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an oral antibiotic (trade name Chloromycetin) used to treat serious infections (especially typhoid fever) (同)Chloromycetin

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/12/20 05:28:09」(JST)

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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.

This article incorporates text from the public domain Pfam and InterPro IPR001707

UpToDate Contents

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1. 髄膜炎菌感染の治療および予防 treatment and prevention of meningococcal infection
2. グラム陰性桿菌性髄膜炎：治療 gram negative bacillary meningitis treatment
3. ロッキー山紅斑熱の治療 treatment of rocky mountain spotted fever
4. 発疹熱の診断および治療 diagnosis and treatment of murine typhus
5. ツツガ虫病：治療および予防 scrub typhus treatment and prevention

English Journal

The Cellular Factor NXP2/MORC3 Is a Positive Regulator of Influenza Virus Multiplication.

Ver LS1, Marcos-Villar L1, Landeras-Bueno S1, Nieto A1, Ortín J2.
Journal of virology.J Virol.2015 Oct 1;89(19):10023-30. doi: 10.1128/JVI.01530-15. Epub 2015 Jul 22.
Transcription and replication of influenza A virus are carried out in the nuclei of infected cells in the context of viral ribonucleoproteins (RNPs). The viral polymerase responsible for these processes is a protein complex composed of the PB1, PB2, and PA proteins. We previously identified a set of
PMID 26202233

Unique plasmids generated via pUC replicon mutagenesis in an error-prone thermophile derived from Geobacillus kaustophilus HTA426.

Kobayashi J1, Tanabiki M2, Doi S2, Kondo A3, Ohshiro T2, Suzuki H4.
Applied and environmental microbiology.Appl Environ Microbiol.2015 Aug 28. pii: AEM.01574-15. [Epub ahead of print]
The plasmid pGKE75-catA138T, which comprises pUC18 and the catA138T gene encoding thermostable chloramphenicol acetyltransferase (CATA138T), serves as an Escherichia coli-Geobacillus kaustophilus shuttle plasmid that confers moderate chloramphenicol resistance on G. kaustophilus HTA426. The present
PMID 26319877

Selective retinol production by modulating the composition of retinoids from metabolically engineered E. coli.

Jang HJ1,2, Ha BK1, Zhou J1, Ahn J3, Yoon SH1, Kim SW4.
Biotechnology and bioengineering.Biotechnol Bioeng.2015 Aug;112(8):1604-12. doi: 10.1002/bit.25577. Epub 2015 May 12.
Retinoids can be produced from E. coli when introduced with the β-carotene biosynthesis pathway and the BCMO gene. E. coli has no inherent metabolic pathways related to retinoids, therefore only retinal should be produced from the cleavage of β-carotene by BCMO. However, retinol and retinyl acetat
PMID 25726762

Japanese Journal

ビワがんしゅ病細菌の病原性遺伝子psvAにコードされている蛋白質の機能解析

Kamiunten Hiroshi,Sakamaki Ikuko,Matsuo Mitsuhiro
宮崎大学農学部研究報告 57, 1-10, 2011-02-28
… To confirm our previous report that PsvA is associated with the outer membrane, a psvAN-chloramphenicol acetyltransferase (CAT) fusion gene (psvAN-CAT) was constructed and transformed into Pse PEO. …
NAID 120003913446

ビワがんしゅ病細菌の病原性遺伝子psvAにコードされている蛋白質の機能解析

上運天博,坂巻幾子,松尾光弘
宮崎大学農学部研究報告 57, 1-10, 2011-02-28
… （Cya）レポーターシステムを用いてPsvAが植物細胞内に分泌されることを明らかにした．PsvAが細菌の外膜に関連していることを以前に報告したが、そのことを確かめるため、psvAN遺伝子とChloramphenicol acetyltransferase （CAT）遺伝子を融合させ、Pseに導入し、CAT抗血清を用いてウエスターンブロッティングで調べた結果、PsvAN-CAT融合蛋白質は外膜と細胞質画分に検出された．なお、CATのみの場合は細胞質 …
NAID 110008672354

An Improved Transfection Assay for Evaluating the Effects of Heavy Metals

,
Industrial Health 47(4), 419-422, 2009
… Of the reporters we tested, luciferase (Luc) enzyme activity was affected by heavy metals, whereas gene product levels of the chloramphenicol acetyltransferase (CAT) or β-galactosidase (βGal) gene were not. …
NAID 130004483393

Related Pictures

★リンクテーブル★

リンク元	「CAT」「クロラムフェニコールアセチル基転移酵素」「クロラムフェニコールアセチルトランスフェラーゼ」「CaT」
関連記事	「acetyltransferase」「chloramphenicol」

「CAT」

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 / EGO
Search
PMC	articles
PubMed	articles
NCBI	proteins

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

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