... peptide acetyltransferase, protein N-terminal acetyltransferase, NAT, Nalpha-acetyltransferase, amino-terminal amino acid- ... Driessen HP, de Jong WW, Tesser GI, Bloemendal H (1985). "The mechanism of N-terminal acetylation of proteins". CRC Crit. Rev. ... In enzymology, a peptide alpha-N-acetyltransferase (EC 2.3.1.88) is an enzyme that catalyzes the chemical reaction acetyl-CoA ... The systematic name of this enzyme class is acetyl-CoA:peptide Nalpha-acetyltransferase. Other names in common use include beta ...

Polevoda B, Sherman F (24 January 2003). "N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of ... "Protein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo". Molecular & Cellular ... Furthermore, Nε-acetyltransferase activity and N-terminal propionyltransferase activity have been reported. Despite the fact ... Polevoda B, Sherman F (15 August 2003). "Composition and function of the eukaryotic N-terminal acetyltransferase subunits". ...

"Characterization of phosphinothricin acetyltransferase and C-terminal enzymatically active fusion proteins". Gene. 102 (1): 33- ... Phosphinothricin acetyltransferase (EC 2.3.1.183, PAT, PPT acetyltransferase, Pt-N-acetyltransferase, ac-Pt) is an enzyme with ... Phosphinothricin+acetyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC ... systematic name acetyl-CoA:phosphinothricin N-acetyltransferase. This enzyme catalyses the following chemical reaction acetyl- ...

Both also have an active site cysteine residue (Cys68) in the N-terminal region. Further, all functional NAT enzymes contain a ... The following is a list of human genes that encode N-acetyltransferase enzymes: Evans DA (1989). "N-acetyltransferase". ... N-acetyltransferases are cytosolic enzymes found in the liver and many tissues of most mammalian species, except the dog and ... N-acetyltransferase (NAT) is an enzyme that catalyzes the transfer of acetyl groups from acetyl-CoA to arylamines, ...

... is a member of the GNAT family of acetyltransferases. It has an overall fold similar to the other N-terminal ... April 2018). "NAA80 is actin's N-terminal acetyltransferase and regulates cytoskeleton assembly and cell motility". Proceedings ... This gene encodes a member of the N-acetyltransferase family. N-acetyltransferases modify proteins by transferring acetyl ... N-acetyltransferase 80 (also known as NAT6 or FUS2) is a protein that in humans is encoded by the NAA80 gene. It acetylates the ...

The N-terminal domain of the protein Serine acetyltransferase helps catalyse acetyl transfer. This particular enzyme catalyses ... Other names in common use include SATase, L-serine acetyltransferase, serine acetyltransferase, and serine transacetylase. This ... The amino-terminal alpha-helical domain particularly the amino acid residues His158 (histidine in position 158) and Asp143 ( ... There are eight alpha helices that form the N-terminal domain. Denk D, Böck A (March 1987). "L-cysteine biosynthesis in ...

It contains an N-terminal repression region that decreases its HAT activity in vitro as well as a C-terminal activation domain ... in particular in the N-terminal and C-terminal (HAT) regions as well as in the receptor and coactivator interaction domains. ... The overall topology resembles a vise, with the central core of the protein at the base and the N- and C-terminal segments on ... Histone acetyltransferases serve many biological roles inside the cell. Chromatin is a combination of proteins and DNA found in ...

To be specific, NatA is the main N{alpha}-terminal acetyltransferase in the yeast cytosol, responsible for the acetylation of ... "Physiological Importance and Identification of Novel Targets for the N-Terminal Acetyltransferase NatB - Caesar et al. 5 (2): ... NatA acetyltransferase(Nα acetyltransferase), is an enzyme that serves to catalyze the addition of acetyl groups to various ... NatA Acetyltransferase is not a single protein but a complex of three subunits. In Saccharomyces cerevisiae NatA ...

The conserved region is situated towards the N-terminal of the protein. This entry talks about the N-terminal domain. ... TAFII55 binds to TAFII250 and inhibits its acetyltransferase activity. The exact role of TAFII55 is currently unknown but ... Pendergrast PS, Morrison D, Tansey WP, Hernandez N (August 1996). "Mutations in the carboxy-terminal domain of TBP affect the ... Gegonne A, Weissman JD, Singer DS (October 2001). "TAFII55 binding to TAFII250 inhibits its acetyltransferase activity". ...

N-terminal Acetylation is catalyzed by a set of enzyme complexes, the N-terminal acetyltransferases (NATs). NATs transfer an ... NAA80/NatH is an N-terminal acetyltransferase that specifically acetylates the N-terminus of actin. N-terminal acetylation of ... Feng J, Hu J, Li Y, Li R, Yu H, Ma L (September 2020). "The N-Terminal Acetyltransferase Naa50 Regulates Arabidopsis Growth and ... Rathore OS, Faustino A, Prudêncio P, Van Damme P, Cox CJ, Martinho RG (February 2016). "Absence of N-terminal acetyltransferase ...

Terminal transferases are transferases that can be used to label DNA or to produce plasmid vectors. It accomplishes both of ... Choline acetyltransferase (also known as ChAT or CAT) is an important enzyme which produces the neurotransmitter acetylcholine ... Terminal transferase is one of the few DNA polymerases that can function without an RNA primer. The family of glutathione ... Strauss WL, Kemper RR, Jayakar P, Kong CF, Hersh LB, Hilt DC, Rabin M (Feb 1991). "Human choline acetyltransferase gene maps to ...

N-terminal acetyltransferase B complex catalytic subunit NAT5 is an enzyme that in humans is encoded by the NAT5 gene. GRCh38: ... 2003). "Nat3p and Mdm20p are required for function of yeast NatB Nalpha-terminal acetyltransferase and of actin and tropomyosin ... Sugiura N, Adams SM, Corriveau RA (Oct 2003). "An evolutionarily conserved N-terminal acetyltransferase complex associated with ... "Entrez Gene: NAT5 N-acetyltransferase 5". Vitale N, Pacheco-Rodriguez G, Ferrans VJ, et al. (2000). "Specific functional ...

Park EC, Szostak JW (June 1992). "ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity". The ... Polevoda B, Brown S, Cardillo TS, Rigby S, Sherman F (1 February 2008). "Yeast N(alpha)-terminal acetyltransferases are ... Sugiura N, Adams SM, Corriveau RA (10 October 2003). "An evolutionarily conserved N-terminal acetyltransferase complex ... Cloning and analysis of a novel gene encoding N-terminal acetyltransferase subunit]". Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue ...

Starheim KK, Gevaert K, Arnesen T (April 2012). "Protein N-terminal acetyltransferases: when the start matters". Trends in ... HATs function similarly to N-terminal acetyltransferases (NATs) but their acetylation is reversible unlike in NATs. HAT ... Acetylation of the N-terminal histone tail is one of the most common protein modifications found in eukaryotes, with about 85% ... HATs form large multiprotein complexes that weaken the association of histones to DNA by acetylating the N-terminal histone ...

A histidine residue, located in the C-terminal section of the enzyme, plays a central role in its catalytic mechanism. The ... Chloramphenicol acetyltransferase (or CAT) is a bacterial enzyme (EC 2.3.1.28) that detoxifies the antibiotic chloramphenicol ... Leslie AG (1990). "Refined crystal structure of type III chloramphenicol acetyltransferase at 1.75 A resolution". J. Mol. Biol ... Gorman, CM; Moffat LF; Howard BH (1982). "Recombinant genomes which express chloramphenicol acetyltransferase in mammalian ...

Acetyltransferases CBP and p300 bind to the transactivation domain. AP1, STAT5 and VDR bind to C-terminal domain. Also, ETS1 ... Phosphorylation of serine residues of the C-terminal domain (in the nucleotide sequence they belong to exon VII) known as ... Ets1 overexpression in stratified squamous epithelial cells causes pro-oncogenic changes, such as suspension of terminal ... its final effect on transcription depends on whether C-terminal domain is phosphorylated. ...

Post-translational acetylation of the histone H4 N-terminal tail in chromatin has been associated with several nuclear ... The NuA4 histone acetyltransferase complex is a protein complex that has histone acetylase activity on chromatin, as well as ... "Gene Ontology Term: NuA4 histone acetyltransferase complex". Saccharomyces Genome Database. Allard S, Utley RT, Savard J, ... an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p". ...

Here, the pantothenic arm's terminal thiol group and the ε2 nitrogen on the catalytic His343 side chain form a hydrogen bond. ... Carnitine O-acetyltransferase also called carnitine acetyltransferase (CRAT, or CAT) (EC 2.3.1.7) is an enzyme that encoded by ... In general, carnitine acetyltransferases have molecular weights of about 70 kDa, and contain approximately 600 residues1. CRAT ... The systematic name of this enzyme class is acetyl-CoA:carnitine O-acetyltransferase. Other names in common use include acetyl- ...

"Physiological importance and identification of novel targets for the N-terminal acetyltransferase NatB". Eukaryotic Cell. 5 (2 ...

This DUB module is an independently folding subcomplex that is connected to the C-terminal tail of Sgf 73, Sgf73, as well as ... Spt-Ada-Gcn5 acetyltransferase (SAGA) complex is a multicomponent regulator of acetylation. It has been found that this complex ... The histone acetylation is mediated by the GCN5 histone acetyl transferase, while the deubiquitinating activity is mediated by ... This 15 subunit complex has been best characterized for its histone acetyltransferase activity (HAT). The acetylating activity ...

The amino (N) terminal charged tails are the site of the post-translational modifications, such as the one seen in H3K36me3. H4 ... Histone acetyltransferase KAT2A is the specific reader. Proteins are typically acetylated on lysine residues and this reaction ... The carboxyl (C) terminal end of these histones contribute to histone-histone interactions, as well as histone-DNA interactions ... Sadoul K, Boyault C, Pabion M, Khochbin S (2008). "Regulation of protein turnover by acetyltransferases and deacetylases". ...

The N-terminal domain (the lipoyl domain), consists of 1-3 lipoyl groups of approximately 80 amino acids each. The peripheral ... The E2 subunit, or dihydrolipoyl acetyltransferase, for both prokaryotes and eukaryotes, is generally composed of three domains ... Finally, the C-terminal (catalytic) domain catalyzes the transfer of acetyl groups and acetyl-CoA synthesis. The E3 subunit, ... Dihydrolipoamide acetyltransferase (E2) deficiency". Annals of Neurology. 58 (2): 234-241. doi:10.1002/ana.20550. ISSN 0364- ...

As with most nerve terminal proteins, ChAT is produced in the body of the neuron and is transported to the nerve terminal, ... Structure of choline acetyltransferase binding sites Crystal structure of choline ion bound in choline acetyltransferase. Side ... In humans, the choline acetyltransferase enzyme is encoded by the CHAT gene. Choline acetyltransferase was first described by ... Choline+Acetyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (Articles ...

... conserved acetyltransferase is responsible for the regulation of transcription by lysine acetylation of the histone N-terminal ... Similar to how plant peroxisomal enzymes bind propionyl-CoA and isobutyryl-CoA, Gen5, an acetyltransferase in humans, binds to ...

It was the first reported human genetic disorder linked with a mutation in an N-terminal acetyltransferase (NAT) gene. The ... Ogden syndrome, also known as N-terminal acetyltransferase deficiency (NATD), is an X-linked disorder of infancy comprising a ... Arnesen, T. (2009). "Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases ... a gene encoding the catalytic subunit of the major human N-terminal acetyltransferase enzyme system (NatA). This same mutation ...

Each histone has both an N-terminal tail and a C-terminal histone-fold. Each of these key components interacts with DNA in its ... p300 and cAMP response element-binding protein (CBP) possess histone acetyltransferase activity. p300 and CBP are the most ... The N-terminal tails do not interact with a specific region of DNA but rather stabilize and guide the DNA wrapped around the ... Each histone in the octamer has an N-terminal tail that protrudes from the histone core. The tails play roles both in inter and ...

Seth A, Alvarez E, Gupta S, Davis RJ (December 1991). "A phosphorylation site located in the NH2-terminal domain of c-Myc ... McMahon SB, Wood MA, Cole MD (January 2000). "The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c- ... Upon cleavage, the C-terminus of Myc (containing the DNA binding domain) is degraded, while Myc-nick, the N-terminal segment ... Gupta S, Davis RJ (October 1994). "MAP kinase binds to the NH2-terminal activation domain of c-Myc". FEBS Letters. 353 (3): 281 ...

"Using VAAST to Identify an X-Linked Disorder Resulting in Lethality in Male Infants Due to N-Terminal Acetyltransferase ...

Xu W, Edmondson DG, Roth SY (1998). "Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-terminal domains ... Histone acetyltransferase KAT2A is an enzyme that in humans is encoded by the KAT2A gene. GCN5L2 has been shown to interact ... Wang L, Mizzen C, Ying C, Candau R, Barlev N, Brownell J, Allis CD, Berger SL (1997). "Histone acetyltransferase activity is ... Wang L, Mizzen C, Ying C, Candau R, Barlev N, Brownell J, Allis CD, Berger SL (January 1997). "Histone acetyltransferase ...

A C-terminal Myf5 domain, a central basic helix-loop-helix (bHLH) domain and an N-terminal basic domain. The bHLH region ... These are histone acetyltransferases and histone deacetylases which activate and repress genes involved in the myocyte lineage ...