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Information on EC 6.1.1.11 - serine-tRNA ligase and Organism(s) Bos taurus and UniProt Accession Q9N0F3
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6.1.1.11 serine-tRNA ligaseIUBMB Comments
This enzyme also recognizes tRNASec, the special tRNA for selenocysteine, and catalyses the formation of L-seryl-tRNASec, the substrate for EC 2.9.1.1, L-seryl-tRNASec selenium transferase.
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Word Map
- 6.1.1.11
-
raman
-
surface-enhanced
- nanoparticles
- silver
- aminoacyl-trna
- aminoacylation
-
serylation
-
colloid
- selenocysteine
-
anticodon
- trnasec
- asprs
-
isoacceptors
-
aarss
- lysyl-trna
-
roughened
- phenylalanyl-trna
- trnatyr
-
langmuir-blodgett
- alanyl-trna
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handheld
- albomycins
-
citrate-reduced
- molecular biology
-
nanostars
- selenophosphate
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
serrs, seryl-trna synthetase, seryl trna synthetase, mtserrs, serrs2, seryl-trna-synthetase, mmbserrs, serzmo, serrs1, methanogenic serrs, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
62 kDa RNA-binding protein
-
-
-
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Serine transfer RNA synthetase
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-
-
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Serine translase
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-
-
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Serine--tRNA ligase
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-
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SerRS
SerRSmt
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-
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SERSEC
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-
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Seryl-transfer ribonucleate synthetase
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-
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Seryl-transfer ribonucleic acid synthetase
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Seryl-transfer RNA synthetase
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Seryl-tRNA synthetase
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-
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Synthetase, seryl-transfer ribonucleate
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-
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SerRS
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer
the tRNA recognition mechanism of mammalian mitochondrial enzymediffers considerably from that of its prokaryotic counterpart
ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer
tRNA recoginition mechanism, dual recognition mode for isoacceptors, the mitochondrial isozyme specifically recognizes the TPiC loop sequence in each isoacceptor
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
esterification
Aminoacylation
esterification
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-
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Aminoacylation
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
L-serine:tRNASer ligase (AMP-forming)
This enzyme also recognizes tRNASec, the special tRNA for selenocysteine, and catalyses the formation of L-seryl-tRNASec, the substrate for EC 2.9.1.1, L-seryl-tRNASec selenium transferase.
CAS REGISTRY NUMBER
COMMENTARY
9023-48-7
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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-serine + tRNASerGCU
AMP + diphosphate + L-seryl-tRNASerGCU
GCU for codon AGY, unusual tRNASer substrate, the mitochondrial isozyme aminoacylates both mitochondrial tRNASer types, the first corresponding to the codon AGY lacking the entire D arm
-
?
ATP + L-serine + tRNASerGCU
AMP + diphosphate + L-seryl-tRNASerGCU
GCU for codon AGY, unusual tRNASer substrate, the mitochondrial isozyme aminoacylates both mitochondrial tRNASer types, the first corresponding to the codon AGY lacking the entire D arm
-
?
ATP + L-serine + tRNASerUGA
AMP + diphosphate + L-seryl-tRNASerUGA
UGA for codon UCN, unusual tRNASer substrate, the mitochondrial isozyme aminoacylates both mitochondrial tRNASer types, the second corresponding to the codon UCN with a different cloverleaf structure
-
?
ATP + L-serine + tRNASerUGA
AMP + diphosphate + L-seryl-tRNASerUGA
UGA for codon UCN, unusual tRNASer substrate, the mitochondrial isozyme aminoacylates both mitochondrial tRNASer types, the second corresponding to the codon UCN with a different cloverleaf structure
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?
additional information
?
-
substrate specificity with diverse mutant variants of tRNASerUGA and tRNASerGCU with the recombinant mitochondrial isozyme, overview
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?
additional information
?
-
-
substrate specificity with diverse mutant variants of tRNASerUGA and tRNASerGCU with the recombinant mitochondrial isozyme, overview
-
?
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics with diverse mutant variants of tRNASerUGA and tRNASerGCU with the recombinant mitochondrial isozyme, overview
-
additional information
additional information
-
kinetics with diverse mutant variants of tRNASerUGA and tRNASerGCU with the recombinant mitochondrial isozyme, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kcat for diverse mutant variants of tRNASerUGA and tRNASerGCU with the recombinant mitochondrial isozyme, overview
-
additional information
additional information
-
kcat for diverse mutant variants of tRNASerUGA and tRNASerGCU with the recombinant mitochondrial isozyme, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH 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
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). SYSM_BOVIN
518
0
58296
Swiss-Prot
Mitochondrion (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of mtRS in complex with seryl adenylate at 1.65 A resolution, space group P222(1) with unit cell parameters a = 79.9, b = 230 A, c = 135.6 A
recombinant enzyme, hanging drop vapor-diffusion method. Crystals diffract well beyond a resolution of 1.16 A and belong to the orthorhombic space group C222(1), with unit cell parameters a = 79.89, b = 230.42, c = 13560. There is one dimer in the asymmetric unit, with a solvent content of 55%
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sitting-drop vapour-diffusion method. Crystals grew in a very narrow range of conditions using PEG 8000 as precipitant at room temperature. An appropriate concentration of lithium sulfate was critical for crystal nucleation. Crystals diffracted well beyond a resolution of 1.6 A and were found to belong to the orthorhombic space group C222(1), with unit-cell parameters a = 79.89 A, b = 230.42 A, c = 135.60 A. There is one dimer in the asymmetric unit, with a solvent content of 55%
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Webster jr., L.T.; Davie, E.W.
Purification and properties of serine-activating enzyme from beef pancreas
J. Biol. Chem.
236
479-484
1961
Bos taurus
Walker, E.J.; Treacy, G.B.; Jeffrey, P.D.
Molecular weights of mitochondrial and cytoplasmic aminoacyl-tRNA synthetases of beef liver and their complexes
Biochemistry
22
1934-1941
1983
Bos taurus
Mizutani, T.; Narihara, T.; Hashimoto, A.
Purification and properties of bovine liver seryl-tRNA synthetase
Eur. J. Biochem.
143
9-13
1984
Bos taurus
Tachibana, Y.; Kanbe, K.; Mizutani, T.
A study of the interaction between tRNASer and seryl-tRNA synthetase from bovine liver
Nucleic Acids Symp. Ser.
16
217-220
1985
Bos taurus
Yokogawa, T.; Shimada, N.; Takeuchi, N.; Benkowski, L.; Suzuki, T.; Omori, A.; Ueda, T.; Nishikawa, K.; Spremulli, L.L.; Watanabe, K.
Characterization and tRNA recognition of mammalian mitochondrial seryl-tRNA synthetase
J. Biol. Chem.
275
19913-19920
2000
Mus musculus (Q9JJL8), Mus musculus, Bos taurus (Q9N0F3), Bos taurus, Homo sapiens (Q9NP81), Homo sapiens
Shimada, N.; Suzuki, T.; Watanabe, K.
Dual mode recognition of two isoacceptor tRNAs by mammalian mitochondrial seryl-tRNA synthetase
J. Biol. Chem.
276
46770-46778
2001
Bos taurus (Q9N0F3), Bos taurus
Chimnaronk, S.; Jeppesen, M.G.; Shimada, N.; Suzuki, T.; Nyborg, J.; Watanabe, K.
Crystallization and preliminary X-ray diffraction study of mammalian mitochondrial seryl-tRNA synthetase
Acta Crystallogr. Sect. D
40
1319-1322
2004
Bos taurus
-
Chimnaronk, S.; Jeppesen, M.G.; Shimada, N.; Suzuki, T.; Nyborg, J.; Watanabe, K.
Crystallization and preliminary X-ray diffraction study of mammalian mitochondrial seryl-tRNA synthetase
Acta Crystallogr. Sect. D
60
1319-1322
2004
Bos taurus
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