スレオニンtRNAリガーゼ、トレオニンtRNAリガーゼ
- 関
- threonyl-tRNA synthetase
WordNet
- a colorless crystalline amino acid found in protein; occurs in the hydrolysates of certain proteins; an essential component of human nutrition
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/01/04 00:40:01」(JST)
[Wiki en表示]
| threonine-tRNA ligase |
| Identifiers |
| EC number |
6.1.1.3 |
| CAS number |
9023-46-5 |
| 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 threonine-tRNA ligase (EC 6.1.1.3) is an enzyme that catalyzes the chemical reaction
- ATP + L-threonine + tRNAThr AMP + diphosphate + L-threonyl-tRNAThr
The 3 substrates of this enzyme are ATP, L-threonine, and tRNA(Thr), whereas its 3 products are AMP, diphosphate, and L-threonyl-tRNA(Thr).
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-threonine:tRNAThr ligase (AMP-forming). Other names in common use include threonyl-tRNA synthetase, threonyl-transfer ribonucleate synthetase, threonyl-transfer RNA synthetase, threonyl-transfer ribonucleic acid synthetase, threonyl ribonucleic synthetase, threonine-transfer ribonucleate synthetase, threonine translase, threonyl-tRNA synthetase, and TRS. This enzyme participates in glycine, serine and threonine metabolism and aminoacyl-trna biosynthesis.
Structural studies
As of late 2007, 17 structures have been solved for this class of enzymes, with PDB accession codes 1EVK, 1EVL, 1FYF, 1KOG, 1NYQ, 1NYR, 1QF6, 1TJE, 1TKE, 1TKG, 1TKY, 1WWT, 1Y2Q, 2HKZ, 2HL0, 2HL1, and 2HL2.
References
- ALLEN EH, GLASSMAN E, SCHWEET RS (1960). "Incorporation of amino acids into ribonucleic acid. I. The role of activating enzymes". J. Biol. Chem. 235: 1061–7. PMID 13792726.
- HOLLEY RW, BRUNNGRABER EF, SAAD F, WILLIAMS HH (1961). "Partial purification of the threonine- and tyrosine-activating enzymes from rat liver, and the effect of patassium ions on the activity of the tyrosine enzyme". J. Biol. Chem. 236: 197–9. PMID 13715350.
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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
- Alanine
- Arginine
- Asparagine
- Aspartate
- Cysteine
- D-alanine—poly(phosphoribitol) ligase
- Glutamate
- Glutamine
- Glycine
- Histidine
- Isoleucine
- Leucine
- Lysine
- Methionine
- Phenylalanine
- Proline
- Serine
- Threonine
- Tryptophan
- Tyrosine
- Valine
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|
| 6.2: Carbon-Sulfur |
- Succinyl coenzyme A synthetase
- Acetyl—CoA synthetase
- Long-chain-fatty-acid—CoA ligase
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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 synthetase
- Adenylosuccinate synthase
- Argininosuccinate synthase
- Holocarboxylase synthetase
- GMP synthase
- Asparagine synthetase
- Carbamoyl phosphate synthetase
- Glutamate–cysteine ligase
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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
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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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| Kinetics |
- Enzyme kinetics
- Eadie–Hofstee diagram
- Hanes–Woolf plot
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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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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English Journal
- Mutations in LARS2, encoding mitochondrial leucyl-tRNA synthetase, lead to premature ovarian failure and hearing loss in Perrault syndrome.
- Pierce SB, Gersak K, Michaelson-Cohen R, Walsh T, Lee MK, Malach D, Klevit RE, King MC, Levy-Lahad E.SourceDivision of Medical Genetics, Department of Medicine, University of Washington, Seattle WA 98195, USA. sbpierce@uw.edu
- American journal of human genetics.Am J Hum Genet.2013 Apr 4;92(4):614-20. doi: 10.1016/j.ajhg.2013.03.007. Epub 2013 Mar 28.
- The genetic causes of premature ovarian failure (POF) are highly heterogeneous, and causative mutations have been identified in more than ten genes so far. In two families affected by POF accompanied by hearing loss (together, these symptoms compose Perrault syndrome), exome sequencing revealed muta
- PMID 23541342
- Amino acid signalling upstream of mTOR.
- Jewell JL, Russell RC, Guan KL.SourceDepartment of Pharmacology and Moores Cancer Center, University of California, San Diego, La Jolla, California 92093, USA.
- Nature reviews. Molecular cell biology.Nat Rev Mol Cell Biol.2013 Mar;14(3):133-9. doi: 10.1038/nrm3522. Epub 2013 Jan 30.
- Mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that is part of mTOR complex 1 (mTORC1), a master regulator that couples amino acid availability to cell growth and autophagy. Multiple cues modulate mTORC1 activity, such as growth factors, stress, energy status and amino acids. Alt
- PMID 23361334
- Identification of bacteria-selective threonyl-tRNA synthetase substrate inhibitors by structure-based design.
- Teng M, Hilgers MT, Cunningham ML, Borchardt A, Locke JB, Abraham S, Haley G, Kwan BP, Hall C, Hough GW, Shaw KJ, Finn J.SourceMedicinal Chemistry, Trius Therapeutics, Inc., 6310 Nancy Ridge Drive, San Diego, California 92121, United States. mteng@triusrx.com
- Journal of medicinal chemistry.J Med Chem.2013 Feb 28;56(4):1748-60. doi: 10.1021/jm301756m. Epub 2013 Feb 12.
- A series of potent and bacteria-selective threonyl-tRNA synthetase (ThrRS) inhibitors have been identified using structure-based drug design. These compounds occupied the substrate binding site of ThrRS and showed excellent binding affinities for all of the bacterial orthologues tested. Some of the
- PMID 23362938
Related Links
- actin cytoskeleton, cytoplasm, cytosol, extracellular exosome, protein homodimerization activity, RNA binding, threonine-tRNA ligase activity, threonyl-tRNA aminoacylation, translation, tRNA aminoacylation for protein translation ... ...
- In enzymology, a threonine-tRNA ligase (EC 6.1.1.3) is an enzyme that catalyzes the chemical reaction ATP + L-threonine + tRNAThr AMP + diphosphate + L-threonyl-tRNAThr The 3 substrates of this enzyme are ATP, L-threonine, and tRNA(Thr), whereas its 3 ...
★リンクテーブル★
[★]
スレオニルtRNA合成酵素、スレオニルtRNAシンテターゼ
- 関
- threonine-tRNA ligase
[★]
- 英
- threonine-tRNA ligase
- 関
- スレオニルtRNA合成酵素、トレオニンtRNAリガーゼ
[★]
- 英
- threonine-tRNA ligase
- 関
- スレオニンtRNAリガーゼ
[★]
トランスファーRNA, transfer RNA, 転位RNA
[★]
リガーゼ、連結酵素
- 関
- synthetase
[★]
スレオニン L-threonine T Thr
[★]
トランスファーRNA transfer RNAs
[★]
tRNAリガーゼ
- 関
- RNA ligase