アラニルtRNA合成酵素、アラニルtRNAシンテターゼ
- 関
- alanine-tRNA ligase
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/10/24 00:21:30」(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 |
| NCBI |
proteins |
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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
- 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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- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 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 carboxylation |
- Pyruvate carboxylase
- Acetyl-CoA carboxylase
- Propionyl-CoA carboxylase
- Methylcrotonyl-CoA carboxylase
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| Other |
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- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 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
- Cobalt chelatase
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- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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UpToDate Contents
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English Journal
- Divergent Alanyl-tRNA Synthetase Genes of Vanderwaltozyma polyspora Descended from a Common Ancestor through Whole-Genome Duplication Followed by Asymmetric Evolution.
- Chang CP1, Chang CY1, Lee YH1, Lin YS2, Wang CC3.
- Molecular and cellular biology.Mol Cell Biol.2015 Jul 1;35(13):2242-53. doi: 10.1128/MCB.00018-15. Epub 2015 Apr 20.
- Cytoplasmic and mitochondrial forms of a eukaryotic aminoacyl-tRNA synthetase (aaRS) are generally encoded by two distinct nuclear genes, one of eukaryotic origin and the other of mitochondrial origin. However, in most known yeasts, only the mitochondrial-origin alanyl-tRNA synthetase (AlaRS) gene i
- PMID 25896914
- Genotype/phenotype correlations in AARS-related neuropathy in a cohort of patients from the United Kingdom and Ireland.
- Bansagi B1, Antoniadi T, Burton-Jones S, Murphy SM, McHugh J, Alexander M, Wells R, Davies J, Hilton-Jones D, Lochmüller H, Chinnery P, Horvath R.
- Journal of neurology.J Neurol.2015 Jun 2. [Epub ahead of print]
- Charcot-Marie-Tooth disease (CMT) is the most common inherited neuropathy with heterogeneous clinical presentation and genetic background. The axonal form (CMT2) is characterised by decreased action potentials indicating primary axonal damage. The underlying pathology involves axonal degeneration wh
- PMID 26032230
- A novel AARS mutation in a family with dominant myeloneuropathy.
- Motley WW1, Griffin LB1, Mademan I1, Baets J1, De Vriendt E1, De Jonghe P1, Antonellis A1, Jordanova A1, Scherer SS2.
- Neurology.Neurology.2015 May 19;84(20):2040-7. doi: 10.1212/WNL.0000000000001583. Epub 2015 Apr 22.
- OBJECTIVE: To determine the genetic cause of neurodegeneration in a family with myeloneuropathy.METHODS: We studied 5 siblings in a family with a mild, dominantly inherited neuropathy by clinical examination and electrophysiology. One patient had a sural nerve biopsy. After ruling out common genetic
- PMID 25904691
Japanese Journal
- A Hamster Temperature-Sensitive Alanyl-tRNA Synthetase Mutant Causes Degradation of Cell-Cycle Related Proteins and Apoptosis
- Wang Yonggang,Sekiguchi Takeshi,Noguchi Eishi [他],NISHIMOTO Takeharu
- The journal of biochemistry 135(1), 7-16, 2004-01-01
- NAID 10016197271
- A Hamster Temperature-Sensitive Alanyl-tRNA Synthetase Mutant Causes Degradation of Cell-Cycle Related Proteins and Apoptosis
- Wang Yonggang,Sekiguchi Takeshi,Noguchi Eishi,Nishimoto Takeharu
- The Journal of Biochemistry 135(1), 7-16, 2004
- … We have isolated a temperature-sensitive alanyl-tRNA synthetase mutant from hamster BHK21 cells, designated as is ET12. … The mutation was localized between two RNA-binding domains of alanyl-tRNA synthetase. … Thus far, we have isolated two temperature-sensitive aminoacyl-tRNA synthetase mutants from the BHK21 cell line: is BN250 and is BN269. …
- NAID 130003418123
- Kinetic parameters for tmRNA binding to alanyl-tRNA synthetase and elongation factor Tu from Escherichia coli
Related Links
- The human alanyl-tRNA synthetase (AARS) belongs to a family of tRNA synthases, of the class II enzymes. Class II tRNA synthases evolved early in evolution and are highly conserved. This is reflected by the fact that ...
- McLaughlin et al. (2012) identified a heterozygous R329H mutation in affected members of an Australian family with CMT2N. The substitution occurs within a highly conserved residue in the tRNA-binding domain. Aminoacylation ...
★リンクテーブル★
[★]
- 英
- alanyl-tRNA synthetase
- 関
- アラニンtRNAリガーゼ、アラニルtRNAシンテターゼ
[★]
- 英
- alanyl-tRNA synthetase
- 関
- アラニルtRNA合成酵素
[★]
アラニンtRNAリガーゼ
- 関
- alanyl-tRNA synthetase
[★]
フェニルアラニルtRNA合成酵素、フェニルアラニルtRNAシンテターゼ
- 関
- phenylalanine-tRNA ligase
[★]
- 関
- ligase、synthase
[★]
アラニル、アラニンの
- 関
- A、Ala、alanine
[★]
トランスファーRNA, transfer RNA, 転位RNA
[★]
トランスファーRNA transfer RNAs