Other uses Hat disambiguation enzyme Name Histoneacetyltransferase EC number 2.3.1.48 CAS number 9054 51 7 IUBMB EC number 2 3 1 48 GO code 0004402 image width caption Histone acetyltransferases HAT are enzyme s that acetylation acetylate conserved lysine amino acid s on histone proteins by transferring an acetyl group from Coenzyme A acetyl CoA to form N acetyl lysine. In general, histone acetylation is linked to DNA transcription transcriptional activation and associated with euchromatin . When it was first discovered, it was thought that acetylation of lysine neutralizes the positive electric charge charge normally present, thus reducing affinity between histone and negatively charged DNA, which renders DNA more accessible to transcription factors . Research has emerged, since, to show that lysine acetylation and other posttranslational modification s of histones generate binding sites for specific protein protein interaction domains, such as the acetyl lysine binding bromodomain . Citation needed date July 2008 Histone acetyltransferases can also acetylate non histone proteins, such as transcription factors and nuclear receptors to facilitate gene expression. Examples Human proteins that possess histoneacetyltransferase catalytic activity include CREB binding protein CREBBP ... coactivator 3 NCOA3 , MGEA5 NCOAT GTF3C4 TF3C4 Interaction with HDACs Histone acetyltransferases HATs and histone deacetylase s HDACs are recruited to their target promoters through a physical interaction ... also Histone Modifying Enzymes Histone deacetylase Histone methyltransferase RNA polymerase control by chromatin structure Acetyltransferase External links MeshName Histone Acetyltransferases Acyltransferases Transcription DEFAULTSORT HistoneAcetyltransferase Category Transferases Category EC 2.3.1 Category Epigenetics transferase stub es Histona acetiltransferasa fr Histone ac tyl transf rase it Istone acetiltransferasi hu Hiszton acetiltranszfer z nl Histon acetyltransferase ru ... more details
Histoneacetyltransferase References reflist 2 Chromo External links http www.youtube.com ... journal author Redon C, Pilch D, Rogakou E, Sedelnikova O, Newrock K, Bonner W title Histone H2A variants ... pmid 11893489 doi 10.1016 S0959 437X 02 00282 4 url ref Classes Pfam box Symbol Histone Name Core histone H2A H2B H3 H4 image Protein H2AFJ PDB 1aoi.png width caption Protein Data Bank PDB rendering ... 1s32 , PDB2 1tyz , PDB2 1u35 , PDB2 2aro , PDB2 2cv5 , PDB2 2hio Pfam box Symbol Linker histone Name linker histone H1 and H5 family image PBB Protein HIST1H1B image.jpg width caption Protein Data Bank ... 9305837 doi 10.1038 38444 url PDB 1AOI ref The linker histone H1 binds the nucleosome and the entry .... The following is a list of human histone proteins class wikitable border 1 Super family Family Subfamily Members rowspan 4 align center Linker rowspan 3 align center Histone H1 H1 H1F H1F0 , H1FNT ... center Core rowspan 4 align center Histone H2A H2A H2AF H2AFB1 , H2AFB2 , H2AFB3 , H2AFJ , H2AFV , H2AFX ... 4 align center Histone H2B H2B H2BF H2BFM , H2BFO , H2BFS , H2BFWT H2B1 HIST1H2BA , HIST1H2BB , HIST1H2BC ... , HIST1H2BL , HIST1H2BM , HIST1H2BN , HIST1H2BO H2B2 HIST2H2BE rowspan 4 align center Histone H3 ... , HIST1H3J H3A2 HIST2H3C H3A3 HIST3H3 rowspan 3 align center Histone H4 H4 H41 HIST1H4A , HIST1H4B ... translational modification see below . It has been proposed that histone proteins are evolutionarily ... M, Lupas AN title On the origin of the histone fold journal BMC Struct Biol volume 7 year 2007 ... R, Bowman A, El Mkami H, Owen Hughes T, Norman DG title Long distance PELDOR measurements on the histone ... of histone proteins Nonpolar interactions between the histone and deoxyribose sugars on DNA Salt ... nature of histones, aside from facilitating DNA histone interactions, contributes to their water ... . In general, gene s that are active have less bound histone, while inactive genes are highly associated ... called histone code . ref name pmid10638745 cite journal author Strahl BD, Allis CD title The language ... more details
Image Acetyl.png thumb Chemical structure of an acetyl group bound to the remainder R of a molecule. Acetyltransferase or transacetylase is a type of transferase enzyme that transfers an acetyl group. Examples include Histoneacetyltransferase s including CBP histoneacetyltransferase Choline acetyltransferase Chloramphenicol acetyltransferase Serotonin N acetyl transferase NatA Acetyltransferase NatB acteyltransferase See also Acyltransferase External links MeshName Acetyltransferases Acyltransferases Category Transferases enzyme stub es Acetiltransferasa fr Ac tyltransf rase pt Acetiltransferase ru sr Acetiltransferaza ... more details
protein Name euchromatic histone lysine N methyltransferase 1 caption image width HGNCid 24650 Symbol EHMT1 AltSymbols EntrezGene 79813 OMIM 607001 RefSeq NM 024757 UniProt Q9H9B1 PDB ECnumber 2.1.1.43 Chromosome 9 Arm Band LocusSupplementaryData Histone methyltransferases HMT are enzyme s, EZH2 histone lysine N methyltransferase and histone arginine N methyltransferase, that catalyze the transfer of one to three methyl groups from the cofactor biochemistry cofactor S Adenosyl methionine to lysine and arginine residues of histone protein s. These proteins clarify date October 2010 often contain a SET S u var 3 9, E nhancer of Zeste, T rithorax Protein domain domain , however the recently discovered HMT Dot1 lacks the characteristic SET domain. fact date October 2010 Role in gene regulation Histone methylation serves in epigenetic gene regulation . Methylated histones bind DNA more tightly, which inhibits transcription genetics transcription . fact date October 2010 Methylated histones can either repress or activate transcription as different experimental findings suggest. See Histone Chromatin regulation . See also Histone Modifying Enzymes HistoneacetyltransferaseHistone deacetylase RNA polymerase control by chromatin structure Histone methylation References reflist External links http www.ncbi.nlm.nih.gov bookshelf br.fcgi?book gene&part kleefstra GeneReviews NCBI NIH UW entry on Kleefstra Syndrome MeshName Histone Lysine N Methyltransferase MeshName Protein Arginine N Methyltransferase http www.begellhouse.com journals 6dbf508d3b17c437,277d588e5dacdac4,25a707f32f2d19e3.html Structure and Function of Histone Methyltransferases. Trievel. 2004 http www.genetics.org cgi content short 182 2 437 The Dot1 Histone Methyltransferase and the Rad9 Checkpoint Adaptor Contribute to Cohesin Dependent Double Strand Break Repair by Sister Chromatid Recombination in Saccharomyces cerevisiae. Methyltransferases Transcription DEFAULTSORT Histone Methyltransferase Category EC 2.1.1 ... more details
month March pmid 11242053 doi 10.1038 35065132 url issn ref Acetylation of histone H3 occurs at several different lysine positions in the histone tail and is performed by a family of enzymes known as histoneacetyltransferase s HATs . Acetylation of lysine14 is commonly seen in genes that are being ...Unreferenced date April 2007 protein Name H3 histone, family 3A H3.3A caption image width HGNCid 4764 ... Chromosome 1 Arm q Band 41 LocusSupplementaryData protein Name H3 histone, family 3B H3.3B caption ... P84243 PDB ECnumber Chromosome 17 Arm q Band 25 LocusSupplementaryData Histone H3 is one of the five main histone protein s involved in the structure of chromatin in eukaryotic cell s. Citation needed ... is involved with the structure of the nucleosome s of the beads on a string structure. Histone proteins are highly post translationally modified however Histone H3 is the most extensively modified of the five histones. The term Histone H3 alone is purposely ambiguous in that it does not distinguish between sequence variants or modification state. Histone H3 is an important protein in the emerging ... Modifications The N terminal tail of histone H3 protrudes from the globular nucleosome core and can ... R, Zhang MQ title Determination of enriched histone modifications in non genic portions of the human ... author Lachner M, O Carroll D, Rea S, Mechtler K, Jenuwein T title Methylation of histone H3 lysine ... of histone H3. These are denoted as Histone H3.1, Histone H3.2 and Histone H3.3 but are highly ... WF, Gongidi P, Woods KR, Jin J, Maltais LJ title The human and mouse replication dependent histone ... patterns and post translational modifications associated with mammalian histone H3 variants journal ... jbc.M509266200 url issn ref Genetics Histone H3s are coded by several genes in the human genome ... , HIST1H3I , HIST1H3J H3.2 HIST2H3A , HIST2H3C , HIST2H3D H3.3 H3F3A , H3F3B See also Other histone proteins Histone H1 H1 Histone H2A H2A Histone H2B H2B Histone H4 H4 Nucleosome Histone Chromatin ... more details
Unreferenced stub auto yes date December 2009 Orphan date February 2009 A histone gene is a gene that codes for histone protein s. See also Histone H1 Histone H2A Histone H2B Histone H3 Histone H4 DEFAULTSORT Histone Gene Category Genes Cell biology stub ... more details
The histone code is a hypothesis that the transcription of genetic information encoded in DNA is in part regulated by chemical modifications to histone proteins, primarily on their unstructured ends. Together ... Jenuwein cite journal author Jenuwein T, Allis C title Translating the histone code journal Science ... with a flexible N terminus taken to be the tail that protrudes from the nucleosome. Many of the histone tail modifications correlate very well to chromatin structure and both histone modification state and chromatin structure correlate well to gene expression levels. The critical concept of the histone code hypothesis is that the histone modifications serve to recruit other proteins by specific recognition of the modified histone via protein domain s specialized for such purposes, rather than through simply stabilizing or destabilizing the interaction between histone and the underlying DNA .... For details of gene expression regulation by histone modifications see Histone code Modifications ... of histone modifications. While it is accepted that modifications such as methylation , acetylation , ADP ribosylation, ubiquitination and phosphorylation to histone tails alter chromatin structure, a complete understanding of the precise mechanisms by which these alterations to histone tails influence DNA histone interactions remains elusive. However, some specific examples have been worked out in detail. For example, phosphorylation of serine residues 10 and 28 on histone H3 is a marker ... of a lysine residue 14 on histone H3 is a tell tale sign of active Transcription genetics ... author Strahl B, Allis C title The language of covalent histone modifications journal Nature volume 403 issue 6765 pages 41 5 year 2000 pmid 10638745 doi 10.1038 47412 ref Acetylation by Histoneacetyltransferase HAT histone acetyl transferase deacetylation by HDAC histone deacetylase Deacetylation ... last6 Zhang first6 Michael Q author5 link Michael Q. Zhang title Determination of enriched histone ... more details
acetylation. Its action is opposite to that of histoneacetyltransferase . HDAC proteins are now also .... Acetylation of PTEN by the histoneacetyltransferase p300 CBP associated factor PCAF can repress ...enzyme Name histone deacetylase EC number 3.5.1.98 CAS number 9076 57 7 IUBMB EC number 3 5 1 98 GO code 0046970 image width caption Pfam box Symbol Hist deacetyl Name Histone deacetylase superfamily image ... Histone deacetylases HDAC Enzyme Commission number EC number 3.5.1 are a class of enzyme s that remove acetyl group s O C CH sub 3 sub from an N acetyl lysine amino acid on a histone . This is important ... includes non histone proteins. ref name pmid19608861 cite journal author Choudhary C title Lysine ... with the acetylpolyamine amidohydrolase s and the acetoin utilization protein s, the histone deacetylases form an ancient protein superfamily known as the histone deacetylase superfamily. ref name pmid9278492 cite journal author Leipe DD, Landsman D title Histone deacetylases, acetoin utilization ... M, Clarke C, Marks PA title Histone deacetylase inhibitors overview and perspectives journal Mol. Cancer ... histone acetylation, increase in p21 and p27 HDAC2 1 Nucleus Ubiquitous Glucocorticoid receptor ... except class III contain zinc and are known as Zn dependent histone deacetylases. ref name pmid19459166 cite journal author Marks PA, Xu WS title Histone Deacetylase Inhibitors Potential in Cancer ... potassium dependency 3 Rpd3 , which corresponds to Class I histone deacetylase 1 hda1 , corresponding ... cite journal author Sengupta N, Seto E title Regulation of histone deacetylase activities ... author de Ruijter AJ, van Gennip AH, Caron HN, Kemp S, van Kuilenburg AB title Histone deacetylases ... pmid16532030 cite journal author Longworth MS, Laimins LA title Histone deacetylase 3 localizes ... j.tcb.2008.04.003 url issn ref Function Histone modification Histone tails are normally positively ... help the histone tails to interact with and bind to the negatively charged phosphate group s on the DNA ... more details
unreferenced date November 2010 Unreferenced stub auto yes date December 2009 A histone octamer is an octamer of the histone s found at the center of a nucleosome core particle . It consists of 2 copies of each of the four core histone proteins Histone H2A H2A , Histone H2B H2B , Histone H3 H3 and Histone H4 H4 . The octamer assembles when a tetramer, containing two copies of both H3 and H4, complexes with two H2A H2B dimers. These histones of the histone octamer all contain N terminal tail s that emanate from their central histone fold s, and core domains with the C terminals. The core domains are hydrophobic. See also Nucleosome Histone Chromatin DEFAULTSORT Histone Octamer Category Proteins Category Molecular biology Biochem stub pl Oktamer histonowy ... more details
Unreferenced stub auto yes date December 2009 Orphan date December 2009 A histone fold is a fold found near the C terminus of each type histone in a histone octamer . The core histones share a structurally conserved Structural motif motif , the histone fold, averaging about 70 amino acid s. The histone fold consists of three alpha helix alpha helices connected by short loops. DEFAULTSORT Histone Fold Category Protein folding Category Molecular biology Biochem stub ar ... more details
Unreferenced stub auto yes date December 2009 Protein Name H4 histone, family 3 caption image width HGNCid 4780 Symbol H4F3 AltSymbols EntrezGene 3023 OMIM RefSeq UniProt P62805 PDB ECnumber Chromosome 3 Arm q Band 13.13 LocusSupplementaryData Histone H4 is one of the 5 main histone protein s involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N terminal tail, H4 is a structural component of the nucleosome , and is subject to covalent modification, including acetylation and methylation , which may alter expression of genes located on DNA associated with its parent histone octamer. Genetics Histone H4 is encoded in multiple genes at different loci including HIST1H4A , HIST1H4B , HIST1H4C , HIST1H4D , HIST1H4E , HIST1H4F , HIST1H4H , HIST1H4I , HIST1H4J , HIST1H4K , HIST1H4L , HIST2H4A , HIST2H4B , HIST4H4 , Hip See also nucleosome histone chromatin Other histone proteins involved in chromatin Histone H1 H1 Histone H2A H2A Histone H2B H2B Histone H3 H3 Chromo Cell biology stub de Histon H4 hu H4 hiszton pl Histon H4 zh H4 ... more details
Unreferenced stub auto yes date December 2009 Protein Name H2B histone family, member M caption image width HGNCid 27867 Symbol H2BFM AltSymbols EntrezGene 286436 OMIM RefSeq XM 210048 UniProt Q99879 PDB ECnumber Chromosome X Arm q Band 22.2 LocusSupplementaryData Histone H2B is one of the 5 main histone protein s involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N terminal tail H2B is involved with the structure of the nucleosome s of the beads on a string structure. See nucleosome , histone and chromatin . Other histone proteins involved Histone H1 H1 Histone H2A H2A Histone H3 H3 Histone H4 H4 Chromo In popular culture H2B is mentioned in the Rap music rap song pistol pistol in Obie Trice s remix, saying a H2B to light your kidneys DEFAULTSORT Histone H2b Cell biology stub hu H2B zh H2B ... more details
Histone H2A is one of the 5 main histone protein s involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N terminal tail, H2A is involved with the structure of the nucleosome s of the beads on a string structure. Other histone proteins involved Histone H1 H1 Histone H2B H2B Histone H3 H3 Histone H4 H4 Sequence Variants The term Histone H2A is intentionally non specific and refers to a variety of closely related proteins that vary often by only a few amino acids. Notable variants include H2A.1, H2A.2, H2A.X, and H2A.Z. Genetics H2A is coded by many genes in the human genome, including H2AFB1 , H2AFB2 , H2AFB3 , H2AFJ , H2AFV , H2AFX , H2AFY , H2AFY2 , and H2AFZ See also Chromatin Nucleosome Chromo External links http www.nextbio.com b home home.nb?q h2a Nextbio Cell biology stub Category Proteins de Histon H2B it Istone H2a hu H2A zh H2A ... more details
Histone methylation is the modification of certain amino acids in a histone protein by the addition of one, two, or three methyl groups. In the cell nucleus, DNA is wound around histones. Methylation and demethylation of histones turns the genes in DNA off and on , respectively, either by loosening their tails, thereby allowing transcription factors and other proteins to access the DNA, or by encompassing their tails around the DNA, thereby restricting access to the DNA. This is true in most cases. Function This modification alters the properties of the nucleosome and affects its interactions with other proteins. Histone methylation is in general associated with transcriptional Repressor repression . However, methylation of some lysine and arginine residues of histones results in transcriptional activation. Examples include methylation of lysine 4 of histone 3 H3K4 , and arginine R residues on H3 and Histone H4 H4 . See also methylation Histone methyltransferase Histone acetylation and deacetylation Transcription DEFAULTSORT Histone Methylation Category Molecular genetics Category Cellular processes Cell biology stub genetics stub ar ... more details
Lead missing date March 2011 For many years histone methylation was thought to be a permanent modification. Very recently two families of histone demethylating enzyme s were discovered. The first was Lysine Specific Demethylase 1 LSD1 which is an Flavin group flavin dependent monoamine oxidase which can demethylate mono and di methylated lysines, specifically histone 3, lysines 4 and 9 H3K4 and H3K9 . This enzyme cannot demethylate tri methylated lysines and for a short while it was thought that tri methylated lysines may indeed be permanent modifications. In late 2005 the Jumonji domain containing JmjC histone demethylases were discovered which are able to demethylate mono , di , or tri methylated lysines thereby disproving the theory that histone methylation is permanent once and for all. Although this conclusion has since come into question. ref Webby CJ et al. Jmjd6 catalyses lysyl hydroxylation of U2AF65, a protein associated with RNA splicing. 2009 Science 325 5936 90 3. ref Two specific JmjC histone demethylase s are PHF8 and KIAA1718 . References reflist External links MeshName Histone demethylase CH NH2 oxidoreductases Transcription Category Molecular genetics biochem stub ... more details
Pfam box Symbol Linker histone Name linker histone H1 and H5 family image PBB Protein HIST1H1B image.jpg ... 1hst , PDB2 1uhm , PDB2 1uss , PDB2 1ust , PDB2 1yqa Histone H1 is one of the five main histone protein ... sequence conserved , it is nevertheless the most variable histone in sequence across species. Structure ... V, Finch JT, Graziano V, Lee PL, Sweet RM title Crystal structure of globular domain of histone ... quote isbn 0 12 364565 4 oclc doi url accessdate ref Much has been learned about histone H1 from studies ... pmid561660 cite journal author Thoma F, Koller T title Influence of histone H1 on chromatin structure ... of histone H1 in the organization of the nucleosome and of the salt dependent superstructures ... suggest that the globular domain of histone H1 localizes near the nucleosome dyad, where it protects ... of histone H1 journal Nucleic Acids Res. volume 3 issue 2 pages 477 92 year 1976 month February pmid ... JP, Simpson RT title Removal of histone H1 exposes a fifty base pair DNA segment between nucleosomes ... C, Aviles FX title The structure of histone H1 and its location in chromatin journal Nature volume ..., linker DNA, and linker histone form a unique structural motif that directs the higher order folding ..., Kandolf H, Smith RC title The maternal histone H1 variant, H1M B4 protein , is the predominant H1 histone ... cite journal author Gunjan A, Alexander BT, Sittman DB, Brown DT title Effects of H1 histone variant ... histone depletion causes 2 fold lengthwise extension of mitotic chromosomes, while overexpression ... Maresca TJ, Freedman BS, Heald R title Histone H1 is essential for mitotic chromosome architecture ... of multiple isoforms that may be present in several gene clusters, but various linker histone isoforms ... histone H1 isoform H1.1 is essential for chromatin silencing and germline development in Caenorhabditis ... P, Konev AY, Fyodorov DV, Skoultchi AI title Linker histone H1 is essential for Drosophila development ... journal author Misteli T, Gunjan A, Hock R, Bustin M, Brown DT title Dynamic binding of histone H1 to chromatin ... more details
N acetyltransferase is an enzyme that catalysis catalyzes the transfer of acetyl groups from acetyl CoA to arylamine s. ref name pmid2664821 cite journal author Evans DA title N acetyltransferase journal Pharmacology & Therapeutics volume 42 issue 2 pages 157 234 year 1989 pmid 2664821 doi 10.1016 0163 7258 89 90036 3 url issn ref They have wide specificity for aromatic amine s, particularly serotonin , and can also catalyze acetyl transfer between arylamines without CoA. EC 2.3.1.5. Examples The following is a list of human gene s that encode N acetyltransferase enzymes class wikitable border 1 Symbol Name Serotonin N acetyl transferase AANAT arylalkylamine N acetyltransferase ARD1A ARD1 homolog A, N acetyltransferase S. cerevisiae GNPNAT1 glucosamine phosphate N acetyltransferase 1 HGSNAT heparan alpha glucosaminide N acetyltransferase MAK10 MAK10 homolog, amino acid N acetyltransferase subunit S. cerevisiae NAT1 N acetyltransferase 1 arylamine N acetyltransferase N acetyltransferase 2 NAT2 N acetyltransferase 2 arylamine N acetyltransferase NAT5 N acetyltransferase 5 GCN5 related, putative NAT6 N acetyltransferase 6 GCN5 related NAT8 N acetyltransferase 8 GCN5 related, putative NAT8L N acetyltransferase 8 like GCN5 related, putative NAT9 N acetyltransferase 9 GCN5 related, putative NAT10 N acetyltransferase 10 GCN5 related NAT11 N acetyltransferase 11 GCN5 related, putative NAT12 N acetyltransferase 12 GCN5 related, putative NAT13 N acetyltransferase 13 GCN5 related NAT14 N acetyltransferase 14 GCN5 related, putative NAT15 N acetyltransferase 15 GCN5 related, putative References Reflist transferase stub Acyltransferases Category EC 2.3.1 ... more details
enzyme Name thioethanolamine S acetyltransferase EC number 2.3.1.11 CAS number 9029 93 0 IUBMB EC number 2 3 1 11 GO code 0050336 image width caption In enzymology , a thioethanolamine S acetyltransferase EC number 2.3.1.11 is an enzyme that catalysis catalyzes the chemical reaction acetyl CoA 2 aminoethanethiol eqm CoA S 2 aminoethyl thioacetate Thus, the two substrate biochemistry substrates of this enzyme are acetyl CoA and 2 aminoethanethiol , whereas its two product chemistry products are coenzyme A CoA and S 2 aminoethyl thioacetate . This enzyme belongs to the family of transferase s, specifically those acyltransferase s transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl CoA 2 aminoethanethiol S acetyltransferase . Other names in common use include thioltransacetylase B , thioethanolamine acetyltransferase , and acetyl CoA thioethanolamine S acetyltransferase . References reflist 1 cite journal author BRADY RO, STADTMAN ER date 1954 title Enzymatic thioltransacetylation journal J. Biol. Chem. volume 211 pages 621&ndash 9 pmid 13221570 issue 2 McElroy, W.D. and Glass, B. Eds. , A Symposium on the Mechanism of Enzyme Action, Johns Hopkins Press, Baltimore, 1954, p. 545 580. transferase stub Category EC 2.3.1 Category Enzymes of unknown structure it Tioetanolammina S acetiltransferasi ... more details
enzyme Name Diaminobutyrate acetyltransferase EC number 2.3.1.178 CAS number IUBMB EC number 2 3 1 178 GO code image width caption Orphan date February 2009 In enzymology , a diaminobutyrate acetyltransferase EC number 2.3.1.178 is an enzyme that catalysis catalyzes the chemical reaction acetyl CoA L 2,4 diaminobutanoate math rightleftharpoons math CoA N sub 4 sub acetyl L 2,4 diaminobutanoate Thus, the two substrate biochemistry substrates of this enzyme are acetyl CoA and L 2,4 diaminobutanoate , whereas its two product chemistry products are coenzyme A CoA and N4 acetyl L 2,4 diaminobutanoate . This enzyme belongs to the family of transferase s, specifically those acyltransferase s transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl CoA L 2,4 diaminobutanoate N4 acetyltransferase . Other names in common use include L 2,4 diaminobutyrate acetyltransferase , L 2,4 diaminobutanoate acetyltransferase , EctA , diaminobutyric acid acetyltransferase , DABA acetyltransferase , 2,4 diaminobutanoate acetyltransferase , DAB acetyltransferase , DABAcT , and acetyl CoA L 2,4 diaminobutanoate 4 N acetyltransferase . This enzyme participates in glycine, serine and threonine metabolism . References reflist 1 cite journal author Peters P, Galinski EA and Truper HG date 1990 title The biosynthesis of ectoine journal FEMS Microbiol. Lett. volume 71 pages 157&ndash 162 doi 10.1111 j.1574 6968.1990.tb03815.x cite journal author A, Takano M, Murooka Y date 1999 title Characterization of Biosynthetic Enzymes for Ectoine as a Compatible Solute in a Moderately Halophilic Eubacterium, Halomonas elongata journal J. Bacteriol. volume 181 pages 91&ndash 9 pmid 9864317 issue 1 pmc 103536 cite journal author Reshetnikov AS, Mustakhimov II, Khmelenina VN, Trotsenko YA date Mosc title Cloning, purification, and characterization of diaminobutyrate acetyltransferase from the halotolerant methanotroph Methylomicrobium alcaliphilum 20Z journal B volume ... more details
Cleanup date January 2010 NatA Acetyltransferase N sup sup acetyltransferase , is an enzyme that serves to catalyze the addition of acetyl groups to various proteins emerging from the ribosome . Upon translation, the NatA binds to the ribosome and then stretches to the front end of the forming, or nascent, polypeptide, where it adds this acetyl group. This acetyl group is added to the front end, or N terminus of the new protein. Forty percent of all proteins in the yeast proteome are thought to be N terminally acetylated, with a corresponding figure of 90 in mammalian proteins. ref Caesar, Robert, Jonas Warringer, and Anders Blomberg. Physiological Importance and Identification of Novel Targets for the N Terminal Acetyltransferase NatB Caesar et al. 5 2 368 . Eukaryotic Cell. 16 December 2005. Web. 31 January 2010. http ec.asm.org cgi content full 5 2 368 . ref To be specific, NatA is the main N alpha terminal acetyltransferase in the yeast cytosol, responsible for the acetylation of proteins at locations in which small L small serine , small L small alanine , small L small threonine , or glycine are present. ref Gautschi, Matthias, S ren Just, Andrej Mun, Suzanne Ross, Peter R cknagel, Yves Dubaqui , Ann Ehrenhofer Murray, and Sabine Rospert. The Yeast N alpha Acetyltransferase ... ref Polevoda, Bogdan, Jason Hoskins, and Fred Sherman. Properties of Nat4, an N alpha Acetyltransferase ... of Nat4, an N alpha Acetyltransferase of Saccharomyces cerevisiae That Modifies N Termini of Histones ... mcb.asm.org cgi content full 29 11 2913 . ref NatA Acetyltransferase is not a single protein but a complex of three subunits . Sup35p Acetylation In Saccharomyces cerevisiae NatA Acetyltransferase ... own conformation. Thus, PSI strains deficient in NatA Acetyltransferase have been found to have ... in PSI strains lacking NatA Acetyltransferase. ref The NatA Acetyltransferase Couples Sup35 Prion ... DEFAULTSORT Nata Acetyltransferase Category Enzymes ... more details
enzyme Name sulfoacetaldehyde acetyltransferase EC number 2.3.3.15 CAS number IUBMB EC number 2 3 3 15 GO code 0050487 image width caption In enzymology , a sulfoacetaldehyde acetyltransferase EC number 2.3.3.15 is an enzyme that catalysis catalyzes the chemical reaction acetyl phosphate sulfite math rightleftharpoons math 2 sulfoacetaldehyde phosphate Thus, the two substrate biochemistry substrates of this enzyme are acetyl phosphate and sulfite , whereas its two product chemistry products are 2 sulfoacetaldehyde and phosphate . This enzyme belongs to the family of transferase s, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is acetyl phosphate sulfite S acetyltransferase acyl phosphate hydrolysing, 2 oxoethyl forming . This enzyme is also called Xsc . This enzyme participates in taurine and hypotaurine metabolism . References reflist 1 cite journal author Ruff J, Denger K, Cook AM date 2003 title Sulphoacetaldehyde acetyltransferase yields acetyl phosphate purification from Alcaligenes defragrans and gene clusters in taurine degradation journal Biochem. J. volume 369 pages 275&ndash 85 pmid 12358600 doi 10.1042 BJ20021455 issue Pt 2 pmc 1223080 transferase stub Category EC 2.3.3 Category Enzymes of unknown structure it Sulfoacetaldeide acetiltransferasi ... more details
enzyme Name Choline acetyltransferase EC number 2.3.1.6 CAS number 9012 78 6 IUBMB EC number 2 3 1 6 GO code 0004102 image width caption PBB geneid 1103 Choline acetyltransferase abbreviated ChAT is an enzyme ... terminal via axoplasmic flow . The role of choline acetyltransferase is to join Acetyl coenzyme A Acetyl ... entrez cite web title Entrez Gene CHAT choline acetyltransferase url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 1103 accessdate ref In humans, the choline acetyltransferase ... RR, Jayakar P, Kong CF, Hersh LB, Hilt DC, Rabin M title Human choline acetyltransferase gene ... used as an immunohistochemical marker for motor neuron s motoneurons . See also Acetyltransferase ... Oda Y title Choline acetyltransferase the structure, distribution and pathologic changes in the central ... DNA for human choline acetyltransferase induces two forms of enzyme with different molecular ... acetyltransferase CHAT partial gene sequence and potential control regions journal Genomics volume ... R, Strauss WL title Two mRNAs are transcribed from the human gene for choline acetyltransferase journal ... cite journal author Misawa H, Ishii K, Deguchi T title Gene expression of mouse choline acetyltransferase ... of the human choline acetyltransferase gene journal Neurosci. Lett. volume 132 issue 2 pages 191 ... choline acetyltransferase gene maps to region 10q11 q22.2 by in situ hybridization journal Genomics ... E title Localization of a 900 bp long fragment of the human choline acetyltransferase gene to 10q11.2 ... N title Cloning of Drosophila choline acetyltransferase cDNA journal Proc. Natl. Acad. Sci. U.S.A. ... choline acetyltransferase journal J. Neurochem. volume 51 issue 6 pages 1843 5 year 1988 pmid ... S title cDNA cloning and complete sequence of porcine choline acetyltransferase in vitro translation ... acetyltransferase gene localization of alternative first exons journal J. Neurosci. Res. volume 40 ... P title Identification and analysis of the human choline acetyltransferase gene promoter journal Neuroreport ... more details
Pfam box Symbol CAT Name Chloramphenicol acetyltransferase image Chloramphenicol acetyltransferase 3CLA transparent.png width caption Ribbon diagram of the chloramphenicol acetyltransferase trimer biochemistry trimer with chloramphenicol bound. From PDB 3CLA . Pfam PF00302 InterPro IPR001707 SMART Prosite PDOC00093 SCOP 3cla TCDB OPM family OPM protein PDB PDB3 1q23 G 6 209 PDB3 1pd5 A 6 209 PDB3 1noc B 6 209 PDB3 1qca 1 205 PDB3 3cla 1 205 PDB3 4cla 1 205 PDB3 1cia 1 205 PDB3 1cla 1 205 PDB3 2cla 1 205 Chloramphenicol acetyltransferase or CAT is a bacteria l enzyme EC number 2.3.1.28 ref name PUB00000094 cite journal doi 10.1146 annurev.bb.20.060191.001033 author Engel J, Prockop DJ title The zipper like folding of collagen triple helices and the effects of mutations that disrupt the zipper journal Annu. Rev. Biophys. Biophys. Chem. volume 20 issue 1 pages 137 152 year 1991 pmid 1867713 ref that detoxifies the antibiotic chloramphenicol and is responsible for chloramphenicol resistance in bacteria. ref name pmid390404 cite journal author Shaw WV, Packman LC, Burleigh BD, Dell A, Morris HR, Hartley BS title Primary structure of a chloramphenicol acetyltransferase specified by R plasmids journal Nature volume 282 issue 5741 pages 870 2 year 1979 pmid 390404 doi 10.1038 282870a0 url issn ref This enzyme covalently attaches an acetyl group from acetyl CoA to chloramphenicol, which prevents chloramphenicol from binding to ribosome s. A histidine residue, located in the C terminal section of the enzyme, plays a central role in its catalytic mechanism. The crystal structure of the type III enzyme from Escherichia coli with chloramphenicol bound has been determined. CAT is a trimer of identical subunits monomer Mr 25,000 and the trimeric structure is stabilised by a number of hydrogen bonds, some of which result in the extension of a beta sheet across the subunit interface. Chloramphenicol ... acetyltransferase at 1.75 A resolution journal J. Mol. Biol. volume 213 issue 1 pages 167 186 ... more details
enzyme Name phosphate acetyltransferase EC number 2.3.1.8 CAS number 9029 91 8 IUBMB EC number 2 3 1 8 GO code 0008959 image width caption In enzymology , a phosphate acetyltransferase EC number 2.3.1.8 is an enzyme that catalysis catalyzes the chemical reaction acetyl CoA phosphate math rightleftharpoons math CoA acetyl phosphate Thus, the two substrate biochemistry substrates of this enzyme are acetyl CoA and phosphate , whereas its two product chemistry products are coenzyme A CoA and acetyl phosphate . This enzyme belongs to the family of transferase s, specifically those acyltransferase s transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl CoA phosphate acetyltransferase . Other names in common use include phosphotransacetylase , phosphoacylase , and PTA . This enzyme participates in 3 metabolism metabolic pathways taurine and hypotaurine metabolism , pyruvate metabolism , and propanoate metabolism . Structural studies As of late 2007, 7 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1QZT , PDB link 1R5J , PDB link 1TD9 , PDB link 1VMI , PDB link 1XCO , PDB link 2AF3 , and PDB link 2AF4 . References reflist 1 cite journal author BERGMEYER HU, HOLZ G, KLOTZSCH H, LANG G date 1963 title PHOSPHOTRANSACETYLASE FROM CLOSTRIDIUM KLUYVERI. CULTURE OF THE BACTERIUM, ISOLATION, CRYSTALLIZATION AND PROPERTIES OF THE ENZYME. journal Biochem. Z. volume 338 pages 114&ndash 21 pmid 14087284 cite journal author STADTMAN ER date 1952 title The purification and properties of phosphotransacetylase journal J. Biol. Chem. volume 196 pages 527&ndash 34 pmid 12980995 issue 2 cite journal author Stadtman ER date 1955 title Phosphotransacetylase from Clostridium kluyveri journal Methods Enzymol. volume 1 pages 596&ndash 599 doi 10.1016 0076 6879 55 01103 8 series Methods in Enzymology editor1 last Stadtman editor1 first ER isbn 0121818012 transferase stub Category ... more details
to which transcriptionally active genes are correlated with rapid turnover of histone acetylation. This requires that the HATs and HDACs must act continuously on the affected histone tail. Methylation at a specific lysine residue K4 is involved in targeting histone tails for continuous acetylation and deacetylation. See also Histone methylation External links cite journal author Clayton A, Hazzalin C, Mahadevan L title Enhanced histone acetylation and transcription a dynamic perspective journal ... of histone tail acetylation and deacetylation http www.broad.harvard.edu chembio lab schreiber ... more details
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