ペプチジルトランスフェラーゼ、ペプチド生成酵素
- 関
- peptidyl transferase、transpeptidase
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/07/26 02:20:39」(JST)
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Peptidyl transferase |
Identifiers |
EC number |
2.3.2.12 |
CAS number |
9059-29-4 |
Databases |
IntEnz |
IntEnz view |
BRENDA |
BRENDA entry |
ExPASy |
NiceZyme view |
KEGG |
KEGG entry |
MetaCyc |
metabolic pathway |
PRIAM |
profile |
PDB structures |
RCSB PDB PDBe PDBsum |
Search |
PMC |
articles |
PubMed |
articles |
NCBI |
proteins |
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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. Ribozymes are the only enzymes which are not made up of proteins, but ribonucleotides. All other enzymes are made up of proteins. 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.
Contents
- 1 Antibiotic target
- 2 See also
- 3 References
- 4 External links
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]
See also
- Transferase
- Translation
- Enzyme
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)
Protein biosynthesis: translation (prokaryotic, eukaryotic)
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Proteins |
Initiation factor |
Prokaryotic |
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Archaeal |
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Eukaryotic |
eIF1 |
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eIF2 |
- EIF2S1
- EIF2S2
- EIF2S3
- EIF2B1
- EIF2B2
- EIF2B3
- EIF2B4
- EIF2B5
- EIF-2 kinase
- eIF2A
- eIF2D
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eIF3 |
- EIF3A
- B
- C
- D
- E
- F
- G
- H
- I
- J
- K
- L
- M
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eIF4 |
- EIF4A2
- A3
- B
- E1
- E2
- E3
- G1
- G2
- G3
- H
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eIF5 |
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eIF6 |
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Elongation factor |
Prokaryotic |
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Archaeal |
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Eukaryotic |
- EEF-1
- EEF1A1
- EEF1A2
- EEF1A3
- EEF1B1
- EEF1B2
- EEF1B3
- EEF1B4
- EEF1D
- EEF1E1
- EEF1G
- EEF2
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Release factor |
- Prokaryotic
- Archaeal
- Eukaryotic (ETF1)
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Ribosomal Proteins |
- RPS1
- RPS2
- RPS3
- RPS4
- RPS5
- RPS6
- RPS7
- RPS8
- RPS9
- RPS10
- RPS11
- RPS12
- RPS13
- RPS14
- RPS15
- RPS16
- RPS17
- RPS18
- RPS19
- RPS20
- RPS21
- RPS22
- RPS23
- RPS24
- RPS25
- RPS26
- RPS27
- RPS28
- RPS29
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Other concepts |
- Aminoacyl tRNA synthetase
- Reading frame
- Start codon
- Stop codon
- Shine-Dalgarno sequence/Kozak consensus sequence
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Transferases: acyltransferases (EC 2.3)
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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
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2.3.2: Aminoacyltransferases |
- Gamma-glutamyl transpeptidase
- Peptidyl transferase
- Transglutaminase
- Tissue transglutaminase
- Keratinocyte transglutaminase
- Factor XIII
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2.3.3: converted into alkyl on transfer |
- Citrate synthase
- ATP citrate lyase
- HMG-CoA synthase
- Malate synthase
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Enzymes
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Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
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Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
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UpToDate Contents
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- 1. 腸球菌感染症の治療 treatment of enterococcal infections
English Journal
- Characterization of Discrete Phosphopantetheinyl Transferases in Streptomyces tsukubaensis L19 Unveils a Complicate Phosphopantetheinylation Network.
- Wang YY1, Zhang XS1, Luo HD1, Ren NN1, Jiang XH1, Jiang H1, Li YQ2,3.
- Scientific reports.Sci Rep.2016 Apr 7;6:24255. doi: 10.1038/srep24255.
- Phosphopantetheinyl transferases (PPTases) play essential roles in both primary metabolisms and secondary metabolisms via post-translational modification of acyl carrier proteins (ACPs) and peptidyl carrier proteins (PCPs). In this study, an industrial FK506 producing strain Streptomyces tsukubaensi
- PMID 27052100
- Translation regulation via nascent polypeptide-mediated ribosome stalling.
- Wilson DN1, Arenz S2, Beckmann R3.
- Current opinion in structural biology.Curr Opin Struct Biol.2016 Apr;37:123-33. doi: 10.1016/j.sbi.2016.01.008. Epub 2016 Feb 7.
- As the nascent polypeptide chain is being synthesized, it passes through a tunnel within the large ribosomal subunit. Interaction between the nascent polypeptide chain and the ribosomal tunnel can modulate the translation rate and induce translational stalling to regulate gene expression. In this ar
- PMID 26859868
- The substrate promiscuity of a phosphopantetheinyl transferase SchPPT for coenzyme A derivatives and acyl carrier proteins.
- Wang YY1, Luo HD1, Zhang XS1, Lin T2, Jiang H3, Li YQ1.
- Archives of microbiology.Arch Microbiol.2016 Mar;198(2):193-7. doi: 10.1007/s00203-015-1179-z. Epub 2016 Jan 9.
- Phosphopantetheinyl transferases (PPTases) catalyze the posttranslational modification of acyl carrier proteins (ACPs) in fatty acid synthases (FASs), ACPs in polyketide synthases, and peptidyl carrier proteins (PCPs) in nonribosomal peptide synthetases (NRPSs) in all organisms. Some bacterial PPTas
- PMID 26748983
Japanese Journal
- Ribosomal protein L3 mediated the transport of digoxin in Xenopus laevis oocyte
- Kobayashi Yasuna,Kawakami Kanako,Ohbayashi Masayuki [他],KOHYAMA Noriko,YAMAMOTO Toshinori
- Journal of toxicological sciences 35(6), 827-834, 2010-12-01
- … Ribosomal protein L3 (RPL3) is known to be an indispensable and essential component for the peptidyltransferase center. …
- NAID 10026962974
- Structures of five antibiotics bound at the peptidyltransferase center of the large ribosomal subunit
- Decreased peptidyltransferase activity correlates with increased programmed-1 ribosomal frameshifting and viral maintenance defects in the yeast Saccharomyces cerevisiae
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- 英
- peptidyl transferase、peptidyltransferase
- 関
- ペプチジルトランスフェラーゼ、ペプチド転移酵素