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Information on EC 6.1.1.2 - tryptophan-tRNA ligase and Organism(s) Mus musculus and UniProt Accession P32921
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6.1.1.2 tryptophan-tRNA ligaseSpecify your search results
Word Map
- 6.1.1.2
- synthetases
- aminoacyl-trna
- aminoacylation
- pancreas
- beef
-
anticodon
- stearothermophilus
- tyrrs
- tyrosyl-trna
- indoleamine
-
angiostatic
-
kmsks
-
ido
- tryptamine
-
tryptophan-dependent
-
aarss
- ap4a
- glutaminyl-trna
- hisrs
-
anticodon-binding
- glnrs
- medicine
- synthesis
- biotechnology
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
tryptophanyl-trna synthetase, trprs, wars2, mini-trprs, t2-trprs, tryptophanyl trna synthetase, htrprs, trprs1, trprs ii, trp-rs, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(Mt)TrpRS
-
-
-
-
hWRS
-
-
-
-
IFP53
-
-
-
-
Synthetase, tryptophanyl-transfer ribonucleate
-
-
-
-
TrpRS
Tryptophan translase
-
-
-
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Tryptophan--tRNA ligase
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-
-
-
Tryptophanyl ribonucleic synthetase
-
-
-
-
Tryptophanyl-transfer ribonucleate synthetase
-
-
-
-
Tryptophanyl-transfer ribonucleic acid synthetase
-
-
-
-
Tryptophanyl-transfer ribonucleic synthetase
-
-
-
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Tryptophanyl-transfer RNA synthetase
-
-
-
-
Tryptophanyl-tRNA synthase
-
-
-
-
Tryptophanyl-tRNA synthetase
TrpRS
-
-
-
-
Tryptophanyl-tRNA synthetase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
esterification
-
-
-
-
Aminoacylation
Aminoacylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-tryptophan:tRNATrp ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY
9023-44-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
-
-
?
additional information
?
-
-
tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in mouse models, the dietary supplementation with tryptophan as a tryptamine competitor may not counteract the deleterious influence of tryptamine, overview
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
-
-
?
additional information
?
-
-
tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in mouse models, the dietary supplementation with tryptophan as a tryptamine competitor may not counteract the deleterious influence of tryptamine, overview
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tryptamine
-
a metabolic tryptophan analog that acts as a potent competitive inhibitor of TrpRS, overview
additional information
the full-length-WRS-induced TNF-alpha and MIP-1alpha production is significantly inhibited when TLR4, MD2, and TLR2 (to lesser degree) are suppressed
-
additional information
-
the full-length-WRS-induced TNF-alpha and MIP-1alpha production is significantly inhibited when TLR4, MD2, and TLR2 (to lesser degree) are suppressed
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in mouse models, overview
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
the full-length-WRS-induced TNF-alpha and MIP-1alpha production is significantly inhibited when TLR4, MD2, and TLR2 (to lesser degree) are suppressed, full-length-WRS-induced neutrophil infiltration is almost ablated in the TLR4-/- and MD2-/- mice, and partially reduced in TLR2-/- mice. Although truncated WRS mutant lacking N47 can bring the two TLR4-MD2 complexes into proximity through homodimerization of the WRS catalytic domain, it may not be able to induce the functional dimerization of TLR4-MD2 to activate downstream signalling
physiological function
the secreted tryptophanyl-tRNA synthetase is a primary defence system against infection, it functions as an intrinsic defensive factor against infection. Administration of full-length murine WRS into Salmonella typhimurium-infected mice reduces the levels of bacteria and improves mouse survival, whereas its titration with the specific antibody aggravates the infection. Full-length WRS protects mice from typhimurium infection-induced lethality. The enzyme is secreted in N-terminal truncated form or in full-length form, the full-length wild-type enzyme, but not the short form, is rapidly secreted upon pathogen infection to prime innate immunity. Proposed working mechanism of full-length-WRS for TLR4-MD2 activation, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SYWC_MOUSE
481
0
54358
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
TrpRS N-terminal peptide self-assembles in double-helical fibrils in vitro
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kisselev, L.L.
Mammalian tryptophanyl-tRNA synthetases
Biochimie
75
1027-1039
1993
Bos taurus, Oryctolagus cuniculus, Ovis aries, Homo sapiens, Mammalia, Mus musculus, Primates, Rattus norvegicus, Rodentia, Ruminantia
Paley, E.L.; Denisova, G.; Sokolova, O.; Posternak, N.; Wang, X.; Brownell, A.L.
Tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in human cell and mouse models
Neuromolecular Med.
9
55-82
2007
Homo sapiens, Mus musculus, Mus musculus BALB/c
Wakasugi, K.
Species-specific differences in the regulation of the aminoacylation activity of mammalian tryptophanyl-tRNA synthetases
FEBS Lett.
584
229-232
2010
Bos taurus, Mus musculus, Homo sapiens (P23381), Homo sapiens
Miyanokoshi, M.; Tanaka, T.; Tamai, M.; Tagawa, Y.; Wakasugi, K.
Expression of the rodent-specific alternative splice variant of tryptophanyl-tRNA synthetase in murine tissues and cells
Sci. Rep.
3
3477
2013
Mus musculus (P32921), Mus musculus
Ahn, Y.H.; Park, S.; Choi, J.J.; Park, B.K.; Rhee, K.H.; Kang, E.; Ahn, S.; Lee, C.H.; Lee, J.S.; Inn, K.S.; Cho, M.L.; Park, S.H.; Park, K.; Park, H.J.; Lee, J.H.; Park, J.W.; Kwon, N.H.; Shim, H.; Han, B.W.; Kim, P.; Lee, J.Y.; Jeon, Y.; Huh, J.W.; Jin, M.; Kim, S.
Secreted tryptophanyl-tRNA synthetase as a primary defence system against infection
Nat. Microbiol.
2
16191
2016
Homo sapiens (P23381), Homo sapiens, Mus musculus (P32921), Mus musculus, Mus musculus C57BL/6 (P32921)
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