Apoprotein can refer to Apoenzyme Cofactors 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
APOE may refer to Apolipoprotein E , a main apoprotein of the chylomicron, also studied for its involvement in Alzheimer s Disease risk. Professional Oklahoma Educators , an organization in Oklahoma formerly known as the Association of Professional Oklahoma Educators or APOE. disambig ... more details
Unreferenced date December 2009 Orphan date December 2009 A Holoprotein or conjugated protein 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 approximately 1 of the population. ref name Boman1975 Boman H,Hazzard WR, AlbersJJ, et ah Frequency of monogenic forms of hyperlipidemia in a normal population. AmJ ttum Genet 27 19A,1975. http www.ncbi.nlm.nih.gov pmc articles PMC1762895 pdf ajhg00439 0130.pdf ref 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 Category Lipid metabolism disorders ... 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 Lipidemias Deficiencies of intracellular signaling peptides and proteins pl Zesp chylomikronemii ... more details
wiktionarypar apo apo Apo or APO may refer to African Press Organization Acting Pilot Officer , the lowest commissioned grade in the Royal Air Force Pulmonary edema Acute Pulmomary Oedema , fluid accumulation on the lungs African Political Organization , a Coloured political organization in early twentieth century South Africa Alpha Phi Omega , a U.S. service fraternity Apo, a god of mountains in Inca mythology Serok Apo or Abdullah calan, Kurdistan Workers Party leader Apochromat , a type of photographic or other lens Apolipoprotein Apoprotein , a protein without its bound cofactor Apotex , Canadian pharmaceutical company, producer of generic drugs Application Performance Optimization Army Post Office chiefly U.S. Army and U.S. Air Force postal services. Also See military mail Association for Professional Observers , an association of fisheries observers lang de Au erparlamentarische Opposition , a political protest movement in West Germany during the 1960s and 1970s Authorized Personnel Only , a fictional black ops unit on Alias After Peak oil Peak Oil , an epoch used in dating years following the estimated Peak of Global Oil Production Places Apo Island , a volcanic island in the Philippines Mount Apo , a stratovolcano on the island of Mindanao in the Philippines Kara River or Apo, a tributary of the Danube in the Banat region of Serbia and Romania Apo eup , an Eup administrative division eup in Gimcheon, Gyeongsangbuk do, central South Korea Apache Point Observatory , an observatory in the Sacramento Mountains in Sunspot, New Mexico, U.S. Music Auckland Philharmonia Orchestra Armenian Philharmonic Orchestra APO Hiking Society , a Filipino singing group Aldworth Philharmonic Orchestra , the orchestra of Reading Blue Coat School Trivia Reading Blue Coat School See also Apolipoprotein , lipid binding protein APU disambiguation disambig cs APO de APO Begriffskl rung es APO eo APO fr APO it APO nl Apo ja APO pl APO pt Apo ro APO sv APO tl Apo ... more details
Infobox Disease Name Lipoprotein lipase deficiency Image Caption DiseasesDB 4697 ICD10 ICD10 E 78 e 78 ICD9 ICDO OMIM 238600 MedlinePlus 000408 eMedicineSubj eMedicineTopic MeshID D008072 GeneReviewsID lpl GeneReviewsName Familial Lipoprotein Lipase Deficiency Lipoprotein lipase deficiency also known as chylomicronemia, , ref name Andrews 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 and hyperlipoproteinemia type Ia ref http omim.org entry 238600 OMIM entry 238600 last updated 03 18 2004 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 Lipid metabolism disorders Category Lipid metabolism disorders Category Skin conditions resulting from errors in metabolism disease stub nl Lipoprote ne lipase defici ntie ... more details
amino acid apoprotein Disambiguation needed date July 2011 to which the chromophore is tightly ... is a very potent DNA damaging agent it is very labile and the role of the apoprotein is to protect ... more details
Leghemoglobin also leghaemoglobin or legoglobin is a nitrogen or oxygen carrier, because naturally occurring oxygen and nitrogen interact similarly with this protein and a hemoprotein found in the Nitrogen fixation nitrogen fixing root nodules of legume leguminous plants. It is produced by legumes in response to the roots being infected by nitrogen fixing bacteria, termed 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 holoprotein protein heme cofactor is widely 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 There is some evidence however suggesting 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. Leghemogl ... more details
, niacin , and fibric acids . Apo B is an integral apoprotein whereas the others are peripheral apoproteins. References reflist See also Apolipoprotein L Apoprotein External links http www.ncbi.nlm.nih.gov ... more details
Infobox protein family Symbol Flavoprotein Name Flavoprotein image PDB 1e20 EBI.jpg width caption the fmn binding protein athal3 Pfam PF02441 Pfam clan InterPro IPR003382 SMART PROSITE MEROPS SCOP 1e20 TCDB OPM family OPM protein CAZy CDD 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 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 Apoenzyme apoprotein and a bright yellow pigment. Neither apoprotein nor pigment alone could catalyse the oxidation of NADH , but mixing of the two restored the enzy ... 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 image malcolmdixon.jpg 175px image size 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 David E. Green 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 enzyme kinetics 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 wa ... more details
Orphan date July 2011 enzyme Name holocytochrome c synthase EC number 4.4.1.17 CAS number 75139 03 6 IUBMB EC number 4 4 1 17 GO code 0004408 image width caption Infobox protein family Symbol Cyto heme lyase Name Cytochrome c c1 heme lyase image width caption Pfam PF01265 Pfam clan InterPro IPR000511 SMART PROSITE PDOC00647 MEROPS SCOP TCDB OPM family OPM protein CAZy CDD In enzymology , a holocytochrome c synthase EC number 4.4.1.17 is an enzyme that catalysis catalyzes the chemical reaction holocytochrome c math rightleftharpoons math apocytochrome c heme Hence, this enzyme has one substrate biochemistry substrate , holocytochrome c , and two product chemistry products , apocytochrome c and heme . This enzyme belongs to the family of lyase s, specifically the class of carbon sulfur lyases. The systematic name of this enzyme class is holocytochrome c apocytochrome c lyase heme forming . Other names in common use include cytochrome c heme lyase , holocytochrome c synthetase , and holocytochrome c apocytochrome c lyase . This enzyme participates in porphyrin and chlorophyll metabolism . Cytochrome c haem lyase CCHL and cytochrome Cc1 haem lyase CC1HL are mitochondrion mitochondrial enzyme s that catalyse the covalent attachment of a haem group on two cysteine residues of cytochrome c and c1. These two enzymes are functionally and evolution evolutionary related. There are two conserved sequence conserved regions, the first is located in the central section and the second in the C terminal section. Both patterns contain conserved histidine , tryptophan and acidic residues which could be important for the interaction of the enzymes with the apoprotein s and or the haem group. ref name pmid1499554 cite journal author Zollner A, Rodel G, Haid A title Molecular cloning and characterization of the Saccharomyces cerevisiae CYT2 gene encoding cytochrome c1 heme lyase journal Eur. J. Biochem. volume 207 issue 3 pages 1093 100 year 1992 month August pmid 1499554 doi 10.1111 j.1 ... more details
PBB geneid 79135 Infobox protein family Symbol ApoO Name ApoO image width caption Pfam PF09769 Pfam clan InterPro IPR019166 SMART PROSITE MEROPS SCOP TCDB OPM family OPM protein CAZy CDD Apolipoprotein O also known as protein FAM121B is a protein that in humans is encoded by the APOO gene . APOO is a member of the apolipoprotein family. ref name pmid16956892 cite journal author Lamant M, Smih F, Harmancey R, Philip Couderc P, Pathak A, Roncalli J, Galinier M, Collet X, Massabuau P, Senard JM, Rouet P title ApoO, a novel apolipoprotein, is an original glycoprotein up regulated by diabetes in human heart journal J. Biol. Chem. volume 281 issue 47 pages 36289 302 year 2006 month November pmid 16956892 doi 10.1074 jbc.M510861200 ref The human, apolipoprotein O is a 198 amino acid s protein that contains a 23 amino acids long signal peptide . The apoprotein is secreted by a microsome microsomal triglyceride transfer protein MTTP dependent mechanism, probably as a VLDL associated protein that is subsequently transferred to high density lipoprotein HDL . Apolipoprotein O is the first chondroitin sulphate chondroitine sulphate polymer chain containing apolipoprotein. ref name pmid16956892 cite journal author Lamant M, Smih F, Harmancey R, Philip Couderc P, Pathak A, Roncalli J, Galinier M, Collet X, Massabuau P, Senard JM, Rouet P title ApoO, a novel apolipoprotein, is an original glycoprotein up regulated by diabetes in human heart journal J. Biol. Chem. volume 281 issue 47 pages 36289 302 year 2006 month November pmid 16956892 doi 10.1074 jbc.M510861200 url ref Apolipoproteins are proteins that binds to lipids. Members of this family promote cholesterol efflux from macrophage cells. They are present in various lipoprotein complexes, including high density lipoprotein HDL , low density lipoprotein LDL and very low density lipoprotein VLDL . References reflist Further reading refbegin 2 cite journal author Talmud PJ, Drenos F, Shah S, et al. title Gene centric association s ... 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
lipoprotein lipase and reduces apoprotein CIII, which increases lipolysis and elimination of triglyceride ... density lipoprotein VLDL and low density lipoprotein LDL containing apoprotein B, and increases high density lipoprotein HDL containing apoprotein AI and AII. In addition, by reducing the synthesis ... more details
. It is located in the thylakoid membrane of the chloroplast and it is composed of an apoprotein ... jbc.M109.008912 ref This is believed to destabilize the complex, at which point breakdown of the apoprotein occurs. An important enzyme in the breakdown of the apoprotein is FtsH6, which belongs to the FtsH ... 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, bound to the proteins, which allow fats to move through the water outside cells and inside cells. The proteins serve to emulsify the lipid otherwise called fat molecules. 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 that cells use both to control internal water content and 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 make 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 a with 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 ... more details
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