バリンtRNAリガーゼ
- 関
- valyl-tRNA synthetase
WordNet
- an essential amino acid found in proteins; important for growth in children and nitrogen balance in adults
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/10/16 13:06:57」(JST)
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valine-tRNA ligase |
Identifiers |
EC number |
6.1.1.9 |
CAS number |
9023-47-6 |
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 valine-tRNA ligase (EC 6.1.1.9) is an enzyme that catalyzes the chemical reaction
- ATP + L-valine + tRNAVal AMP + diphosphate + L-valyl-tRNAVal
The 3 substrates of this enzyme are ATP, L-valine, and tRNA(Val), whereas its 3 products are AMP, diphosphate, and L-valyl-tRNA(Val).
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-valine:tRNAVal ligase (AMP-forming). Other names in common use include valyl-tRNA synthetase, valyl-transfer ribonucleate synthetase, valyl-transfer RNA synthetase, valyl-transfer ribonucleic acid synthetase, valine transfer ribonucleate ligase, and valine translase. This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyl-trna biosynthesis.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1GAX, 1IVS, 1IYW, 1WK9, and 1WKA.
See also
References
- Berg P, Bergmann FH, Ofengand EJ, Dieckmann M (1961). "The enzymic synthesis of amino acyl derivatives of ribonucleic acid I. The mechanism of leucyl-, valyl-, isoleucyl- and methionyl ribonucleic acid formation". J. Biol. Chem. 236: 1726–1734.
- Bergmann FH, Berg P, Dieckmann M (1961). "The enzymic synthesis of amino acyl derivatives of ribonucleic acid II. The preparation of leucyl-, valyl-, isoleucyl- and methionyl ribonucleic acid synthetases from Escherichia coli". J. Biol. Chem. 236: 1735–1740.
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
- 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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English Journal
- Identification of distinctive molecular traits that are characteristic of the phylum "Deinococcus-Thermus" and distinguish its main constituent groups.
- Ho J1, Adeolu M1, Khadka B1, Gupta RS2.
- Systematic and applied microbiology.Syst Appl Microbiol.2016 Oct;39(7):453-463. doi: 10.1016/j.syapm.2016.07.003. Epub 2016 Jul 29.
- PMID 27506333
- Proteomic analysis of an environmental isolate of Rhodotorula mucilaginosa after arsenic and cadmium challenge: Identification of a protein expression signature for heavy metal exposure.
- Ilyas S1, Rehman A1, Coelho AV2, Sheehan D3.
- Journal of proteomics.J Proteomics.2016 Jun 1;141:47-56. doi: 10.1016/j.jprot.2016.04.012. Epub 2016 Apr 16.
- PMID 27090762
- WHITE PANICLE1, a Val-tRNA Synthetase Regulating Chloroplast Ribosome Biogenesis in Rice, Is Essential for Early Chloroplast Development.
- Wang Y1, Wang C1, Zheng M1, Lyu J1, Xu Y1, Li X1, Niu M1, Long W1, Wang D1, Wang H1, Terzaghi W1, Wang Y2, Wan J2.
- Plant physiology.Plant Physiol.2016 Apr;170(4):2110-23. doi: 10.1104/pp.15.01949. Epub 2016 Feb 2.
- PMID 26839129
Japanese Journal
- Valyl-tRNA synthetase from Bacillus stearothermophilus. Purification and Binding with the Substrates L-Valine and ATP(Biological Chemistry)
- KAKITANI Makoto,TONOMURA Ben'ichiro,HIROMI Keitaro
- Agricultural and Biological Chemistry 50(10), 2437-2444, 1986-10-23
- … Valyl-tRNA synthetase (L-valine:tRNA^<val> … ligase (AMP forming); … Enzyme activity in tRNA aminoacylation reaction increased as the temperature increased up to 52℃ at pH 7.6 and pH 8.5. … Ligand-induced decrease of the enzyme protein fluorescence was observed and used as a probe for studying the binding of substrates (L-valine and ATP) to VRS. …
- NAID 110006322713
Related Links
- In enzymology, a valine-tRNA ligase (EC 6.1.1.9) is an enzyme that catalyzes the chemical reaction ... This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds.
- Valine-tRNA ligase (also known as Valyl-tRNA synthetase) (EC:6.1.1.9) is an alpha monomer that belongs to class Ia ... The aminoacyl-tRNA synthetase (also known as aminoacyl-tRNA ligase) catalyse the attachment of an amino acid to its ...
★リンクテーブル★
[★]
バリルtRNA合成酵素、バリルtRNAシンテターゼ
- 関
- valine-tRNA ligase
[★]
- 英
- valine-tRNA ligase
- 関
- バリル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
[★]
バリン
- 関
- L-valine、V、Val
[★]
トランスファーRNA transfer RNAs
[★]
tRNAリガーゼ
- 関
- RNA ligase