ヒスチジンtRNAリガーゼ
- 関
- histidyl-tRNA synthetase
WordNet
- an essential amino acid found in proteins that is important for the growth and repair of tissue
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/11/22 10:37:26」(JST)
[Wiki en表示]
| histidine-tRNA ligase |
| Identifiers |
| EC number |
6.1.1.21 |
| CAS number |
9068-78-4 |
| 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, a histidine-tRNA ligase (EC 6.1.1.21) is an enzyme that catalyzes the chemical reaction
- ATP + L-histidine + tRNAHis AMP + diphosphate + L-histidyl-tRNAHis
The 3 substrates of this enzyme are ATP, L-histidine, and tRNA(His), whereas its 3 products are AMP, diphosphate, and L-histidyl-tRNA(His).
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-histidine:tRNAHis ligase (AMP-forming). Other names in common use include histidyl-tRNA synthetase, histidyl-transfer ribonucleate synthetase, and histidine translase. This enzyme participates in histidine metabolism and aminoacyl-trna biosynthesis.
Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1ADJ, 1ADY, 1H4V, 1HTT, 1KMM, 1KMN, 1QE0, 1WU7, and 1X59.
See also
References
- von Tigerstrom M, Tener GM (1967). "Histidyl transfer ribonucleic acid synthetase from bakers' yeast". Can. J. Biochem. 45 (7): 1067–74. doi:10.1139/o67-123. PMID 6035970.
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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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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
- A novel papillation assay for the identification of genes affecting mutation rate in Pseudomonas putida and other pseudomonads.
- Tagel M1, Tavita K1, Hõrak R1, Kivisaar M1, Ilves H2.
- Mutation research.Mutat Res.2016 Aug;790:41-55. doi: 10.1016/j.mrfmmm.2016.06.002. Epub 2016 Jul 6.
- Formation of microcolonies (papillae) permits easy visual screening of mutational events occurring in single colonies of bacteria. In this study, we have established a novel papillation assay employable in a wide range of pseudomonads including Pseudomonas aeruginosa and Pseudomonas putida for monit
- PMID 27447898
- Identification of DNA-binding proteins that interact with the 5'-flanking region of the human D-amino acid oxidase gene by pull-down assay coupled with two-dimensional gel electrophoresis and mass spectrometry.
- Tran DH1, Shishido Y2, Chung SP1, Trinh HT1, Yorita K1, Sakai T1, Fukui K3.
- Journal of pharmaceutical and biomedical analysis.J Pharm Biomed Anal.2015 Dec 10;116:94-100. doi: 10.1016/j.jpba.2015.02.031. Epub 2015 Feb 23.
- D-Amino acid oxidase (DAO) is a flavoenzyme that metabolizes D-amino acids and is expected to be a promising therapeutic target of schizophrenia and glioblastoma. The study of DNA-binding proteins has yielded much information in the regulation of transcription and other biological processes. However
- PMID 25749303
- Closely-related taxa influence woody species discrimination via DNA barcoding: evidence from global forest dynamics plots.
- Pei N1,2, Erickson DL3, Chen B1,2, Ge X4, Mi X5, Swenson NG6, Zhang JL7, Jones FA8, Huang CL9, Ye W4, Hao Z10, Hsieh CF11, Lum S12, Bourg NA13, Parker JD14, Zimmerman JK15, McShea WJ13, Lopez IC3, Sun IF16, Davies SJ17, Ma K5, Kress WJ3.
- Scientific reports.Sci Rep.2015 Oct 12;5:15127. doi: 10.1038/srep15127.
- To determine how well DNA barcodes from the chloroplast region perform in forest dynamics plots (FDPs) from global CTFS-ForestGEO network, we analyzed DNA barcoding sequences of 1277 plant species from a wide phylogenetic range (3 FDPs in tropics, 5 in subtropics and 5 in temperate zone) and compare
- PMID 26456472
Related Links
- ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His). GO - Molecular function i ATP binding Source: UniProtKB-HAMAP histidine-tRNA ligase activity Source: UniProtKB-HAMAP ...
- cytoplasm, histidine-tRNA ligase activity, histidyl-tRNA aminoacylation UniProtKB x UniProtKB Protein knowledgebase Proteomes Protein sets from fully sequenced genomes UniRef Sequence clusters Supporting data ...
★リンクテーブル★
[★]
ヒスチジルtRNA合成酵素、ヒスチジルtRNAシンテターゼ
- 関
- histidine-tRNA ligase
[★]
- 英
- histidine-tRNA ligase
- 関
- ヒスチジル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