アラニンtRNAリガーゼ
- 関
- alanyl-tRNA synthetase
WordNet
- a crystalline amino acid that occurs in many proteins
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/04/25 17:26:28」(JST)
[Wiki en表示]
| alanine-tRNA ligase |
| Identifiers |
| EC number |
6.1.1.7 |
| CAS number |
9031-71-4 |
| 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 |
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In enzymology, an alanine-tRNA ligase (EC 6.1.1.7) is an enzyme that catalyzes the chemical reaction
- ATP + L-alanine + tRNAAla AMP + diphosphate + L-alanyl-tRNAAla
The 3 substrates of this enzyme are ATP, L-alanine, and tRNA(Ala), whereas its 3 products are AMP, diphosphate, and L-alanyl-tRNA(Ala).
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-alanine:tRNAAla ligase (AMP-forming). Other names in common use include alanyl-tRNA synthetase, alanyl-transfer ribonucleate synthetase, alanyl-transfer RNA synthetase, alanyl-transfer ribonucleic acid synthetase, alanine-transfer RNA ligase, alanine transfer RNA synthetase, alanine tRNA synthetase, alanine translase, alanyl-transfer ribonucleate synthase, AlaRS, and Ala-tRNA synthetase. This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis.
See also
- Sticky mouse - mutation in the gene
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1RIQ, 1V4P, 1YFR, 1YFS, 1YFT, 1YGB, and 2E1B.
References
- HOLLEY RW, GOLDSTEIN J (1959). "An alanine-dependent, ribonuclease-inhibited conversion of adenosine 5'-phosphate to adenosine triphosphate. II. Reconstruction of the system from purified components". J. Biol. Chem. 234 (7): 1765–8. PMID 13672960.
- Webster GC (1961). "Isolation of an alanine-activating enzyme from pig liver". Biochim. Biophys. Acta 49: 141–152. doi:10.1016/0006-3002(61)90877-0. PMID 13783653.
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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 (I, II) - 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
- 3.1.3.48
- 3.4.21
- 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 |
Polyketide synthase
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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
- 3.1.3.48
- 3.4.21
- 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 |
DNA ligase
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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
- 3.1.3.48
- 3.4.21
- 4.1
- 5.1
- 6.1-3
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UpToDate Contents
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English Journal
- Compound heterozygous mutations in glycyl-tRNA synthetase are a proposed cause of systemic mitochondrial disease.
- McMillan HJ1, Schwartzentruber J, Smith A, Lee S, Chakraborty P, Bulman DE, Beaulieu CL, Majewski J, Boycott KM, Geraghty MT.
- BMC medical genetics.BMC Med Genet.2014 Mar 26;15:36. doi: 10.1186/1471-2350-15-36.
- BACKGROUND: Glycyl-tRNA synthetase (GARS) is an aminoacyl-tRNA synthetase (ARS) that links the amino acid glycine to its corresponding tRNA prior to protein translation and is one of three bifunctional ARS that are active within both the cytoplasm and mitochondria. Dominant mutations in GARS cause r
- PMID 24669931
- Natural reassignment of CUU and CUA sense codons to alanine in Ashbya mitochondria.
- Ling J1, Daoud R, Lajoie MJ, Church GM, Söll D, Lang BF.
- Nucleic acids research.Nucleic Acids Res.2014 Jan;42(1):499-508. doi: 10.1093/nar/gkt842. Epub 2013 Sep 17.
- The discovery of diverse codon reassignment events has demonstrated that the canonical genetic code is not universal. Studying coding reassignment at the molecular level is critical for understanding genetic code evolution, and provides clues to genetic code manipulation in synthetic biology. Here w
- PMID 24049072
- Lipid II-independent trans editing of mischarged tRNAs by the penicillin resistance factor MurM.
- Shepherd J1, Ibba M.
- The Journal of biological chemistry.J Biol Chem.2013 Sep 6;288(36):25915-23. doi: 10.1074/jbc.M113.479824. Epub 2013 Jul 18.
- Streptococcus pneumoniae is a causative agent of nosocomial infections such as pneumonia, meningitis, and septicemia. Penicillin resistance in S. pneumoniae depends in part upon MurM, an aminoacyl-tRNA ligase that attaches L-serine or L-alanine to the stem peptide lysine of Lipid II in cell wall pep
- PMID 23867453
★リンクテーブル★
[★]
アラニルtRNA合成酵素、アラニルtRNAシンテターゼ
- 関
- alanine-tRNA ligase
[★]
- 英
- alanine-tRNA ligase
- 関
- アラニルtRNA合成酵素
[★]
ファニルアラニンtRNAリガーゼ
- 関
- phenylalanyl-tRNA synthetase
[★]
アラニン
- 関
- A、Ala、alanyl、L-alanine
[★]
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