リジンtRNAリガーゼ
- 関
- lysyl-tRNA synthetase
WordNet
- any substance (such as an antibody) or agent that can cause lysis
- an essential amino acid found in proteins; occurs especially in gelatin and casein
PrepTutorEJDIC
- リジン(細胞溶解素), = lysine
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/04/01 16:07:15」(JST)
[Wiki en表示]
| lysine-tRNA ligase |
| Identifiers |
| EC number |
6.1.1.6 |
| CAS number |
9031-26-9 |
| 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 |
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In enzymology, a lysine-tRNA ligase (EC 6.1.1.6) is an enzyme that catalyzes the chemical reaction
- ATP + L-lysine + tRNALys AMP + diphosphate + L-lysyl-tRNALys
The 3 substrates of this enzyme are ATP, L-lysine, and tRNA(Lys), whereas its 3 products are AMP, diphosphate, and L-lysyl-tRNA(Lys).
This enzyme belongs to the family of ligases, to be specific, those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-lysine:tRNALys ligase (AMP-forming). Other names in common use include lysyl-tRNA synthetase, lysyl-transfer ribonucleate synthetase, lysyl-transfer RNA synthetase, L-lysine-transfer RNA ligase, lysine-tRNA synthetase, and lysine translase. This enzyme participates in 3 metabolic pathways: lysine biosynthesis, aminoacyl-trna biosynthesis, and amyotrophic lateral sclerosis (als).
References
- Allen, E. H.; Glassman, E; Schweet, R. S. (1960). "Incorporation of amino acids into ribonucleic acid. I. The role of activating enzymes". J. Biol. Chem. 235: 1061–7. PMID 13792726.
- Chlumecka, V.; Von Tigerstrom, M.; D'Obrenan, P; Smith, C. J. (1969). "Purification and properties of lysyl transfer ribonucleic acid synthetase from baker's yeast". J. Biol. Chem. 244 (20): 5481–8. PMID 4310598.
- Lagerkvist, U.; Rymo, L.; Lindqvist, O.; Andersson, E. (1972). "Some properties of crystals of lysine transfer ribonucleic acid ligase from yeast". J. Biol. Chem. 247 (12): 3897–9. PMID 4555953.
- Stern, R.; Mehler, A. H. (1965). "Lysyl-sRNA synthetase from Escherichia coli". Biochem. Z. 342 (4): 400–9. PMID 4284804.
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Enzymes: CO CS and CN ligases (EC 6.1-6.3)
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| 6.1: Carbon-Oxygen |
- Aminoacyl tRNA synthetase
- Tyrosine
- Tryptophan
- Threonine
- Leucine
- Isoleucine
- Lysine
- Alanine
- Valine
- Methionine
- Serine
- Aspartate
- D-alanine-poly(phosphoribitol) ligase
- Glycine
- Proline
- Cysteine
- Glutamate
- Glutamine
- Arginine
- Phenylalanine
- Histidine
- Asparagine
- Aspartate
- Glutamate
- Lysine
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| 6.2: Carbon-Sulfur |
- Succinyl coenzyme A synthetase - Acetyl Co-A synthetase - Long fatty acyl CoA synthetase
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| 6.3: Carbon-Nitrogen |
- Glutamine synthetase
- Ubiquitin ligase
- Cullin
- Von Hippel-Lindau tumor suppressor
- UBE3A
- Mdm2
- Anaphase-promoting complex
- UBR1
- Glutathione synthetase
- CTP synthase
- Adenylosuccinate synthase
- Argininosuccinate synthetase
- Holocarboxylase synthetase
- GMP synthase
- Asparagine synthetase
- Carbamoyl phosphate synthetase
- Gamma-glutamylcysteine synthetase
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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Ligases: carbon-carbon ligases (EC 6.4)
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|
| Biotin dependent carboxylase |
- Pyruvate carboxylase
- Acetyl-CoA carboxylase
- Propionyl-CoA carboxylase
- Methylcrotonyl-CoA carboxylase
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| Other |
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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Enzymes: Phosphoric ester and nitrogen-metal ligases (EC 6.5-6.6)
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| 6.5: Phosphoric Ester |
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| 6.6: Nitrogen-Metal |
- Magnesium chelatase
- Cobaltochelatase
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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UpToDate Contents
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English Journal
- Molecular evolution of protein-RNA mimicry as a mechanism for translational control.
- Katz A1, Solden L, Zou SB, Navarre WW, Ibba M.
- Nucleic acids research.Nucleic Acids Res.2014 Mar;42(5):3261-71. doi: 10.1093/nar/gkt1296. Epub 2013 Dec 13.
- Elongation factor P (EF-P) is a conserved ribosome-binding protein that structurally mimics tRNA to enable the synthesis of peptides containing motifs that otherwise would induce translational stalling, including polyproline. In many bacteria, EF-P function requires post-translational modification w
- PMID 24335280
- Chemical inhibition of prometastatic lysyl-tRNA synthetase-laminin receptor interaction.
- Kim DG1, Lee JY1, Kwon NH2, Fang P3, Zhang Q4, Wang J3, Young NL5, Guo M3, Cho HY6, Mushtaq AU6, Jeon YH6, Choi JW7, Han JM2, Kang HW8, Joo JE8, Hur Y8, Kang W9, Yang H9, Nam DH9, Lee MS10, Lee JW10, Kim ES11, Moon A11, Kim K2, Kim D2, Kang EJ12, Moon Y12, Rhee KH10, Han BW10, Yang JS13, Han G13, Yang WS2, Lee C14, Wang MW15, Kim S16.
- Nature chemical biology.Nat Chem Biol.2014 Jan;10(1):29-34. doi: 10.1038/nchembio.1381. Epub 2013 Nov 10.
- Lysyl-tRNA synthetase (KRS), a protein synthesis enzyme in the cytosol, relocates to the plasma membrane after a laminin signal and stabilizes a 67-kDa laminin receptor (67LR) that is implicated in cancer metastasis; however, its potential as an antimetastatic therapeutic target has not been explore
- PMID 24212136
- Spectrophotometric detection of histidine and lysine using combined enzymatic reactions.
- Kugimiya A1, Takamitsu E.
- Materials science & engineering. C, Materials for biological applications.Mater Sci Eng C Mater Biol Appl.2013 Dec 1;33(8):4867-70. doi: 10.1016/j.msec.2013.08.004. Epub 2013 Aug 15.
- An amino acid-sensing system with absorption spectrophotometric detection was developed. To ensure specific recognition of each amino acid, aminoacyl-tRNA synthetases were employed and the concentration of NADH produced by way of several enzymatic reactions was measured. Using this detection system,
- PMID 24094198
Japanese Journal
- Lysyl-tRNA Synthetase from Bacillus stearothermophilus. Stopped-Flow Kinetic Analysis of Enzyme-Lysyladenylate Formation.
- Lysyl-tRNA Synthetase from Bacillus stearothermophilus. Formation and Isolation of an EnzymeLysyladenylate Complex and Its Analogue.
- Lysyl-tRNA Synthetase from Bacillus stearothermophilus. Purification, and Fluorometric and Kinetic Analysis of the Binding of Substrates, L-Lysine and ATP.
Related Links
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★リンクテーブル★
[★]
リジルtRNA合成酵素、リジルtRNAシンテターゼ
- 関
- lysine-tRNA ligase
[★]
- 英
- lysine-tRNA ligase
- 関
- リジルtRNA合成酵素
[★]
トランスファーRNA, transfer RNA, 転位RNA
[★]
リガーゼ、連結酵素
- 関
- synthetase
[★]
トランスファーRNA transfer RNAs
[★]
tRNAリガーゼ
- 関
- RNA ligase