pmid 9536042 pmc 35032 ref In plants infected with Rhizobium , such as alfalfa or soybean s , the presence of oxygen in the root nodules would reduce the activity of the oxygen sensitive nitrogenase an enzyme responsible for the fixation of atmospheric nitrogen. Leghemoglob ... more details
For the rugby league footballer of the 1960s and 70s for Great Britain, England, Yorkshire, and Featherstone Rovers, see Malcolm Dixon rugby league Malcolm Mal Dixon Infobox Scientist name Malcolm Dixon box width 300px image malcolmdixon.jpg 175px image width 175px caption Malcolm Dixon 1899 1985 birth date 18 April 1899 birth place Cambridge , UK death date death date and age 1985 12 7 1899 4 18 df y death place Cambridge, UK residence UK nationality United Kingdom British ethnicity field Biochemistry work institutions University of Cambridge alma mater University of Cambridge doctoral advisor Frederick Hopkins doctoral students known for author abbrev bot author abbrev zoo prizes religion Anglican footnotes Malcolm Dixon 18 April 1899 7 December 1985 was a British biochemist. He was born in Cambridge, UK to Allick Page and Caroline Dewe n e Mathews Dixon. ref http www.jstor.org pss 770048 ref He received his PhD in 1925, under Frederick Hopkins Frederick Gowland Hopkins at the University of Cambridge . He studied physical biochemistry , especially the purification of enzymes and the kinetics of enzyme catalyzed reactions. He studied the oxidation of glutathione and other thiols by molecular oxygen and measured the redox potential of the thiol disulfide system, also establishing that the oxidation of glutathione was catalyzed by trace metals. He investigated xanthine oxidase, and thereby established many aspects of the chemistry of dehydrogenases. He showed that the hydrogen peroxide formed in the reaction of xanthine oxidase with molecular oxygen inactivated the enzyme and that the inhibition could be relieved by the addition of catalase, thus helping to establish a biochemical role for the latter enzyme. Dixon published a series of papers on D amino acid oxidase , detailing the kinetics and thermodynamics of association of the coenzyme with the apoprotein , the substrate and inhibitor specificity, and the effect of pH on the kinetic constants. He was an expert on ... more details
chembox verifiedrevid 396492132 ImageFile1 Heme b.svg ImageSize1 130px IUPACName OtherNames Section1 Chembox Identifiers ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 16739950 InChI 1 C34H34N4O4.Fe c1 7 21 17 3 25 13 26 19 5 23 9 11 33 39 40 31 37 26 16 32 24 10 12 34 41 42 20 6 28 38 32 15 30 22 8 2 18 4 27 36 30 14 29 21 35 25 h7 8,13 16H,1 2,9 12H2,3 6H3, H4,35,36,37,38,39,40,41,42 q 2 p 2 b25 13 ,26 13 ,27 14 ,28 15 ,29 14 ,30 15 ,31 16 ,32 16 rC34H32FeN4O4 c1 7 21 17 3 25 13 29 20 6 24 10 12 34 42 43 32 16 28 23 9 11 33 40 41 18 4 26 37 28 14 31 22 8 2 19 5 30 15 27 21 36 25 38 31 35 39 29 32 h7 8,13 16H,1 2,9 12H2,3 6H3, H,40,41 H,42,43 b25 13 ,26 14 ,27 15 ,28 16 ,29 13 ,30 15 ,31 14 ,32 16 InChIKey KABFMIBPWCXCRK SMDPYJEOBB StdInChI Ref stdinchicite correct chemspider StdInChI 1S C34H34N4O4.Fe c1 7 21 17 3 25 13 26 19 5 23 9 11 33 39 40 31 37 26 16 32 24 10 12 34 41 42 20 6 28 38 32 15 30 22 8 2 18 4 27 36 30 14 29 21 35 25 h7 8,13 16H,1 2,9 12H2,3 6H3, H4,35,36,37,38,39,40,41,42 q 2 p 2 b25 13 ,26 13 ,27 14 ,28 15 ,29 14 ,30 15 ,31 16 ,32 16 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey KABFMIBPWCXCRK RGGAHWMASA L CASNo Ref cascite correct CAS CASNo 14875 96 8 PubChem 444098 SMILES OC O CC C6 C C C 3 N C6 C C2 C CCC O O C C C1 C C5 N C C c4n Fe N12 c C 3 c C C c4C C C C C5 C MeSHName Heme b Section2 Chembox Properties Formula C sub 34 sub H sub 32 sub O sub 4 sub N sub 4 sub Fe MolarMass 616.487 Appearance Density MeltingPt BoilingPt Section3 Chembox Hazards Solubility MainHazards FlashPt Autoignition Heme B is the most abundant heme , both hemoglobin and myoglobin are examples of oxygen transport proteins that contain heme B. The peroxidase family of enzymes also contain heme B. The COX 1 and COX 2 enzymes cyclooxygenase of recent fame, also contain heme B at one of two active sites. Generally, heme B is attached to the surrounding protein matrix known as the apoprotein through a single coordination bond between the heme iro ... more details
ApoA 1 Milano also ETC 216 , now MDCO 216 is a naturally occurring genetic mutation mutated variant of the apolipoprotein A1 protein found in human high density lipoprotein HDL , the lipoprotein particle that carries cholesterol from tissues to the liver and is associated with protection against cardiovascular disease . ApoA1 Milano was first identified by Dr. Cesare Sirtori in Milan , who also demonstrated that its presence significantly reduced cardiovascular disease , even though it caused a reduction in HDL levels and an increase in triglyceride levels. ref name pmid7430351 cite journal author Franceschini G, Sirtori CR, Capurso A, Weisgraber KH, Mahley RW title A IMilano apoprotein. Decreased high density lipoprotein cholesterol levels with significant lipoprotein modifications and without clinical atherosclerosis in an Italian family journal J. Clin. Invest. volume 66 issue 5 pages 892 900 year 1980 pmid 7430351 doi 10.1172 JCI109956 url http www.jci.org articles view 109956 pdf format PDF pmc 371523 PMC 371523 ref Discovery Discovered by accident, the mutation was found to be present in about 3.5 of the population of Limone sul Garda , a small village in northern Italy . It has been traced to a mutation in a single man, Giovanni Pomarelli ref Drug for Heart Disease Called Breakthrough, Los Angeles Times , November 5, 2003 ref , who lived in the village in the 18th century and passed it on to his offspring. ref name pmid3936350 cite journal author Gualandri V, Franceschini G, Sirtori CR, et al. title AIMilano apoprotein identification of the complete kindred and evidence of a dominant genetic transmission journal Am. J. Hum. Genet. volume 37 issue 6 pages 1083 97 year 1985 pmid 3936350 pmc 1684746 PMC 1684746 ref It is characterized by the replacement of a single amino acid at R173C. ref name pmid6401735 cite journal author Weisgraber KH, Rall SC, Bersot TP, Mahley RW, Franceschini G, Sirtori CR title Apolipoprotein A IMilano. Detection of normal A I in affect ... more details
PBB geneid 4547 Microsomal triglyceride transfer protein large subunit is a protein that in humans is encoded by the MTTP gene . ref name pmid8111381 cite journal author Shoulders CC, Brett DJ, Bayliss JD, Narcisi TM, Jarmuz A, Grantham TT, Leoni PR, Bhattacharya S, Pease RJ, Cullen PM, et al. title Abetalipoproteinemia is caused by defects of the gene encoding the 97 kDa subunit of a microsomal triglyceride transfer protein journal Hum Mol Genet volume 2 issue 12 pages 2109 16 year 1994 month Mar pmid 8111381 pmc doi 10.1093 hmg 2.12.2109 ref ref name entrez cite web title Entrez Gene MTTP microsomal triglyceride transfer protein url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 4547 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text MTP encodes the large subunit of the heterodimeric microsomal triglyceride transfer protein. Protein disulfide isomerase PDI completes the heterodimeric microsomal triaglyceride transfer protein, which has been shown to play a central role in lipoprotein assembly. Mutations in MTP can cause abetalipoproteinemia . ref name entrez cite web title Entrez Gene MTTP microsomal triaglyceride transfer protein url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 4547 accessdate ref Apoprotein B48 on chylomicra and Apoprotein B100 on LDL, IDL, and VLDL are important for MTP binding. Interactive pathway map StatinPathway WP430 highlight Microsomal triglyceride transfer protein References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Luz JM, Lennarz WJ title Protein disulfide isomerase a multifunctional protein of the endoplasmic reticulum. journal EXS volume 77 issue pages 97 117 year 1996 pmid 8856971 doi cite journal author Wetterau JR, Lin MC, Jamil H title Microsomal triaglyceride transfer protein. journal Biochim. Biophys. A ... more details
of apoprotein CIII. Activation of PPAR also induces an increase in the synthesis of apoproteins ... lipoprotein low density fractions VLDL and LDL containing apoprotein B and an increase in the high density lipoprotein fraction HDL containing apoprotein AI and AII. In addition, through modulation ... more details
Image Chylomicron.svg thumb 250px Lipoprotein structure chylomicron br ApoA, ApoB, ApoC, ApoE apolipoprotein s T triacylglycerol C cholesterol green phospholipid s A lipoprotein is a biochemistry biochemical assembly that contains both protein s and lipid s water bound to the proteins. Many enzyme s, transporter s, structural proteins, antigen s, adhesin s and toxin s are lipoproteins. Examples include the High density lipoprotein high density HDL and Low density lipoprotein low density LDL lipoproteins which enable fats to be carried in the blood stream, the transmembrane protein s of the mitochondrion and the chloroplast , and bacterial lipoproteins. ref http www.mrc lmb.cam.ac.uk genomes dolop mrc lmb.cam.ac.uk ref Function The function of lipoprotein particles is to transport lipids fats such as triacylglycerol around the body in the blood. All cell biology cell s use and rely on fat s and cholesterol as building blocks to create the multiple cell membrane membrane s which cells use to both control internal water content, internal water soluble elements and to organize their internal structure and protein enzymatic systems. The lipoprotein particles have hydrophilic groups of phospholipids, cholesterol and apoproteins directed outward. Such characteristics makes them soluble in the salt water based blood pool. Triglyceride fats and cholesterol esters are carried internally, shielded from the water by the phospholipid monolayer and the apoprotein s. The interaction of the proteins forming the surface of the particles with a enzymes in the blood, b with each other, and c with specific proteins on the surfaces of cells determine whether triglycerides and cholesterol will be added to or removed from the lipoprotein transport particles. Regarding atheroma development and progression as opposed to regression, the key issue has always been cholesterol transport patterns, not cholesterol concentration itself. Citation needed date May 2010 Transmembrane lipoproteins The ... more details
PBB geneid 1548 Cytochrome P450 2A6 abbreviated CYP2A6 is a member of the cytochrome P450 mixed function oxidase system, which is involved in the metabolism of xenobiotic s in the body. CYP2A6 is the primary enzyme responsible for the oxidation of nicotine and cotinine . It is also involved in the metabolism of several pharmaceuticals, carcinogens, and a number of coumarin type alkaloids. CYP2A6 is the only enzyme in the human body that appreciably catalyzes the 7 hydroxylation of coumarin , such that the formation of the product of this reaction, 7 hydroxycoumarin, is used as a probe for CYP2A6 activity. The CYP2A6 gene is part of a large cluster of cytochrome P450 genes from the CYP2A, CYP2B and CYP2F subfamilies on chromosome 19q. The gene was formerly referred to as CYP2A3 however, it has been renamed CYP2A6. ref cite web title Entrez Gene CYP2A6 cytochrome P450, family 2, subfamily A, polypeptide 6 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 1548 accessdate ref Interactive pathway map FluoropyrimidineActivity WP1601 highlight CYP2A6 Distribution CYP2A6 localizes to the endoplasmic reticulum and is found predominantly in the liver. Variability Significant interindividual variability in CYP2A6 apoprotein and mRNA levels has been observed. Induction CYP2A6 is known to be Enzyme induction and inhibition inducible by phenobarbital and rifampicin , and it is suspected that other antiepileptic drugs may also have this effect. CYP2A6 Ligands class wikitable width 100 Selected inducers, inhibitors and substrates of CYP2A6 Substrates Inhibitors Inducers style vertical align top Many Carcinogen s MNAN NNK procarcinogen N Nitrosodiethylamine NDEA carcinogen MTBE carcinogen Other toxin s aflatoxin B sub 1 sub mycotoxin 1,3 butadiene in synthetic rubber coumarin DCBN herbicide 7 ethoxycoumarin test substrate skatole quinoline 4,4 methylene bis 2 chloroaniline MOCA in polyurethane production halothane anaesthetic losigamone anticonvulsan ... more details
PBB geneid 344 Apolipoprotein C2 or Apolipoprotein C II is a protein that in humans is encoded by the APOC2 gene . The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text The protein encoded by this gene is secreted in plasma where it is a component of very low density lipoprotein s and chylomicron s. This protein activates the enzyme lipoprotein lipase in capillaries ref name pmid16314153 cite journal author Kim SY, Park SM, Lee ST title Apolipoprotein C II is a novel substrate for matrix metalloproteinases journal Biochem. Biophys. Res. Commun. volume 339 issue 1 pages 47 54 year 2006 pmid 16314153 doi 10.1016 j.bbrc.2005.10.182 ref , which hydrolyzes triglycerides and thus provides free fatty acid s for cells. Mutations in this gene cause Familial apoprotein CII deficiency hyperlipoproteinemia type IB , characterized by hypertriglyceridemia , xanthoma s, and increased risk of pancreatitis and early atherosclerosis . ref name entrez cite web title Entrez Gene APOC2 apolipoprotein C II url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 344 accessdate ref Interactive pathway map StatinPathway WP430 highlight APOC2 See also Apolipoprotein C References reflist refbegin 2 PBB Further reading citations cite journal author Jackson RL, Baker HN, Gilliam EB, Gotto AM title Primary structure of very low density apolipoprotein C II of human plasma. journal Proc. Natl. Acad. Sci. U.S.A. volume 74 issue 5 pages 1942 5 year 1977 pmid 194244 doi 10.1073 pnas.74.5.1942 pmc 431048 cite journal author Lycksell PO, Ohman A, Bengtsson Olivecrona G, et al. title Sequence specific 1H NMR assignments and secondary structure of a carboxy terminal functional fragment of apolipoprotein CII. journal Eur. J. Biochem. volume 205 issue 1 pages 223 31 year 1992 pmid 1555583 doi 10.1111 j.1432 1033.1992.tb16772.x cite journal author Hegele RA, Connelly PW, Maguire GF ... more details
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