システインtRNAリガーゼ
- 関
- cysteinyl-tRNA synthetase
WordNet
- an amino acid containing sulfur that is found in most proteins; oxidizes on exposure to air to form cystine
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2019/10/16 10:00:51」(JST)
[Wiki en表示]
| cysteine-tRNA ligase |
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| Identifiers |
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| EC number | 6.1.1.16 |
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| CAS number | 37318-56-2 |
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| Databases |
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| IntEnz | IntEnz view |
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| BRENDA | BRENDA entry |
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| ExPASy | NiceZyme view |
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| KEGG | KEGG entry |
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| MetaCyc | metabolic pathway |
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| PRIAM | profile |
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| PDB structures | RCSB PDB PDBe PDBsum |
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| Gene Ontology | AmiGO / QuickGO |
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| Search |
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| PMC | articles |
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| PubMed | articles |
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| NCBI | proteins |
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In enzymology, a cysteine-tRNA ligase (EC 6.1.1.16) is an enzyme that catalyzes the chemical reaction
- ATP + L-cysteine + tRNACys AMP + diphosphate + L-cysteinyl-tRNACys
The 3 substrates of this enzyme are ATP, L-cysteine, and tRNA(Cys), whereas its 3 products are AMP, diphosphate, and L-cysteinyl-tRNA(Cys).
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-cysteine:tRNACys ligase (AMP-forming). Other names in common use include cysteinyl-tRNA synthetase, cysteinyl-transferRNA synthetase, cysteinyl-transfer ribonucleate synthetase, and cysteine translase. This enzyme participates in cysteine metabolism and aminoacyl-trna biosynthesis.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1LI5, 1LI7, and 1U0B.
References
- Mccorquodale DJ (December 1964). "The separation and partial purification of aminoacyl-RNA synthetases from Escherichia coliI". Biochimica et Biophysica Acta. 91: 541–8. doi:10.1016/0926-6550(64)90001-5. PMID 14262440.
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
- Enzyme activator
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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)
- EC7 Translocases (list)
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UpToDate Contents
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English Journal
- X-ray crystallographic structure of BshC, a unique enzyme involved in bacillithiol biosynthesis.
- VanDuinen AJ1, Winchell KR, Keithly ME, Cook PD.
- Biochemistry.Biochemistry.2015 Jan 20;54(2):100-3. doi: 10.1021/bi501394q. Epub 2014 Dec 18.
- Bacillithiol is produced by many Gram-positive bacteria via a pathway utilizing the enzymes BshA, BshB, and BshC. Here we report the 1.77 Å resolution crystal structure of BshC, the putative cysteine ligase in bacillithiol production. The structure reveals that BshC contains a core Rossmann fold wi
- PMID 25496067
- A homozygous splice-site mutation in CARS2 is associated with progressive myoclonic epilepsy.
- Hallmann K1, Zsurka G1, Moskau-Hartmann S1, Kirschner J1, Korinthenberg R1, Ruppert AK1, Ozdemir O1, Weber Y1, Becker F1, Lerche H1, Elger CE1, Thiele H1, Nürnberg P1, Sander T1, Kunz WS2.
- Neurology.Neurology.2014 Dec 2;83(23):2183-7. doi: 10.1212/WNL.0000000000001055. Epub 2014 Oct 31.
- OBJECTIVE: We report a consanguineous family with 2 affected individuals whose clinical symptoms closely resembled MERRF (myoclonus epilepsy with ragged red fibers) syndrome including severe myoclonic epilepsy, progressive spastic tetraparesis, progressive impairment of vision and hearing, as well a
- PMID 25361775
- Ancient translation factor is essential for tRNA-dependent cysteine biosynthesis in methanogenic archaea.
- Liu Y1, Nakamura A2, Nakazawa Y3, Asano N3, Ford KA1, Hohn MJ1, Tanaka I4, Yao M5, Söll D6.
- Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2014 Jul 22;111(29):10520-5. doi: 10.1073/pnas.1411267111. Epub 2014 Jul 7.
- Methanogenic archaea lack cysteinyl-tRNA synthetase; they synthesize Cys-tRNA and cysteine in a tRNA-dependent manner. Two enzymes are required: Phosphoseryl-tRNA synthetase (SepRS) forms phosphoseryl-tRNA(Cys) (Sep-tRNA(Cys)), which is converted to Cys-tRNA(Cys) by Sep-tRNA:Cys-tRNA synthase (SepCy
- PMID 25002468
★リンクテーブル★
[★]
システイニルtRNA合成酵素、システイニルtRNAシンテターゼ
- 関
- cysteine-tRNA ligase
[★]
- 英
- cysteine-tRNA ligase
- 関
- システイニルtRNAシンテターゼ
[★]
トランスファーRNA, transfer RNA, 転位RNA
[★]
リガーゼ、連結酵素
- 関
- synthetase
[★]
トランスファーRNA transfer RNAs
[★]
tRNAリガーゼ
- 関
- RNA ligase