メチオニンtRNAリガーゼ
- 関
- methionyl-tRNA synthetase
WordNet
- a crystalline amino acid containing sulfur; found in most proteins and essential for nutrition
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2013/03/15 16:44:54」(JST)
[Wiki en表示]
methionine-tRNA ligase |
Identifiers |
EC number |
6.1.1.10 |
CAS number |
9033-22-1 |
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 methionine-tRNA ligase (EC 6.1.1.10) is an enzyme that catalyzes the chemical reaction
- ATP + L-methionine + tRNAMet AMP + diphosphate + L-methionyl-tRNAMet
The 3 substrates of this enzyme are ATP, L-methionine, and tRNA(Met), whereas its 3 products are AMP, diphosphate, and L-methionyl-tRNA(Met).
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-methionine:tRNAMet ligase (AMP-forming). Other names in common use include methionyl-tRNA synthetase, methionyl-transfer ribonucleic acid synthetase, methionyl-transfer ribonucleate synthetase, methionyl-transfer RNA synthetase, methionine translase, and MetRS. This enzyme participates in 3 metabolic pathways: methionine metabolism, selenoamino acid metabolism, and aminoacyl-trna biosynthesis.
Structural studies
As of late 2007, 21 structures have been solved for this class of enzymes, with PDB accession codes 1A8H, 1F4L, 1MEA, 1MED, 1MKH, 1P7P, 1PFU, 1PFV, 1PFW, 1PFY, 1PG0, 1PG2, 1QQT, 1RQG, 1WOY, 2CSX, 2CT8, 2D54, 2D5B, 2DJV, and 2HSN.
References
- Bergmann FH, Berg P and 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.
- Lee CP, Dyson MR, Mandal N, Varshney U, Bahramian B, RajBhandary UL (1992). "Striking effects of coupling mutations in the acceptor stem on recognition of tRNAs by Escherichia coli Met-tRNA synthetase and Met-tRNA transformylase". Proc. Natl. Acad. Sci. U.S.A. 89 (19): 9262–6. doi:10.1073/pnas.89.19.9262. PMC 50106. PMID 1409632. //www.ncbi.nlm.nih.gov/pmc/articles/PMC50106/.
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
- 2.7.10
- 2.7.11-12
- 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
- 2.7.10
- 2.7.11-12
- 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
- 2.7.10
- 2.7.11-12
- 3.1
- 4.1
- 5.1
- 6.1-3
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UpToDate Contents
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English Journal
- MYC-driven inhibition of the glutamate-cysteine ligase promotes glutathione depletion in liver cancer.
- Anderton B1,2, Camarda R1,2, Balakrishnan S1,2, Balakrishnan A1,2,3, Kohnz RA4, Lim L1,2, Evason KJ5, Momcilovic O1,2, Kruttwig K1,2, Huang Q6, Xu G6, Nomura DK4, Goga A7,2.
- EMBO reports.EMBO Rep.2017 Apr;18(4):569-585. doi: 10.15252/embr.201643068. Epub 2017 Feb 20.
- PMID 28219903
- A genetic assay for gene essentiality in Clostridium.
- Walker DJ1, Heap JT1, Winzer K1, Minton NP2.
- Anaerobe.Anaerobe.2016 Dec;42:40-43. doi: 10.1016/j.anaerobe.2016.07.007. Epub 2016 Jul 31.
- PMID 27487328
- Targeting methionyl tRNA synthetase: design, synthesis and antibacterial activity against Clostridium difficile of novel 3-biaryl-N-benzylpropan-1-amine derivatives.
- Eissa AG1,2, Blaxland JA1, Williams RO1, Metwally KA2, El-Adl SM2, Lashine el-SM2, Baillie LW1, Simons C1.
- Journal of enzyme inhibition and medicinal chemistry.J Enzyme Inhib Med Chem.2016 Dec;31(6):1694-7. doi: 10.3109/14756366.2016.1140754. Epub 2016 Feb 22.
- PMID 26899668
Related Pictures
★リンクテーブル★
[★]
メチオニルtRNA合成酵素、メチオニルtRNAシンテターゼ
- 関
- methionine-tRNA ligase
[★]
- 英
- methionine-tRNA ligase
- 関
- メチオニル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
[★]
メチオニン Met M