クロラムフェニコール-O-アセチルトランスフェラーゼ、クロラムフェニコール-O-アセチル基転移酵素
WordNet
- the 15th letter of the Roman alphabet (同)o
- the blood group whose red cells carry neither the A nor B antigens; "people with type O blood are universal donors" (同)type_O, group O
- an oral antibiotic (trade name Chloromycetin) used to treat serious infections (especially typhoid fever) (同)Chloromycetin
PrepTutorEJDIC
- 《呼び掛けの名前の前につけて》『おお』,あ / (驚き・恐れ・喜び・苦痛などを表して)『おお』,ああ,まあ / 《肯定・否定を強めて》
- oxygenの化学記号
- ohmオーム / Old
- osmiumの化学記号
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2018/02/16 13:55:20」(JST)
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Chloramphenicol acetyltransferase |
Ribbon diagram of the chloramphenicol acetyltransferase trimer with chloramphenicol bound. From PDB: 3CLA.
|
Identifiers |
Symbol |
CAT |
Pfam |
PF00302 |
InterPro |
IPR001707 |
PROSITE |
PDOC00093 |
SCOP |
3cla |
SUPERFAMILY |
3cla |
Available protein structures: |
Pfam |
structures |
PDB |
RCSB PDB; PDBe; PDBj |
PDBsum |
structure summary |
|
Chloramphenicol acetyltransferase |
Identifiers |
EC number |
2.3.1.28 |
CAS number |
9040-07-7 |
Databases |
IntEnz |
IntEnz view |
BRENDA |
BRENDA entry |
ExPASy |
NiceZyme view |
KEGG |
KEGG entry |
MetaCyc |
metabolic pathway |
PRIAM |
profile |
PDB structures |
RCSB PDB PDBe PDBsum |
Gene Ontology |
AmiGO / QuickGO |
Search |
PMC |
articles |
PubMed |
articles |
NCBI |
proteins |
|
Chloramphenicol acetyltransferase (or CAT) is a bacterial enzyme (EC 2.3.1.28)[1] that detoxifies the antibiotic chloramphenicol and is responsible for chloramphenicol resistance in bacteria.[2] This enzyme covalently attaches an acetyl group from acetyl-CoA to chloramphenicol, which prevents chloramphenicol from binding to ribosomes. 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 binds in a deep pocket located at the boundary between adjacent subunits of the trimer, such that the majority of residues forming the binding pocket belong to one subunit while the catalytically essential histidine belongs to the adjacent subunit. His195 is appropriately positioned to act as a general base catalyst in the reaction, and the required tautomeric stabilisation is provided by an unusual interaction with a main-chain carbonyl oxygen.[3]
Application
CAT is used as a reporter system to measure the level of a promoter or its tissue-specific expression. The CAT assay involves monitoring acetylation of radioactively labeled chloramphenicol on a TLC plate; CAT activity is determined by looking for the acetylated forms of chloramphenicol, which have a significantly increased migration rate as compared to the unacetylated form.[4]
References
- ^ Engel J, Prockop DJ (1991). "The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper". Annu. Rev. Biophys. Biophys. Chem. 20 (1): 137–152. doi:10.1146/annurev.bb.20.060191.001033. PMID 1867713.
- ^ Shaw WV, Packman LC, Burleigh BD, Dell A, Morris HR, Hartley BS (1979). "Primary structure of a chloramphenicol acetyltransferase specified by R plasmids". Nature. 282 (5741): 870–2. doi:10.1038/282870a0. PMID 390404.
- ^ Leslie AG (1990). "Refined crystal structure of type III chloramphenicol acetyltransferase at 1.75 A resolution". J. Mol. Biol. 213 (1): 167–186. doi:10.1016/S0022-2836(05)80129-9. PMID 2187098.
- ^ Gorman, CM; Moffat LF; Howard BH (1982). "Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells" (PDF). Mol. Cell. Biol. 2 (9): 1044–1051. doi:10.1128/MCB.2.9.1044. Retrieved 15 October 2012.
Transferases: acyltransferases (EC 2.3)
|
2.3.1: other than amino-acyl groups |
- acetyltransferases: Acetyl-Coenzyme A acetyltransferase
- N-Acetylglutamate synthase
- Choline acetyltransferase
- Dihydrolipoyl transacetylase
- Acetyl-CoA C-acyltransferase
- Beta-galactoside transacetylase
- Chloramphenicol acetyltransferase
- N-acetyltransferase
- Serotonin N-acetyl transferase
- HGSNAT
- ARD1A
- Histone acetyltransferase
- palmitoyltransferases: Carnitine O-palmitoyltransferase
- Serine C-palmitoyltransferase
- other: Acyltransferase like 2
- Aminolevulinic acid synthase
- Beta-ketoacyl-ACP synthase
- Glyceronephosphate O-acyltransferase
- Lecithin—cholesterol acyltransferase
- Glycerol-3-phosphate O-acyltransferase
- 1-acylglycerol-3-phosphate O-acyltransferase
- 2-acylglycerol-3-phosphate O-acyltransferase
- ABHD5
|
2.3.2: Aminoacyltransferases |
- Gamma-glutamyl transpeptidase
- Peptidyl transferase
- Transglutaminase
- Tissue transglutaminase
- Keratinocyte transglutaminase
- Factor XIII
|
2.3.3: converted into alkyl on transfer |
- Citrate synthase
- ATP citrate lyase
- HMG-CoA synthase
- Malate synthase
|
Enzymes
|
Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
|
Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
|
Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
|
Kinetics |
- Enzyme kinetics
- Eadie–Hofstee diagram
- Hanes–Woolf plot
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
|
Types |
- EC1 Oxidoreductases (list)
- EC2 Transferases (list)
- EC3 Hydrolases (list)
- EC4 Lyases (list)
- EC5 Isomerases (list)
- EC6 Ligases (list)
|
This article incorporates text from the public domain Pfam and InterPro IPR001707
UpToDate Contents
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- 1. ロッキー山紅斑熱の治療treatment of rocky mountain spotted fever [show details]
…Pediatrics . Chloramphenicol is the only known alternative agent for the treatment of RMSF. To our knowledge, no other alternative agents have been tested in humans. Although chloramphenicol has been found …
- 2. グラム陰性桿菌性髄膜炎:治療gram negative bacillary meningitis treatment [show details]
…failure rates are probably due to the fact that chloramphenicol has a bacteriostatic mechanism of action . Despite high concentrations of chloramphenicol in CSF, the enteric pathogens may persist because …
- 3. 再生不良性貧血:発症機序、臨床症状、診断aplastic anemia pathogenesis clinical manifestations and diagnosis [show details]
… glutathione-S-transferase) . Chloramphenicol is associated with both idiosyncratic and predictable bone marrow suppression. An idiosyncratic reaction to chloramphenicol causes irreversible bone marrow …
- 4. ツツガ虫病:治療および予防scrub typhus treatment and prevention [show details]
…doxycycline or chloramphenicol are associated with an increased risk of relapse. In one study of three-day therapy, relapse occurred in three of seven patients treated with chloramphenicol and three of six …
- 5. 発疹チフスepidemic typhus [show details]
…mortality is uncommon if either tetracycline or chloramphenicol is given. In a series of 60 hospitalized patients, for example, none of those treated with chloramphenicol or tetracycline died . Most patients remained …
English Journal
- Characterization of the structure and catalytic activity of Legionella pneumophila VipF.
- Young BH1, Caldwell TA1, McKenzie AM1, Kokhan O1, Berndsen CE1.
- Proteins.Proteins.2016 Jun 17. doi: 10.1002/prot.25087. [Epub ahead of print]
- The pathogenic bacteria Legionella pneumophila is known to cause Legionnaires' Disease, a severe pneumonia that can be fatal to immunocompromised individuals and the elderly. Shohdy et al. identified the L. pneumophila vacuole sorting inhibitory protein VipF as a putative N-acetyltransferase based o
- PMID 27315603
- Heme interacts with histidine- and tyrosine-based protein motifs and inhibits enzymatic activity of chloramphenicol acetyltransferase from Escherichia coli.
- Brewitz HH1, Goradia N2, Schubert E3, Galler K4, Kühl T5, Syllwasschy B1, Popp J6, Neugebauer U4, Hagelueken G3, Schiemann O3, Ohlenschläger O7, Imhof D8.
- Biochimica et biophysica acta.Biochim Biophys Acta.2016 Jun;1860(6):1343-53. doi: 10.1016/j.bbagen.2016.03.027. Epub 2016 Mar 23.
- BACKGROUND: The occurrence of free organismal heme can either contribute to serious diseases or beneficially regulate important physiological processes. Research on transient binding to heme-regulatory motifs (HRMs) in proteins resulted in the discovery of numerous Cys-based, especially Cys-Pro (CP)
- PMID 27015758
- Molecular characterization of a human matrix attachment region that improves transgene expression in CHO cells.
- Sun QL1, Zhao CP1, Chen SN1, Wang L1, Wang TY2.
- Gene.Gene.2016 May 15;582(2):168-72. doi: 10.1016/j.gene.2016.02.009. Epub 2016 Feb 9.
- Chinese hamster ovary (CHO) cells offer many advantages for recombinant gene expression, including proper folding and post-translational modification of the recombinant protein. However, due to positional effects resulting from the neighboring chromatin, transgenes are often expressed at low levels
- PMID 26869318
Japanese Journal
- Inhibition of chloramphenicol O-acetyltransferase of Escherichia coli by basic triphenylmethane dyes(Communications to the editor)
- Tanaka Hiroshi [他]
- Journal of Antibiotics 24(5), 324-325, 1971-05
- NAID 40018688685
Related Links
- chloramphenicol O-acetyltransferase activity Source: UniProtKB-EC GO - Biological process i response to antibiotic Source: UniProtKB-KW Complete GO annotation... Keywords - Molecular function i Acyltransferase, Transferase ...
- 1. Cold Spring Harb Protoc. 2010 May;2010(5):pdb.prot5422. doi: 10.1101/pdb.prot5422. Chloramphenicol acetyltransferase assay. Smale ST. When a transient or stable transfection assay is developed for a promoter, a ...
★リンクテーブル★
[★]
- 英
- chloramphenicol O-acetyltransferase
- 関
- クロラムフェニコールアセチルトランスフェラーゼ、クロラムフェニコール-O-アセチルトランスフェラーゼ
[★]
- 英
- chloramphenicol O-acetyltransferase
- 関
- クロラムフェニコール-O-アセチル基転移酵素
[★]
アセチルトランスフェラーゼ、アセチル基転移酵素、アセチル化酵素
- 関
- transacetylase
[★]
- 同
- 食道入口部
[★]
クロラムフェニコール
[★]
オスミウム osmium