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any of various enzymes that move a chemical group from one compound to another compound

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/09/12 19:52:07」(JST)

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The Peptidyl transferase is an aminoacyltransferase (EC 2.3.2.12) as well as the primary enzymatic function of the ribosome, which forms peptide bonds between adjacent amino acids using tRNAs during the translation process of protein biosynthesis.

Peptidyl transferase activity is carried out by the ribosome. Peptidyl transferase activity is not mediated by any ribosomal proteins but by ribosomal RNA (rRNA), a ribozyme. This RNA relic is the most significant piece of evidence supporting the RNA World hypothesis.

In Prokaryotes, the 50S (23S component) ribosome subunit contains the peptidyl transferase component and acts as a ribozyme.
In Eukaryotes, the 60S (28S component) ribosome subunit contains the peptidyl transferase component and acts as the ribozyme.

Peptidyl transferases are not limited to translation, but there are relatively few enzymes with this function.

Antibiotic target

The following protein synthesis inhibitors target peptidyl transferase:

Chloramphenicol binds^[1] to A2451 and A2452 residues in the 23S rRNA of the ribosome and inhibits peptide bond formation.
Pleuromutilins also bind to peptidyl transferase.^[2]
Macrolide antibiotics are thought to inhibit peptidyl transferase, in addition to inhibiting ribosomal translocation.^[3]

References

^ Gu Z, Harrod R, Rogers EJ, Lovett PS (June 1994). "Anti-peptidyl transferase leader peptides of attenuation-regulated chloramphenicol-resistance genes". Proc. Natl. Acad. Sci. U.S.A. 91 (12): 5612–6. doi:10.1073/pnas.91.12.5612. PMC 44046. PMID 7515506.
^ Long, Katherine S; Hansen, LH; Jakobsen, L; Vester, B (April 2006). "Interaction of Pleuromutilin Derivatives with the Ribosomal Peptidyl Transferase Center" (PDF). Antimicrobial Agents and Chemotherapy 50 (4): 1458–1462. doi:10.1128/AAC.50.4.1458-1462.2006. PMC 1426994. PMID 16569865.
^ Protein synthesis inhibitors: macrolides mechanism of action animation. Classification of agents Pharmamotion. Author: Gary Kaiser. The Community College of Baltimore County. Retrieved on July 31, 2009

External links

Peptidyl transferases at the US National Library of Medicine Medical Subject Headings (MeSH)

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English Journal

High-resolution crystal structures of ribosome-bound chloramphenicol and erythromycin provide the ultimate basis for their competition.

Svetlov MS, Plessa E, Chen CW, Bougas A, Krokidis MG, Dinos GP, Polikanov YS.
RNA (New York, N.Y.). 2019 May;25(5)600-606.
The 70S ribosome is a major target for antibacterial drugs. Two of the classical antibiotics, chloramphenicol (CHL) and erythromycin (ERY), competitively bind to adjacent but separate sites on the bacterial ribosome: the catalytic peptidyl transferase center (PTC) and the nascent polypeptide exit tu
PMID 30733327

Protein expression profiles in Bathymodiolus azoricus exposed to cadmium.

Company R, Antúnez O, Cosson RP, Serafim A, Shillito B, Cajaraville M, Bebianno MJ, Torreblanca A.
Ecotoxicology and environmental safety. 2019 Apr;171()621-630.
Proteomic changes in the "gill-bacteria complex" of the hydrothermal vent mussel B. azoricus exposed to cadmium in pressurized chambers ((Incubateurs Pressurises pour l'Observation en Culture d'Animaux Marins Profonds - IPOCAMP) were analyzed and compared with the non-exposed control group. 2-D Fluo
PMID 30658297

Structural insights into unique features of the human mitochondrial ribosome recycling.

Koripella RK, Sharma MR, Risteff P, Keshavan P, Agrawal RK.
Proceedings of the National Academy of Sciences of the United States of America. 2019 Apr;().
Mammalian mitochondrial ribosomes (mitoribosomes) are responsible for synthesizing proteins that are essential for oxidative phosphorylation (ATP generation). Despite their common ancestry with bacteria, the composition and structure of the human mitoribosome and its translational factors are signif
PMID 30962385

Japanese Journal

Single mutations introduced in the essential ribosomal proteins L3 and S10 cause a sporulation defect in Bacillus subtilis

Akanuma Genki,Suzuki Shota,Yano Koichi,Nanamiya Hideaki,Natori Yousuke,Namba Eri,Watanabe Kazuya,Tagami Kazumi,Takeda Takuya,Iizuka Yuka,Kobayashi Ako,Ishizuka Morio,Yoshikawa Hirofumi,Kawamura Fujio
The Journal of General and Applied Microbiology 59(2), 105-117, 2013
… Mutant cells harboring the G52D mutation in the L3 ribosomal protein, which is located at the peptidyl transferase center of 50S, accumulated 30S subunit at 45°C, probably due to a defect in 50S formation, and exhibited a reduction in the sporulation frequency at high temperature. …
NAID 130004449359

リボソームにおけるペプチド生成機構の起源

田村浩二
Viva origino 39(1-4), 31-37, 2012-06-20
… The ribosome is a supercomplex of ribonucleoprotein particles containing both RNAs and proteins, and the peptide bond is produced on the peptidyl transferase center (PTC) of the large subunit of the ribosome. …
NAID 110009470535

ONIOM Study of a Proton Shuttle-Catalyzed Stepwise Mechanism for Peptide Bond Formation in the Ribosome

Fukushima Kazuaki,Iwahashi Hideo,Nishikimi Morimitsu
Bulletin of the Chemical Society of Japan 85(10), 1093-1101, 2012
… The exact reaction mechanism for peptide bond formation in the peptidyl transferase center of the ribosome is, however, still unknown. …
NAID 130004152991

Related Pictures

★リンクテーブル★

リンク元	「ペプチド生成酵素」「peptidyltransferase」「ペプチド転移酵素」「ペプチジルトランスフェラーゼ」
関連記事	「transferase」「transferases」