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 Citation needed date October 2011 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 an ... more details
Context date November 2009 chembox verifiedrevid 404478338 ImageFile Heme c.svg ImageSize 250px IUPACName OtherNames Section1 Chembox Identifiers CASNo 26598 29 8 PubChem 444125 SMILES MeSHName heme C Section2 Chembox Properties Formula C sub 34 sub H sub 36 sub O sub 4 sub N sub 4 sub S sub 2 sub Fe MolarMass 684.651 g mol Appearance Density MeltingPt BoilingPt Section3 Chembox Hazards Solubility MainHazards FlashPt Autoignition Heme C or haem C differs from heme B in that the two vinyl side chains of heme B are replaced by covalent, thioether linkages to the apoprotein . These linkages do not allow the heme C to easily dissociate from the holoprotein , cytochrome c , compared with the more easily dissociated heme B that may dissociate from the holoprotein, the heme protein complex, even under mild conditions. This allows a very wide range of cytochrome c structure and function, with the myriad of c type cytochromes acting primarily as electron carriers. Cytochromes c, existing as dozens to hundreds of structural and functional subtypes, are found in a wide variety of cell types, even in those organisms living under extreme conditions. While heme B plays a variety of roles in cells, heme C is almost always located in proteins functioning in electron transport reactions most often associated with cell, mitochondria or chloroplast membranes. Heme C, along with the closely structurally related Heme B, are the most common heme types observed in functioning hemeproteins . The thioether linkages are commonly arranged with two amino acids between the two cysteinyl groups bound to the heme. This is often written as CXXC, within the amino acid sequence presentation with X being most any common amino acid. Vertebrate c type cytochromes also arrange a histidine amino acid next to this sequence so that CXXCH represents the five key amino acids associated with the thioether linkages in these proteins. The two thioether bonds are made to heme ring positions 2 and 4, but a few c ... more details
PBB geneid 6436 Surfactant, pulmonary associated protein A2B , also known as SFTPA2B , is a human gene . ref name entrez cite web title Entrez Gene SFTPA2 surfactant, pulmonary associated protein A2 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 6436 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 References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Floros J, Hoover RR title Genetics of the hydrophilic surfactant proteins A and D. journal Biochim. Biophys. Acta volume 1408 issue 2 3 pages 312 22 year 1999 pmid 9813381 doi 10.1016 S0925 4439 98 00077 5 cite journal author Katyal SL, Singh G, Locker J title Characterization of a second human pulmonary surfactant associated protein SP A gene. journal Am. J. Respir. Cell Mol. Biol. volume 6 issue 4 pages 446 52 year 1992 pmid 1372511 doi cite journal author Voss T, Melchers K, Scheirle G, Sch fer KP title Structural comparison of recombinant pulmonary surfactant protein SP A derived from two human coding sequences implications for the chain composition of natural human SP A. journal Am. J. Respir. Cell Mol. Biol. volume 4 issue 1 pages 88 94 year 1991 pmid 1986781 doi cite journal author Haagsman HP, White RT, Schilling J, et al. title Studies of the structure of lung surfactant protein SP A. journal Am. J. Physiol. volume 257 issue 6 Pt 1 pages L421 9 year 1990 pmid 2610270 doi cite journal author White RT, Damm D, Miller J, et al. title Isolation and characterization of the human pulmonary surfactant apoprotein gene. journal Nature volume 317 issue 6035 pages 361 3 year 1985 pmid 2995821 doi 10.1038 317361a0 cite journal author Floros J, Steinbrink R, Jacobs K, et al. title Isolation and characterization of cDNA clones for the 35 kDa pulmonary surfactant associated protein. journal J. Biol. Chem. volume 261 issue 19 page ... more details
PBB geneid 3949 The Low Density Lipoprotein LDL Receptor is a mosaic protein of 840 amino acids after removal of signal peptide that mediates the endocytosis of cholesterol rich LDL . It is a cell surface receptor that recognizes the apoprotein B100 which is embedded in the phospholipid outer layer of LDL particles. The receptor also recognizes the apoE protein found in chylomicron remnants and VLDL remnants IDL . In humans, the LDL receptor protein ref name pmid6091915 cite journal author Yamamoto T, Davis CG, Brown MS, Schneider WJ, Casey ML, Goldstein JL, Russell DW title The human LDL receptor a cysteine rich protein with multiple Alu sequences in its mRNA journal Cell volume 39 issue 1 pages 27 38 year 1984 month November pmid 6091915 doi 10.1016 0092 8674 84 90188 0 url issn ref is encoded by the LDLR gene . ref name pmid6326146 cite journal author Francke U, Brown MS, Goldstein JL title Assignment of the human gene for the low density lipoprotein receptor to chromosome 19 synteny of a receptor, a ligand, and a genetic disease journal Proc. Natl. Acad. Sci. U.S.A. volume 81 issue 9 pages 2826 30 year 1984 month May pmid 6326146 pmc 345163 doi 10.1073 pnas.81.9.2826 url issn ref ref name pmid3866240 cite journal author Lindgren V, Luskey KL, Russell DW, Francke U title Human genes involved in cholesterol metabolism chromosomal mapping of the loci for the low density lipoprotein receptor and 3 hydroxy 3 methylglutaryl coenzyme A reductase with cDNA probes journal Proc. Natl. Acad. Sci. U.S.A. volume 82 issue 24 pages 8567 71 year 1985 month December pmid 3866240 pmc 390958 doi 10.1073 pnas.82.24.8567 url issn ref It belongs to the Low density lipoprotein receptor gene family . ref name pmid12074887 cite journal author Nykjaer A, Willnow TE title The low density lipoprotein receptor gene family a cellular Swiss army knife? journal Trends Cell Biol. volume 12 issue 6 pages 273 80 year 2002 month June pmid 12074887 url http linkinghub.elsevier.com retrieve pii S096 ... more details
PBB geneid 344 Infobox protein family Symbol Apo CII Name Apo CII image PDB 1i5j EBI.jpg width caption nmr structure of human apolipoprotein c ii in the presence of sds Pfam PF05355 Pfam clan InterPro IPR008019 SMART PROSITE MEROPS SCOP 1by6 TCDB OPM family OPM protein CAZy CDD 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 assignment ... more details
PBB geneid 8542 APOL1 is the gene , which in humans encodes the Apolipoprotein L1 protein . ref name pmid9325276 cite journal author Duchateau PN, Pullinger CR, Orellana RE, Kunitake ST, Naya Vigne J, O Connor PM, Malloy MJ, Kane JP title Apolipoprotein L, a new human high density lipoprotein apolipoprotein expressed by the pancreas. Identification, cloning, characterization, and plasma distribution of apolipoprotein L journal J Biol Chem volume 272 issue 41 pages 25576 82 year 1997 month Nov pmid 9325276 pmc doi 10.1074 jbc.272.41.25576 ref ref name pmid11374903 cite journal author Page NM, Butlin DJ, Lomthaisong K, Lowry PJ title The human apolipoprotein L gene cluster identification, classification, and sites of distribution journal Genomics volume 74 issue 1 pages 71 8 year 2001 month May pmid 11374903 pmc doi 10.1006 geno.2001.6534 ref ref name pmid16020735 cite journal author Perez Morga D, Vanhollebeke B, Paturiaux Hanocq F, Nolan DP, Lins L, Homble F, Vanhamme L, Tebabi P, Pays A, Poelvoorde P, Jacquet A, Brasseur R, Pays E title Apolipoprotein L I promotes trypanosome lysis by forming pores in lysosomal membranes journal Science volume 309 issue 5733 pages 469 72 year 2005 month Jul pmid 16020735 pmc doi 10.1126 science.1114566 ref ref name entrez cite web title Entrez Gene APOL1 apolipoprotein L, 1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 8542 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 Apolipoprotein L1 apoL1 is a minor apoprotein component of High density lipoprotein HDL High density lipoprotein or good cholesterol which is synthesized in the liver and also in many other tissues, including pancreas, kidney, and brain. Although its intracellular function has not been elucidated, apoL1 circulating in plasma has the ability to kill the trypanosome Trypanosoma brucei that causes African trypan ... more details
surface. ApoB ApoB, in its ApoB100 form, is the main apoprotein , or protein part of the lipoprotein ... Lipoprotein lipase deficiency Familial apoprotein CII deficiency References Reflist 2 External ... more details
PBB geneid 4151 Myoglobin is an iron and oxygen binding protein found in the muscle tissue of vertebrates in general and in almost all mammals. It is related to hemoglobin , which is the iron and oxygen binding protein in blood, specifically in the red blood cells. The only time myoglobin is found in the bloodstream is when it is released following muscle injury. It is an abnormal finding, and can be diagnostically relevant when found in blood. ref name Nelson00 cite book author Nelson, D. L. Cox, M. M. title Lehninger Principles of Biochemistry publisher Worth Publishers location New York year 2000 page 206 edition 3rd isbn 0 7167 6203 X ref Myoglobin abbreviated Mb is a tertiary structure single chain globular protein of 153 ref cite doi 10.1016 j.niox.2009.10.003 ref or 154 ref name review amino acid s, containing a heme iron containing porphyrin prosthetic group in the center around which the remaining apoprotein folds. It has eight alpha helices and a hydrophobic core. It has a molecular weight of 17,699 Atomic mass unit daltons with heme , and is the primary oxygen carrying biological pigment pigment of muscle tissues. ref name review cite journal title Myoglobin an essential hemoprotein in striated muscle author George A. Ordway and Daniel J. Garry journal Journal of Experimental Biology year 2004 volume 207 pages 3441 6 doi 10.1242 jeb.01172 pmid 15339940 issue Pt 20 ref Unlike the blood borne hemoglobin , to which it is structurally related, ref name family cite book chapterurl http www.ncbi.nlm.nih.gov entrez query.fcgi?cmd Search&db books&doptcmdl GenBookHL&term myoglobin AND mcb 5Bbook 5D AND 105134 5Buid 5D&rid mcb.figgrp.540 chapter Evolutionary tree showing the globin protein family members myoglobin and hemoglobin title Molecular Cell Biology edition 4th author Harvey Lodish, Arnold Berk, Lawrence S. Zipursky, Paul Matsudaira, David Baltimore and James Darnell year 2000 publisher W. H. Freeman isbn 0 7167 3136 3 ref this protein does not exhibit coop ... more details
PBB geneid 7436 The very low density lipoprotein receptor VLDL R is a lipoprotein receptor that shows considerable similarity to the LDL receptor low density lipoprotein receptor . This receptor has been suggested to be important for the metabolism of apoprotein E containing triacylglycerol rich lipoproteins, such as Very low density lipoprotein very low density lipoprotein VLDL , beta migrating VLDL and intermediate density lipoprotein. It is also one of the receptors of reelin , an extracellular matrix protein which regulates the processes of neuronal migration and synaptic plasticity . In humans, the VLDL R is encoded by the VLDLR gene . ref name pmid8294473 cite journal author Sakai J, Hoshino A, Takahashi S, Miura Y, Ishii H, Suzuki H, Kawarabayasi Y, Yamamoto T title Structure, chromosome location, and expression of the human very low density lipoprotein receptor gene journal J. Biol. Chem. volume 269 issue 3 pages 2173 82 year 1994 month January pmid 8294473 doi url ref Tissue distribution In rabbits, the mRNA for the VLDLR was found to be most abundant in heart, skeletal muscle, and adipose tissue, but was not detectable in the liver. Human mRNA studies showed a very similar pattern of distribution. Hence, it has been suggested that the VLDLR might play an important role in the fatty acid metabolism of non hepatic tissues. Clinical signifance A rare neurological disorder first described in the 1970s under the name disequilibrium syndrome is now considered to be caused by the disruption of VLDLR gene. ref name pmid18043714 cite journal author Moheb LA title Identification of a nonsense mutation in the very low density lipoprotein receptor gene VLDLR in an Iranian family with dysequilibrium syndrome journal Eur. J. Hum. Genet. volume 16 issue 2 pages 270 3 year 2008 month February pmid 18043714 doi 10.1038 sj.ejhg.5201967 author separator , author2 Tzschach A author3 Garshasbi M display authors 3 last4 Kahrizi first4 Kimia last5 Darvish first5 Hossein last6 He ... more details
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