Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Nakamoto, T.; Miyanokoshi, M.; Tanaka, T.; Wakasugi, K.
    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 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.2 recombinant expression of wild-type and mutant enzymes in Escherichia coli Homo sapiens
6.1.1.2 recombinant expression of wild-type and mutant enzymes in Escherichia coli Danio rerio
6.1.1.2 recombinant expression of wild-type and mutant enzymes in Escherichia coli Bos taurus
6.1.1.2 recombinant expression of wild-type enzyme in Escherichia coli Arabidopsis thaliana

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.2 E451Q site-directed mutagenesis, binds to VE-cadherin like the wild-type, full-length enzyme Homo sapiens
6.1.1.2 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
6.1.1.2 K114Q site-directed mutagenesis, binds to VE-cadherin like the wild-type, full-length enzyme Homo sapiens
6.1.1.2 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
6.1.1.2 K418Q site-directed mutagenesis, binds to VE-cadherin like the wild-type, full-length enzyme Homo sapiens
6.1.1.2 additional information bovine mini TrpRS lacks the first 52 amino acids Bos taurus
6.1.1.2 additional information full-legnth Arabidopsis thaliana TrpRS lacks the N-terminal domain compared to enzymes from mammls and Danio rerio Arabidopsis thaliana
6.1.1.2 additional information human mini TrpRS lacks the first 47 amino acids Homo sapiens
6.1.1.2 additional information zebrafish mini TrpRS lacks the first 42 amino acids Danio rerio
6.1.1.2 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
6.1.1.2 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
6.1.1.2 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

EC Number Localization Comment Organism GeneOntology No. Textmining
6.1.1.2 cytoplasm
-
 Homo sapiens 5737
-
6.1.1.2 cytoplasm
-
 Bos taurus 5737
-
6.1.1.2 cytoplasm
-
 Arabidopsis thaliana 5737
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.2 Mg2+ required Homo sapiens
6.1.1.2 Mg2+ required Danio rerio
6.1.1.2 Mg2+ required Bos taurus
6.1.1.2 Mg2+ required Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.2 ATP + L-tryptophan + tRNATrp Homo sapiens
-
 AMP + diphosphate + L-tryptophyl-tRNATrp
-
 ?
6.1.1.2 ATP + L-tryptophan + tRNATrp Danio rerio
-
 AMP + diphosphate + L-tryptophyl-tRNATrp
-
 ?
6.1.1.2 ATP + L-tryptophan + tRNATrp Bos taurus
-
 AMP + diphosphate + L-tryptophyl-tRNATrp
-
 ?
6.1.1.2 ATP + L-tryptophan + tRNATrp Arabidopsis thaliana
-
 AMP + diphosphate + L-tryptophyl-tRNATrp
-
 ?
6.1.1.2 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

EC Number Organism UniProt Comment Textmining
6.1.1.2 Arabidopsis thaliana Q9SR15
-
-
6.1.1.2 Bos taurus P17248
-
-
6.1.1.2 Danio rerio Q6PBS3
-
-
6.1.1.2 Homo sapiens P23381
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.2 recombinant wild-type and mutant enzymes from Escherichia coli Homo sapiens
6.1.1.2 recombinant wild-type and mutant enzymes from Escherichia coli Danio rerio
6.1.1.2 recombinant wild-type and mutant enzymes from Escherichia coli Bos taurus
6.1.1.2 recombinant wild-type enzyme from Escherichia coli Arabidopsis thaliana

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.2 ATP + L-tryptophan + tRNATrp
-
 Homo sapiens AMP + diphosphate + L-tryptophyl-tRNATrp
-
 ?
6.1.1.2 ATP + L-tryptophan + tRNATrp
-
 Danio rerio AMP + diphosphate + L-tryptophyl-tRNATrp
-
 ?
6.1.1.2 ATP + L-tryptophan + tRNATrp
-
 Bos taurus AMP + diphosphate + L-tryptophyl-tRNATrp
-
 ?
6.1.1.2 ATP + L-tryptophan + tRNATrp
-
 Arabidopsis thaliana AMP + diphosphate + L-tryptophyl-tRNATrp
-
 ?
6.1.1.2 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

EC Number Synonyms Comment Organism
6.1.1.2 TrpRS
-
 Homo sapiens
6.1.1.2 TrpRS
-
 Danio rerio
6.1.1.2 TrpRS
-
 Bos taurus
6.1.1.2 TrpRS
-
 Arabidopsis thaliana
6.1.1.2 Tryptophanyl-tRNA synthetase
-
 Homo sapiens
6.1.1.2 Tryptophanyl-tRNA synthetase
-
 Danio rerio
6.1.1.2 Tryptophanyl-tRNA synthetase
-
 Bos taurus
6.1.1.2 Tryptophanyl-tRNA synthetase
-
 Arabidopsis thaliana

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.2 37
-
 in vivo assay at Homo sapiens
6.1.1.2 37
-
 in vivo assay at Danio rerio
6.1.1.2 37
-
 in vivo assay at Bos taurus
6.1.1.2 37
-
 in vivo assay at Arabidopsis thaliana

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.2 7.5
-
 aminoacylation assay at Homo sapiens
6.1.1.2 7.5
-
 aminoacylation assay at Danio rerio
6.1.1.2 7.5
-
 aminoacylation assay at Bos taurus
6.1.1.2 7.5
-
 aminoacylation assay at Arabidopsis thaliana

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.2 ATP
-
 Homo sapiens
6.1.1.2 ATP
-
 Danio rerio
6.1.1.2 ATP
-
 Bos taurus
6.1.1.2 ATP
-
 Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
6.1.1.2 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
6.1.1.2 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
6.1.1.2 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
6.1.1.2 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
6.1.1.2 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
6.1.1.2 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
6.1.1.2 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
6.1.1.2 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