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Literature summary for 6.1.1.2 extracted from
- Identification of a residue crucial for the angiostatic activity of human mini tryptophanyl-tRNA synthetase by focusing on its molecular evolution (2016), Sci. Rep., 6, 24750 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of wild-type and mutant enzymes in Escherichia coli | Homo sapiens |
| recombinant expression of wild-type and mutant enzymes in Escherichia coli | Danio rerio |
| recombinant expression of wild-type and mutant enzymes in Escherichia coli | Bos taurus |
| recombinant expression of wild-type enzyme in Escherichia coli | Arabidopsis thaliana |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E451Q | site-directed mutagenesis, binds to VE-cadherin like the wild-type, full-length enzyme | Homo sapiens |
| H445E | site-directed mutagenesis, the zebrafish mini mutant TrpRS interacts with VE-cadherin significantly as does human mini wild-type TrpRS, while the zebrafish wild-type enzyme does not | Danio rerio |
| K114Q | site-directed mutagenesis, binds to VE-cadherin like the wild-type, full-length enzyme | Homo sapiens |
| K153Q | site-directed mutagenesis, the human mini K153Q TrpRS mutant cannot inhibit VEGF-stimulated HUVEC migration and cannot bind to the extracellular domain of VE-cadherin | Homo sapiens |
| K418Q | site-directed mutagenesis, binds to VE-cadherin like the wild-type, full-length enzyme | Homo sapiens |
| additional information | bovine mini TrpRS lacks the first 52 amino acids | Bos taurus |
| additional information | full-legnth Arabidopsis thaliana TrpRS lacks the N-terminal domain compared to enzymes from mammls and Danio rerio | Arabidopsis thaliana |
| additional information | human mini TrpRS lacks the first 47 amino acids | Homo sapiens |
| additional information | zebrafish mini TrpRS lacks the first 42 amino acids | Danio rerio |
| Q107K | site-directed mutagenesis, the zebrafish mini mutant TrpRS interacts with VE-cadherin significantly as does human mini wild-type TrpRS, while the zebrafish wild-type enzyme does not | Danio rerio |
| Q146K | site-directed mutagenesis, the zebrafish mini mutant TrpRS interacts with VE-cadherin significantly as does human mini wild-type TrpRS, while the zebrafish wild-type enzyme does not | Danio rerio |
| Q411K | site-directed mutagenesis, the zebrafish mini mutant TrpRS interacts with VE-cadherin significantly as does human mini wild-type TrpRS, while the zebrafish wild-type enzyme does not | Danio rerio |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytoplasm | - |
Homo sapiens | 5737 | - |
| cytoplasm | - |
Bos taurus | 5737 | - |
| cytoplasm | - |
Arabidopsis thaliana | 5737 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Homo sapiens |  |
| Mg2+ | required | Danio rerio | |
| Mg2+ | required | Bos taurus | |
| Mg2+ | required | Arabidopsis thaliana | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-tryptophan + tRNATrp | Homo sapiens | - |
AMP + diphosphate + L-tryptophyl-tRNATrp | - |
? | |
| ATP + L-tryptophan + tRNATrp | Danio rerio | - |
AMP + diphosphate + L-tryptophyl-tRNATrp | - |
? | |
| ATP + L-tryptophan + tRNATrp | Bos taurus | - |
AMP + diphosphate + L-tryptophyl-tRNATrp | - |
? | |
| ATP + L-tryptophan + tRNATrp | Arabidopsis thaliana | - |
AMP + diphosphate + L-tryptophyl-tRNATrp | - |
? | |
| additional information | Homo sapiens | binding of vascular endothelial (VE)-cadherin, the NH2-terminal Trp2 and Trp4 residues of VE-cadherin are docked into the Trp- and adenosine-binding pockets of human TrpRS | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | Q9SR15 | - |
- |
| Bos taurus | P17248 | - |
- |
| Danio rerio | Q6PBS3 | - |
- |
| Homo sapiens | P23381 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type and mutant enzymes from Escherichia coli | Homo sapiens |
| recombinant wild-type and mutant enzymes from Escherichia coli | Danio rerio |
| recombinant wild-type and mutant enzymes from Escherichia coli | Bos taurus |
| recombinant wild-type enzyme from Escherichia coli | Arabidopsis thaliana |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-tryptophan + tRNATrp | - |
Homo sapiens | AMP + diphosphate + L-tryptophyl-tRNATrp | - |
? | |
| ATP + L-tryptophan + tRNATrp | - |
Danio rerio | AMP + diphosphate + L-tryptophyl-tRNATrp | - |
? | |
| ATP + L-tryptophan + tRNATrp | - |
Bos taurus | AMP + diphosphate + L-tryptophyl-tRNATrp | - |
? | |
| ATP + L-tryptophan + tRNATrp | - |
Arabidopsis thaliana | AMP + diphosphate + L-tryptophyl-tRNATrp | - |
? | |
| additional information | binding of vascular endothelial (VE)-cadherin, the NH2-terminal Trp2 and Trp4 residues of VE-cadherin are docked into the Trp- and adenosine-binding pockets of human TrpRS | Homo sapiens | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| TrpRS | - |
Homo sapiens |
| TrpRS | - |
Danio rerio |
| TrpRS | - |
Bos taurus |
| TrpRS | - |
Arabidopsis thaliana |
| Tryptophanyl-tRNA synthetase | - |
Homo sapiens |
| Tryptophanyl-tRNA synthetase | - |
Danio rerio |
| Tryptophanyl-tRNA synthetase | - |
Bos taurus |
| Tryptophanyl-tRNA synthetase | - |
Arabidopsis thaliana |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
in vivo assay at | Homo sapiens |
| 37 | - |
in vivo assay at | Danio rerio |
| 37 | - |
in vivo assay at | Bos taurus |
| 37 | - |
in vivo assay at | Arabidopsis thaliana |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
aminoacylation assay at | Homo sapiens |
| 7.5 | - |
aminoacylation assay at | Danio rerio |
| 7.5 | - |
aminoacylation assay at | Bos taurus |
| 7.5 | - |
aminoacylation assay at | Arabidopsis thaliana |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Homo sapiens | |
| ATP | - |
Danio rerio | |
| ATP | - |
Bos taurus | |
| ATP | - |
Arabidopsis thaliana | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | a human mini K153Q TrpRS mutant cannot inhibit VEGF-stimulated HUVEC migration and cannot bind to the extracellular domain of VE-cadherin | Homo sapiens |
| additional information | tryptophanyl-tRNA synthetase (TrpRS) exists in two forms: a full-length TrpRS and a mini TrpRS. Both human and bovine mini TrpRSs inhibit VEGF-induced endothelial migration, whereas zebrafish mini TrpRS and Arabidopsis thaliana wild-type TrpRS do not. The bovine full-length TrpRS and zebrafish full-length TrpRS have no effect on VEGF-stimulated HUVEC chemotaxis | Homo sapiens |
| additional information | tryptophanyl-tRNA synthetase (TrpRS) exists in two forms: a full-length TrpRS and a mini TrpRS. Both human and bovine mini TrpRSs inhibit VEGF-induced endothelial migration, whereas zebrafish mini TrpRS and Arabidopsis thaliana wild-type TrpRS do not. The bovine full-length TrpRS has no effect on VEGF-stimulated HUVEC chemotaxis | Bos taurus |
| additional information | tryptophanyl-tRNA synthetase (TrpRS) exists in two forms: a full-length TrpRS and a mini TrpRS. Both human and bovine mini TrpRSs inhibit VEGF-induced endothelial migration, whereas zebrafish mini TrpRS and Arabidopsis thaliana wild-type TrpRS do not. The zebrafish full-length TrpRS has no effect on VEGF-stimulated HUVEC chemotaxis | Danio rerio |
| physiological function | aminoacyl-tRNA synthetases catalyze the first step of protein synthesis, which comprises the aminoacylation of their cognate tRNAs. Noncanonical functions distinct from aminoacylation are reported | Danio rerio |
| physiological function | aminoacyl-tRNA synthetases catalyze the first step of protein synthesis, which comprises the aminoacylation of their cognate tRNAs. Noncanonical functions distinct from aminoacylation are reported | Bos taurus |
| physiological function | aminoacyl-tRNA synthetases catalyze the first step of protein synthesis, which comprises the aminoacylation of their cognate tRNAs. Noncanonical functions distinct from aminoacylation are reported, such as the cell-signaling functions of human tryptophanyl-tRNA synthetase (TrpRS) and tyrosyl-tRNA synthetase (TyrRS) in pathways connected to the immune system or angiogenesis. Human mini, but not full-length, TrpRS is an angiostatic factor. The interaction between mini TrpRS and the extracellular domain of vascular endothelial (VE) cadherin is crucial for its angiostatic activity. The Lys153 residue of human mini TrpRS is a VE-cadherin binding site and is therefore crucial for its angiostatic activity, molecular mechanism of the angiostatic activity of human mini TrpRS, overview. VE-cadherin belongs to the cadherin superfamily of cell-cell adhesion molecules and plays a key role in vascular endothelial growth factor (VEGF)-mediated endothelial survival, endothelial barrier function, and angiogenesis | Homo sapiens |
| physiological function | aminoacyl-tRNA synthetases catalyze the first step of protein synthesis, which comprises the aminoacylation of their cognate tRNAs. Noncanonical functions distinct from aminoacylation are reported. Arabidopsis thaliana TrpRS does inhibit VEGF-induced endothelial migration | Arabidopsis thaliana |
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