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2'-dATP + L-serine + tRNASer
2'-dAMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
2-bromoadenosine 5'-triphosphate + L-serine + tRNASer
2-bromoadenosine 5'-monophosphate + diphosphate + L-seryl-tRNASer
-
-
-
?
2-chloroadenosine 5'-triphosphate + L-serine + tRNASer
2-chloroadenosine 5'-monophosphate + diphosphate + L-seryl-tRNASer
-
-
-
?
3'-NH2-ATP + L-serine + tRNASer
3'-NH2-AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
AMP + diphosphate + L-seryl-tRNASer
ATP + L-serine + tRNASer
-
-
-
-
r
ATP + DL-serine hydroxamate + tRNASer
?
-
very weak activity
-
-
?
ATP + L-cysteine + tRNASer
AMP + diphosphate + L-cysteinyl-tRNASer
-
very weak activity
-
-
?
ATP + L-serine + Fusaro tRNAPyl
AMP + diphosphate + L-seryl-Fusaro tRNAPyl
-
Methanosarcina barkeri Fusaro tRNApyrrolysine (tRNAPyl) can be misacylated with serine by the Methanosarcina barkeri bacterial-type seryl-tRNA synthetase in vitro and in vivo in Escherichia coli. Compared to the Methanosarcina barkeri Fusaro tRNA, the Methanosarcina barkeri MS tRNAPyl contains two base changes: a G3:U70 pair
-
-
?
ATP + L-serine + tRNAPyl
AMP + diphosphate + L-seryl-tRNAPyl
-
-
-
-
?
ATP + L-serine + tRNASec
AMP + diphosphate + L-seryl-tRNASec
ATP + L-serine + tRNASec mutant without anticodon arm
?
-
-
-
-
?
ATP + L-serine + tRNASecUCA
AMP + diphosphate + L-seryl-tRNASecUCA
-
SerRS also aminoacylates tRNASec with serine as the first step for the incorporation of selenocysteine into proteins
-
-
?
ATP + L-serine + tRNASer
?
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
ATP + L-serine + tRNASer (Escherichia coli)
AMP + diphosphate + L-seryl-tRNASer (Escherichia coli)
-
-
-
-
?
ATP + L-serine + tRNASer (Saccharomyces cerevisiae)
AMP + diphosphate + L-seryl-tRNASer (Saccharomyces cerevisiae)
-
-
-
-
?
ATP + L-serine + tRNASer mutant without anticodon arm
?
-
-
-
-
?
ATP + L-serine + tRNASer(CGA)
AMP + diphosphate + L-seryl-tRNASer(CGA)
-
-
-
-
?
ATP + L-serine + tRNASer(GCU)
AMP + diphosphate + L-seryl-tRNASer(GCU)
-
-
-
-
?
ATP + L-serine + tRNASer(GGA)
AMP + diphosphate + L-seryl-tRNASer(GGA)
-
-
-
-
?
ATP + L-serine + tRNASer-C-C-2'dA
AMP + diphosphate + L-seryl-tRNASer-C-C-2'dA
-
-
-
-
?
ATP + L-serine + tRNASer-C-C-A
AMP + diphosphate + L-seryl-tRNASer-C-C-A
-
-
-
-
?
ATP + L-serine + tRNASer-C-C-F
AMP + diphosphate + L-seryl-tRNASer-C-C-F
-
-
-
-
?
ATP + L-serine + tRNASer-CmCA
AMP + diphosphate + L-seryl-tRNASer-CmCA
-
-
-
-
?
ATP + L-serine + tRNASer-I-G-A
AMP + diphosphate + L-seryl-tRNASer-I-G-A
-
-
-
-
?
ATP + L-serine + tRNASerCGA
AMP + diphosphate + L-seryl-tRNASerCGA
-
-
-
-
?
ATP + L-serine + tRNASerGCU
AMP + diphosphate + L-seryl-tRNASerGCU
ATP + L-serine + tRNASerUGA
AMP + diphosphate + L-seryl-tRNASerUGA
ATP + L-threonine + tRNASer
AMP + diphosphate + L-threonyl-tRNASer
-
very weak activity
-
-
?
dATP + L-serine + tRNASer
dAMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
formycin 5'-triphosphate + L-serine + tRNASer
formycin 5'-monophosphate + diphosphate + L-seryl-tRNASer
-
-
-
?
additional information
?
-
ATP + D-Ser + tRNASer
?
-
-
-
-
?
ATP + D-Ser + tRNASer
?
-
-
-
-
?
ATP + L-serine + tRNASec
AMP + diphosphate + L-seryl-tRNASec
-
selenocysteine-incorporating tRNA wild-type and deletion mutants, secondary structures
-
?
ATP + L-serine + tRNASec
AMP + diphosphate + L-seryl-tRNASec
15.8% activity compared to tRNASer
-
-
?
ATP + L-serine + tRNASec
AMP + diphosphate + L-seryl-tRNASec
-
SerRS also aminoacylates tRNASec with serine as the first step for the incorporation of selenocysteine into proteins, SerRS is essential for growth Trypanosoma brucei and is responsible for the serylation of both tRNASer and tRNASec
-
-
?
ATP + L-serine + tRNASec
AMP + diphosphate + L-seryl-tRNASec
SerRS also aminoacylates tRNASec with serine as the first step for the incorporation of selenocysteine into proteins, SerRS is responsible for the serylation of both tRNASer and tRNASec
-
-
?
ATP + L-serine + tRNASec
AMP + diphosphate + L-seryl-tRNASec
SerRS also aminoacylates tRNASec with serine as the first step for the incorporation of selenocysteine into proteins
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
D-Ser can replace L-Ser in ATP-diphosphate exchange
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
the enzyme selectively recognizes tRNASer on the basis of its characteristic tertiary structure rather than the nucleotides specific to tRNASer
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
the enzyme only recognizes cognate tRNA
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
100% activity
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
4 isoacceptors of tRNASer, and tRNASer deletion mutants, secondary structures, the anticodon arms D and T are not involved in tRNA substrate recognition by the enzyme, only in formation of the L-shaped tRNA structure
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
serylates tRNASer from methanobacteria, Escherichia coli and Saccharomyces cerevisiae
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
the seryl-tRNA synthetase recognizes eukaryotic and bacterial tRNASer, in addition to the homologous tRNASer and tRNASec
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
serylates tRNASer from methanobacteria, Escherichia coli and Saccharomyces cerevisiae
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
the seryl-tRNA synthetase recognizes eukaryotic and bacterial tRNASer, in addition to the homologous tRNASer and tRNASec
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
serylates tRNASer from methanobacteria and Escherichia coli, no activity with tRNASer from Saccharomyces cerevisiae
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
reaction with tRNASer variants. Two dissimilar seryl-transfer RNA synthases exist in Methanosarcina barkeri, one of bacterial type and the other resembling SerRS present only in some methanogenic archaea. The anticodon stem base pair G30:C40, a determinant for the specific tRNASer recognition, contributes to the efficiency of serylation in both seryl-transfer RNA synthases. The two seryl-transfer RNA synthases do not possess a uniform mode of tRNASer recognition. The methanogenic seryl-transfer RNA synthase relies on G1:C72 identity and on the number of unpaired nucleotides at the base of the variable stem for tRNASer recognition, unlike its bacterial type counterpart
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
zinc-dependent serine recognition mechanism, N-terminal tRNA-binding domain structure, serine-binding site structure, overview
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
gene silencing of the Nicotiana benthamiana SerRS causes severe leaf yellowing and abnormal leaf morphology, while maintaining almost normal plant growth. At the cell level depletion of the NcSRS gene results in dramatically reduced numbers of chloroplasts with reduced sizes and chlorophyll content. The numbers and/or physiology of mitochondria are also severely affected. The abnormal chloroplasts lack most of the thylakoid membranes and appear to be degenerating, whereas some of them show doublet morphology, indicating defective chloroplast division
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
SerRS efficiently aminoacylates not only Pyrococcus horikoshii tRNA(Ser) but also bacterial tRNA(Ser)s from Thermus thermophilus and Escherichia coli
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
tRNASer-C-C-A, tRNASer-C-C-F, tRNASer-C-C-2'dA, and tRNASerC-C-Aoxi-red can act as substrate
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
enzyme aminoacylates E. coli tRNA with Ser much more poorly than its homologous tRNAs
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
epsilon-ATP functions in place of ATP in seryl-tRNA formation. Modified tRNASer, in which the 3'-terminal adenosine is replaced by ethenoadenosine can be used in place of unmodified tRNAs
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
amino acids within motif 2 loop are involved in specific binding of L-serine and ATP to the enzyme
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
wild-type and mutant tRNASer substrates, the enzyme complexed with 1 molecule of tRNASer is more specific and more efficient in catalyzing seryl-adenylate formation than the apoenzyme alone
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
formation of a seryl adenylate intermediate, mechanism of discrimination between cognate and noncognate amino acids, quantitative computational analysis, overview
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
role of Pex21p in enhancing cognate tRNA binding by SerRS
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
recombinant enzyme, tRNASer from Escherichia coli
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
r
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
r
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
r
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
a two-step reaction, seryl-tRNA synthetase is a class II synthetase depending on rather few and simple identity elements in tRNASer to determine the amino acid specificity, tRNASer acceptor stem microhelices can be aminoacylated with serine as part of the tRNA a valuable tool for investigating the structural motifs in a tRNASer-seryl-tRNA synthetase complex, tRNASer secondary structure, overview
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
formation of a seryl adenylate intermediate, mechanism of discrimination between cognate and noncognate amino acids, quantitative computational analysis, overview
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
tttRNASer
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
tttRNASer
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
tttRNASer
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
tRNASec, unlike most trypanosomal tRNAs, is exclusively localized in the cytosol, SerRS is essential for growth Trypanosoma brucei and is responsible for the serylation of both tRNASer and tRNASec
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
responsible for the serylation of both tRNASer and tRNASec
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
enzyme utilizes tRNA substrates from Zea mays, Saccharomyces cerevisiae, and Escherichia coli, recombinant mitochondrial isozyme
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
tRNASer from Escherichia coli, only poor activity with a substrate from yeast
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
tRNASer from Escherichia coli
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
tRNASer from Escherichia coli
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
chloroplastic tRNASer from maize
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
mitochondrial tRNASer from maize
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
mitochondrial tRNASer from yeast subtype 2
-
-
?
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
-
?
additional information
?
-
-
high abundance in middle silk gland may result from an adaption of this organ for the production of the serine-rich protein, sericin
-
-
?
additional information
?
-
substrate specificity with diverse mutant variants of tRNASerUGA and tRNASerGCU with the recombinant mitochondrial isozyme, overview
-
?
additional information
?
-
-
substrate specificity with diverse mutant variants of tRNASerUGA and tRNASerGCU with the recombinant mitochondrial isozyme, overview
-
?
additional information
?
-
-
serine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
structure-function analysis, overview
-
-
?
additional information
?
-
-
L-threonine is a poor substrate, L-cysteine is no substrate for the SerRS, the methanogenic enzyme has evolved two distinct mechanisms for the recognition of the same amino-acid substrate, overview
-
-
?
additional information
?
-
-
in contrast to the bacterial-type SerRS the methanogenic SerRS shows no detectable charging of tRNApyrrolysine (tRNAPyl)
-
-
?
additional information
?
-
-
seryl-tRNA synthetase, MtSerRS, directly and stably interacts with arginyl-tRNA synthetase, MtArgRS, EC 6.1.1.19, two-hybrid system and surface plasmon resonance analysis, overview. The MtSerRS-MtArgRS complex also contains tRNAArg, consistent with the existence of a stable ribonucleoprotein complex active in aminoacylation. Deletion of the HTH motif, which contributes to the stability of SerRS dimers, significantly weakens the interaction between the two synthetases. Stimulation by MtArgRS peaks at 65°C
-
-
?
additional information
?
-
-
substrate specificity with regard to ATP analogs
-
-
?
additional information
?
-
-
serine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
serine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
about 0.4% misactivation of L-threonine by the enzyme compared to cognate L-serine, rate is decreased by binding of the tRNASer, the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
catalyzes the binding of 4-hydroxyaminoquinoline 1-oxide (a reduced metabolite of the carcinogenic and mutagenic compound 4-nitroquinoline 1-oxide) to nucleic acid. Seryl-tRNA synthetase may participate in vivo in the activation of some N-hydroxy compounds through their aminoacylation capacity
-
-
?
additional information
?
-
-
threonine will compete with serine for formation of the activated intermediate while alanineand glycine will not compete significantly, overview
-
-
?
additional information
?
-
-
enzyme contains two sets of sites for tRNASer, L-Ser and MgATP2-
-
-
?
additional information
?
-
-
binding sites for ATP interact with those for tRNA as well as with those for serine
-
-
?
additional information
?
-
-
enzyme contains two sets of sites for tRNASer, L-Ser and MgATP2-
-
-
?
additional information
?
-
-
binding sites for ATP interact with those for tRNA as well as with those for serine
-
-
?
additional information
?
-
SerRS represents the housekeeping seryl-tRNA synthetase in the organism, one role of protein VlmL in valanimycin biosynthesis is to produce seryl-tRNA, which is then utilized for a subsequent step in the biosynthetic pathway, biosynthetic pathway for the antibiotic valanimycin, overview
-
-
?
additional information
?
-
-
SerRS represents the housekeeping seryl-tRNA synthetase in the organism, one role of protein VlmL in valanimycin biosynthesis is to produce seryl-tRNA, which is then utilized for a subsequent step in the biosynthetic pathway, biosynthetic pathway for the antibiotic valanimycin, overview
-
-
?
additional information
?
-
proteins VlmL and SvsR, both involved in valanimycin biosynthesis, are able to catalyze a serine-dependent exchange of diphosphate into ATP and to aminoacylate total Escherichia coli tRNA with L-serine, SvsR is catalytically more efficient than VlmL, overview
-
-
?
additional information
?
-
-
proteins VlmL and SvsR, both involved in valanimycin biosynthesis, are able to catalyze a serine-dependent exchange of diphosphate into ATP and to aminoacylate total Escherichia coli tRNA with L-serine, SvsR is catalytically more efficient than VlmL, overview
-
-
?
additional information
?
-
threonine will compete with serine for formation of the activated intermediate while alanine and glycine will not compete significantly, overview, binding of ATP or seryl adenylate leads to the stabilization of a motif 2 loop that interacts with the tRNA acceptor stem
-
-
?
additional information
?
-
-
threonine will compete with serine for formation of the activated intermediate while alanine and glycine will not compete significantly, overview, binding of ATP or seryl adenylate leads to the stabilization of a motif 2 loop that interacts with the tRNA acceptor stem
-
-
?
additional information
?
-
the interaction of ttRNASer with the enzyme, interactions between the catalytically important loops and tRNA contribute to the change in dynamics of tRNA in free and bound states, respectively. These interactions help in the development of catalytically effective organization of the active site. The A76 end of the tttRNASer exhibits fast dynamics in free State, which is significantly reduced down within the active site bound with adenylate. The loops change their conformation via multimodal dynamics. Presence of bound Mg2+ ions around tRNA and dynamically slow bound water are other common features of the enzyme
-
-
?
additional information
?
-
-
the interaction of ttRNASer with the enzyme, interactions between the catalytically important loops and tRNA contribute to the change in dynamics of tRNA in free and bound states, respectively. These interactions help in the development of catalytically effective organization of the active site. The A76 end of the tttRNASer exhibits fast dynamics in free State, which is significantly reduced down within the active site bound with adenylate. The loops change their conformation via multimodal dynamics. Presence of bound Mg2+ ions around tRNA and dynamically slow bound water are other common features of the enzyme
-
-
?
additional information
?
-
the interaction of ttRNASer with the enzyme, interactions between the catalytically important loops and tRNA contribute to the change in dynamics of tRNA in free and bound states, respectively. These interactions help in the development of catalytically effective organization of the active site. The A76 end of the tttRNASer exhibits fast dynamics in free State, which is significantly reduced down within the active site bound with adenylate. The loops change their conformation via multimodal dynamics. Presence of bound Mg2+ ions around tRNA and dynamically slow bound water are other common features of the enzyme
-
-
?
additional information
?
-
the interaction of ttRNASer with the enzyme, interactions between the catalytically important loops and tRNA contribute to the change in dynamics of tRNA in free and bound states, respectively. These interactions help in the development of catalytically effective organization of the active site. The A76 end of the tttRNASer exhibits fast dynamics in free State, which is significantly reduced down within the active site bound with adenylate. The loops change their conformation via multimodal dynamics. Presence of bound Mg2+ ions around tRNA and dynamically slow bound water are other common features of the enzyme
-
-
?
additional information
?
-
-
no activity with tRNASer from Arabidopsis thaliana, the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
phylogenetic comparison
-
?
additional information
?
-
-
the enzyme shows pre-transfer editing activity
-
-
?
additional information
?
-
-
Gly73 is a major identity element recognized by the enzyme
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.4
2-Bromoadenosine 5'-triphosphate
-
-
0.05
2-Chloroadenosine 5'-triphosphate
-
-
2.35
DL-Serine hydroxamate
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
2
Formycin 5'-triphosphate
-
-
29
L-cysteine
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
2 - 3.4
L-threonine
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.004
tRNASec mutant without anticodon arm
-
pH 7.6, 37°C
-
0.0004
tRNASecUCA
-
pH 7.6, 37°C, recombinant enzyme
-
0.000759
tRNASer (Escherichia coli)
-
at pH 7.5 and 30°C
-
0.000937
tRNASer (Saccharomyces cerevisiae)
-
at pH 7.5 and 30°C
-
0.0011
tRNASer mutant without anticodon arm
-
pH 7.6, 37°C
-
0.0029 - 0.003
tRNASer(CGA)
-
0.0013 - 0.0053
tRNASer(GCU)
-
0.0026 - 0.0047
tRNASer(GGA)
-
0.003
tRNASer-C-C-2'dA
-
-
-
0.0009
tRNASer-C-C-A
-
-
-
0.001
tRNASer-C-C-F
-
-
-
0.00125
tRNASer-CmCA
-
-
-
0.00084 - 0.0014
tRNASer-I-G-A
-
0.0032
tRNASerCGA
-
pH 7.6, 37°C, recombinant enzyme
-
additional information
additional information
-
0.000068
ATP
-
seryl-AMP formation, wild-type enzyme
0.0013
ATP
-
ATP-diphosphate exchange assay, wild-type enzyme, pH 7.2, 30°C, in presence of tRNASer
0.004
ATP
-
ATP-diphosphate exchange
0.01 - 0.048
ATP
-
ATP-diphosphate exchange, mutant enzymes
0.011
ATP
-
wild-type enzyme, pH 7.2, 30°C
0.0143
ATP
-
aminoacylation, truncated enzyme
0.021
ATP
-
aminoacylation, wild-type enzyme
0.025
ATP
-
aminoacylation, wild-type enzyme
0.06 - 0.55
ATP
-
aminoacylation, mutant enzymes
0.08
ATP
-
mutant SerRS11, pH 7.2, 30°C
0.12
ATP
-
mutant SerRS12, pH 7.2, 30°C
0.2
D-Ser
-
2'-dATP
0.2
D-Ser
-
serine-dependent ATP-diphosphate exchange
0.0061
L-Ser
-
wild-type
0.047
L-Ser
-
wild-type, using yeast tRNA
0.051
L-Ser
-
mutant ScSerRSDELTAC13 (deletion of 13 C-terminal residues), using yeast tRNA
0.07028
L-Ser
-
mutant N435A
0.108
L-Ser
-
mutant ZmcSerRSDELTAC12 (deletion of 12 C-terminal residues), using maize tRNA
0.145
L-Ser
-
mutant ZmcSerRSDELTAC18 (deletion of 18 C-terminal residues), using maize tRNA
0.149
L-Ser
-
wild-type, using maize tRNA
0.264
L-Ser
-
mutant W396A
0.3
L-Ser
-
serine-dependent ATP-diphosphate exchange
0.573
L-Ser
-
mutant S437A
0.689
L-Ser
-
mutant N435A/S437A
2.879
L-Ser
-
mutant N435A/S437A/W396A
0.000104
L-serine
-
-
0.016
L-serine
-
wild type enzyme, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.018
L-serine
-
wild-type enzyme, pH 7.2, 30°C
0.0257
L-serine
-
mutant enzyme P395A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.04
L-serine
-
mitochondrial isozyme, aminoacylation reaction, pH 7.5, 30°C
0.049
L-serine
-
mutant enzyme Q400A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.0731
L-serine
-
mutant enzyme H250A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.14
L-serine
-
mutant SerRS12, pH 7.2, 30°C
0.18
L-serine
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.2
L-serine
-
mutant SerRS11, pH 7.2, 30°C
0.2491
L-serine
-
mutant enzyme G402A/G405A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.26
L-serine
diphosphate exchange
0.4
L-serine
diphosphate exchange
0.45
L-serine
-
mitochondrial isozyme, ATP-diphosphate exchange reaction, pH 7.5, 30°C
0.5
L-serine
-
ATP-diphosphate exchange assay, wild-type enzyme, pH 7.2, 30°C, in absence of tRNASer
0.9
L-serine
-
mutant enzyme F397P/A399G, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.00034
Ser
-
seryl-AMP formation, wild-type enzyme
0.0625
Ser
-
aminoacylation, wild-type enzyme
0.063
Ser
-
aminoacylation, wild-type enzyme
0.17 - 0.7
Ser
-
aminoacylation, mutant enzymes
0.252
Ser
-
aminoacylation, truncated enzyme
0.45
Ser
-
serine-dependent ATP-diphosphate exchange, wild-type enzyme
0.45 - 0.89
Ser
-
serine-dependent ATP-diphosphate exchange, mutant enzymes
0.0033
tRNASec
-
pH 7.6, 37°C
-
0.031
tRNASec
at pH 7.6, temperature not specified in the publication
-
0.00004
tRNASer
-
wild-type enzyme, mutant SerRS11, and mutant SerRS12, pH 7.2, 30°C
0.00005
tRNASer
-
aminoacylation, truncated enzyme
0.00011
tRNASer
-
aminoacylation, wild-type enzyme
0.00013
tRNASer
mutant enzyme DELTAG75-N97/DELTAG254-N261, at pH 7.5 and 37°C
0.00019
tRNASer
-
aminoacylation, wild-type enzyme
0.00024
tRNASer
-
substrate from yeast
0.00025
tRNASer
-
substrate from Bombyx mori
0.00025
tRNASer
-
mitochondrial isozyme, pH 7.5, 30°C
0.00026
tRNASer
-
substrate from rabbit liver
0.00033
tRNASer
mutant enzyme DELTAG75-N97, at pH 7.5 and 37°C
0.0004
tRNASer
-
mitochondrial isozyme, pH 7.5, 30°C
0.0005
tRNASer
-
mitochondrial isozyme, pH 7.5, 30°C
0.00051
tRNASer
mutant enzyme DELTAG254-N261, at pH 7.5 and 37°C
0.00054
tRNASer
-
pH 7.6, 37°C
0.00056
tRNASer
-
aminoacylation, wild-type enzyme
0.00058
tRNASer
-
wild-type, using maize tRNA
0.00065
tRNASer
-
mutant ScSerRSDELTAC13 (deletion of 13 C-terminal residues), using yeast tRNA
0.00065
tRNASer
-
mutant ZmcSerRSDELTAC12 (deletion of 12 C-terminal residues), using maize tRNA
0.00066
tRNASer
-
mutant ZmcSerRSDELTAC18 (deletion of 18 C-terminal residues), using maize tRNA
0.00067
tRNASer
-
mitochondrial isozyme, pH 7.5, 30°C
0.00071
tRNASer
-
wild-type, using yeast tRNA
0.00077
tRNASer
wild type enzyme, at pH 7.5 and 37°C
0.0008628
tRNASer
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.002
tRNASer
-
pH 7.5, 50°C, recombinant MtSerRS in presence of recombinant MtArgRS
0.0021
tRNASer
-
mutant E338A
0.0024
tRNASer
-
mutant K164A
0.0026
tRNASer
-
wild-type
0.0029
tRNASer
-
wild-type
0.0034
tRNASer
-
mutant R267A
0.0042
tRNASer
-
mutant E273A
0.0047
tRNASer
-
mutant E273A/D277A/K280A
0.00561
tRNASer
-
pH 7.5, 50°C, recombinant MtSerRS
0.0063
tRNASer
-
mutant R347A
0.0067
tRNASer
-
mutant G340V/G341A
0.0073
tRNASer
at pH 7.6, temperature not specified in the publication
0.0086
tRNASer
37°C, aminoacylation
0.01113
tRNASer
-
wild-type
0.012
tRNASer
30°C, aminoacylation
0.0146
tRNASer
-
mutant R147A
0.02
tRNASer
-
substrate from E. coli
0.24
tRNASer
aminoacylation
0.283
tRNASer
-
mutant N435A
0.41
tRNASer
H270G mutant, aminoacylation
0.412
tRNASer
-
mutant S437A
0.509
tRNASer
-
mutant N435A/S437A
0.76
tRNASer
-
mutant W396A
1.191
tRNASer
-
mutant N435A/S437A/W396A
0.0029
tRNASer(CGA)
-
pH 7.2, 37°C, bacterial type SerRS
-
0.003
tRNASer(CGA)
-
pH 7.2, 37°C, methanogenic SerRS
-
0.0013
tRNASer(GCU)
-
pH 7.2, 37°C, bacterial type SerRS
-
0.0053
tRNASer(GCU)
-
pH 7.2, 37°C, methanogenic SerRS
-
0.0026
tRNASer(GGA)
-
pH 7.2, 37°C, bacterial type SerRS
-
0.0047
tRNASer(GGA)
-
pH 7.2, 37°C, methanogenic SerRS
-
0.00084
tRNASer-I-G-A
-
substrate from yeast
-
0.0011
tRNASer-I-G-A
-
bovine substrate
-
0.0014
tRNASer-I-G-A
-
-
-
0.35
tRNASerGCU
recombinant wild-type enzyme, pH 8.5, 37°C
-
0.37
tRNASerGCU
pH 8.5, 37°C
-
0.37
tRNASerGCU
native wild-type enzyme, pH 8.5, 37°C
-
0.22
tRNASerUGA
pH 8.5, 37°C
-
0.22
tRNASerUGA
native wild-type enzyme, pH 8.5, 37°C
-
0.29
tRNASerUGA
recombinant wild-type enzyme, pH 8.5, 37°C
-
additional information
additional information
-
kinetics
-
additional information
additional information
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
a temperature-dependent inhibition by conformational change of the enzyme (50°C-70°C) lowers both the catalytic activity and the substrate affinity of the ATP and amino acid sites as indicated by a sharp rise in Km with temperature
-
additional information
additional information
-
Lineweaver-Burk plots for Ser and tRNASer are non-linear
-
additional information
additional information
-
Km values for tRNASer transcripts
-
additional information
additional information
-
kinetic changes in presence of several tRNAs, nonchargeable and heterologous ones, in the ATP-diphosphate exchange assay
-
additional information
additional information
-
kinetics for the ATP-diphosphate exchange reaction
-
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
-
additional information
additional information
-
Km-values for different tRNASer variants
-
additional information
additional information
-
calculated binding energies in the activated mode agrees with kinetic measurements of a covalent bond between the amino acid and ATP, quantitative computational analysis of amino acid binding, overview
-
additional information
additional information
calculated binding energies in the activated mode agrees with kinetic measurements of a covalent bond between the amino acid and ATP, quantitative computational analysis of amino acid binding, overview
-
additional information
additional information
-
calculated binding energies in the activated mode agrees with kinetic measurements of a covalent bond between the amino acid and ATP, quantitative computational analysis of amino acid binding, overview
-
additional information
additional information
-
kinetcis
-
additional information
additional information
-
addition of MtArgRS to MtSerRS leads to an almost 4fold increase in the catalytic efficiency of serine attachment to tRNA, also under conditions of elevated temperature and osmolarity, but has no effect on the activity of MtArgRS, steady-state kinetic analyses, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2.433
DL-Serine hydroxamate
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.078
L-cysteine
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.833
L-seryl-tRNASer
-
-
0.14
L-threonine
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.005
tRNASec mutant without anticodon arm
-
pH 7.6, 37°C
-
0.000000011 - 13.7
tRNASer
0.14
tRNASer (Escherichia coli)
-
at pH 7.5 and 30°C
-
0.13
tRNASer (Saccharomyces cerevisiae)
-
at pH 7.5 and 30°C
-
0.023
tRNASer mutant without anticodon arm
-
pH 7.6, 37°C
-
1.07 - 3.05
tRNASer(CGA)
-
0.92 - 1.13
tRNASer(GCU)
-
additional information
additional information
-
0.031 - 0.51
ATP
-
aminoacylation, mutant enzymes
0.04 - 1.97
ATP
-
serine-dependent ATP-diphosphate exchange, mutant enzymes
0.16
ATP
-
wild-type enzyme, pH 7.2, 30°C
0.52
ATP
-
aminoacylation, truncated enzyme
0.59
ATP
-
mutant SerRS11, pH 7.2, 30°C
0.99
ATP
-
aminoacylation, wild-type enzyme
1.16
ATP
-
mutant SerRS12, pH 7.2, 30°C
3.5
ATP
-
serine-dependent ATP-diphosphate exchange, wild-type enzyme
3.9
ATP
-
ATP-diphosphate exchange assay, wild-type enzyme, pH 7.2, 30°C, in absence of tRNASer
6.08
ATP
-
mutant SerRS11, pH 7.2, 30°C
6.08
ATP
-
mutant SerRS12, pH 7.2, 30°C
0.172
L-Ser
-
mutant N435A
0.287
L-Ser
-
mutant W396A
0.46
L-Ser
-
wild-type, using yeast tRNA
0.47
L-Ser
-
mutant ScSerRSDELTAC13 (deletion of 13 C-terminal residues), using yeast tRNA
0.576
L-Ser
-
mutant N435A/S437A
0.729
L-Ser
-
mutant S437A
1.32
L-Ser
-
mutant N435A/S437A/W396A
2.8
L-Ser
-
wild-type, using maize tRNA
3.2
L-Ser
-
mutant ZmcSerRSDELTAC12 (deletion of 12 C-terminal residues), using maize tRNA
3.7
L-Ser
-
mutant ZmcSerRSDELTAC18 (deletion of 18 C-terminal residues), using maize tRNA
0.0014
L-serine
-
mutant enzyme H250A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.016
L-serine
-
mutant enzyme F397P/A399G, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.15
L-serine
-
mutant enzyme P395A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.22
L-serine
-
wild-type enzyme, pH 7.2, 30°C
0.38
L-serine
-
mutant enzyme Q400A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.41
L-serine
-
mutant enzyme G402A/G405A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.78
L-serine
-
mutant SerRS12, pH 7.2, 30°C
1.06
L-serine
-
wild type enzyme, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
1.1
L-serine
-
mutant SerRS11, pH 7.2, 30°C
1.2
L-serine
-
mitochondrial isozyme, aminoacylation reaction, pH 7.5, 30°C
1.8
L-serine
diphosphate exchange
2.5
L-serine
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
6.08
L-serine
-
mutant SerRS12, pH 7.2, 30°C
6.9
L-serine
-
mitochondrial isozyme, ATP-diphosphate exchange reaction, pH 7.2, 30°C
7
L-serine
diphosphate exchange
0.03 - 0.55
Ser
-
aminoacylation, mutant-enzymes
0.052 - 2.1
Ser
-
serine-dependent ATP-diphosphate exchange, mutant enzymes
0.5
Ser
-
ATP, , aminoacylation, wild-type enzyme
0.97
Ser
-
aminoacylation, wild-type enzyme
3.8
Ser
-
serine-dependent ATP-diphosphate exchange, wild-type enzyme
0.007
tRNASec
-
pH 7.6, 37°C
-
9.2
tRNASec
at pH 7.6, temperature not specified in the publication
-
0.000000011
tRNASer
-
mutant G340V/G341A
0.00026
tRNASer
-
mutant R347A
0.005
tRNASer
mutant enzyme DELTAG75-N97/DELTAG254-N261, at pH 7.5 and 37°C
0.0073
tRNASer
-
pH 7.5, 50°C, recombinant MtSerRS
0.0087
tRNASer
-
mutant K164A
0.025
tRNASer
mutant enzyme DELTAG75-N97, at pH 7.5 and 37°C
0.032
tRNASer
-
mutant R267A
0.057 - 0.65
tRNASer
-
aminoacylation, mutant enzymes
0.057
tRNASer
30°C, aminoacylation
0.059
tRNASer
-
mutant E338A
0.062
tRNASer
-
pH 7.6, 37°C
0.1
tRNASer
-
pH 7.5, 50°C, recombinant MtSerRS in presence of recombinant MtArgRS
0.125
tRNASer
37°C, aminoacylation
0.15
tRNASer
-
mutant R147A
0.175
tRNASer
-
mutant N435A/S437A/W396A
0.18
tRNASer
H270G mutant, aminoacylation
0.2
tRNASer
-
mitochondrial isozyme, pH 7.5, 30°C
0.2
tRNASer
mutant enzyme DELTAG254-N261, at pH 7.5 and 37°C
0.239
tRNASer
-
mutant W396A
0.28
tRNASer
-
wild-type enzyme, pH 7.2, 30°C
0.361
tRNASer
-
mutant N435A/S437A
0.396
tRNASer
-
mutant S437A
0.4
tRNASer
-
mutant SerRS11, pH 7.2, 30°C
0.41
tRNASer
-
Ser, , aminoacylation, truncated enzyme
0.43
tRNASer
wild type enzyme, at pH 7.5 and 37°C
0.435
tRNASer
-
mutant N435A
0.454
tRNASer
-
wild-type
0.46
tRNASer
-
mutant SerRS12, pH 7.2, 30°C
0.473
tRNASer
-
wild-type
0.5
tRNASer
-
mitochondrial isozyme, pH 7.5, 30°C
0.54
tRNASer
-
mutant ScSerRSDELTAC13 (deletion of 13 C-terminal residues), using yeast tRNA
0.55
tRNASer
-
aminoacylation, wild-type enzyme
0.55
tRNASer
-
mutant E273A
0.58
tRNASer
-
wild-type, using yeast tRNA
0.9
tRNASer
-
mitochondrial isozyme, pH 7.5, 30°C
1.1
tRNASer
-
aminoacylation, wild-type enzyme
1.1
tRNASer
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
1.2
tRNASer
-
mitochondrial isozyme, pH 7.5, 30°C
1.28
tRNASer
-
mutant ZmcSerRSDELTAC12 (deletion of 12 C-terminal residues), using maize tRNA
1.37
tRNASer
aminoacylation
1.4
tRNASer
-
mutant E273A/D277A/K280A
1.43
tRNASer
-
mutant ZmcSerRSDELTAC18 (deletion of 18 C-terminal residues), using maize tRNA
1.48
tRNASer
-
wild-type, using maize tRNA
13.7
tRNASer
at pH 7.6, temperature not specified in the publication
1.07
tRNASer(CGA)
-
pH 7.2, 37°C, bacterial type SerRS
-
3.05
tRNASer(CGA)
-
pH 7.2, 37°C, methanogenic SerRS
-
0.92
tRNASer(GCU)
-
pH 7.2, 37°C, bacterial type SerRS
-
1.13
tRNASer(GCU)
-
pH 7.2, 37°C, methanogenic SerRS
-
0.9
tRNASer(GGA)
-
pH 7.2, 37°C, bacterial type SerRS
-
4.4
tRNASer(GGA)
-
pH 7.2, 37°C, methanogenic SerRS
-
0.35
tRNASerGCU
pH 8.5, 37°C
-
0.35
tRNASerGCU
native wild-type enzyme, pH 8.5, 37°C
-
0.64
tRNASerGCU
recombinant wild-type enzyme, pH 8.5, 37°C
-
6.08
tRNASerGCU
recombinant wild-type enzyme, pH 8.5, 37°C
-
0.63
tRNASerUGA
pH 8.5, 37°C
-
0.63
tRNASerUGA
native wild-type enzyme, pH 8.5, 37°C
-
0.67
tRNASerUGA
recombinant wild-type enzyme, pH 8.5, 37°C
-
6.08
tRNASerUGA
pH 8.5, 37°C
-
6.08
tRNASerUGA
native wild-type enzyme, pH 8.5, 37°C
-
6.08
tRNASerUGA
recombinant wild-type enzyme, pH 8.5, 37°C
-
additional information
additional information
-
changes in kcat in presence of several tRNAs, nonchargeable and heterologous ones, in the ATP-diphosphate exchange assay
-
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
-
additional information
additional information
-
turnover numbers for different tRNASer variants
-
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DELTA_C
-
mutant, enzymatically inactive
ko095
-
mutant lacking aminoacylation activity
SerRSDELTA35-97
-
truncated mutants with a deletion of the N-terminal arm of the enzyme: SerRSDELTA35-97 and SerRSDELTA56-72. Both mutant have lost their specificity for tRNASer and charge also non-cognate type 1 tRNAs. The deletion has no effect on the amino acid activation step of the reaction, but reduces aminoacylation activity dramatically
C117S
the mutant shows increased activity compared to the wild type enzyme
C46S
the mutant shows increased activity compared to the wild type enzyme
DELTAG254-N261
the mutant shows 72% activity compared to the wild type enzyme
DELTAG75-N97
the mutant shows 13% activity compared to the wild type enzyme
DELTAG75-N97/DELTAG254-N261
the mutant shows 7% activity compared to the wild type enzyme
E156T/R157S
the mutant retains about 10% of wild type activity
E447K
the mutant shows increased activity compared to the wild type enzyme
G136V
the mutant retains about 15% of wild type activity
P30G31Y
the mutation of the P30G31 dipeptide to a single tyrosine almost eliminates serylation activity
C315A
-
site-directed mutagenesis
E273A
-
E273A replacement in helix 9 located in the C-terminal domain
E273A/D277A/K280A
-
triple replacement in helix 9
E338A
-
Km (mM)(tRNASer): 0.0021, kcat (1/sec) (tRNASer): 0.059
F397P/A399G
-
the mutant shows deleterious effects in both kcat and KM values compared to the wild type enzyme
G340V/G341A
-
Km (mM)(tRNASer): 0.0067, kcat (1/sec) (tRNASer): 0.000000011
G402A/G405A
-
the double substitution displays an order of magnitude higher KM but only 2.5fold lower kcat
H250A
-
the mutant is highly efficient in serine activation: kcat is reduced by only 3fold, while KM is reduced relative to the wild type parameters
H250A/Q400A
-
the mutant is highly efficient in serine activation: kcat is reduced by only 3fold, while KM is reduced relative to the wild type parameters
K141A
-
mutated enzyme, serylation rate lowered
K164A
-
K164A replacement in the linker peptide
K79A
-
mutated enzyme, significant drop in the serylation rate
K87A
-
mutated enzyme, retains the serylation ability comparable with the wild-type enzyme
K88A
-
mutated enzyme, retains the serylation ability comparable with the wild-type enzyme
K90A
-
mutated enzyme, retains the serylation ability comparable with the wild-type enzyme
mC306A
-
active site mutant
mC306A/C461A
-
active site mutant
mE338A
-
active site mutant
mG340V/G341A
-
active site mutant
mMbSerRS-CTD
-
START codon introduced at position 167, which generates the C-terminal domain
mMbSerRS-CTDDELTAHTH
-
START codon introduced at position 167 of mMbSerRS-DELTAHTH, generating the C-terminal domain without the helix-turn-helix motif
mMbSerRS-DELTAHTH
-
deleted helix-turn-helix motif
mMbSerRS-NTD
-
STOP codon introduced at position 164, which generates the N-terminal domain
mR267A
-
active site mutant
mR347A
-
active site mutant
mW396A
-
active site mutant
N142A
-
mutated enzyme, serylation rate lowered
N435A
-
Km (mM) (L-Ser): 0.07028, kcat (1/sec) (L-Ser): 0.172, Km (mM)(tRNASer): 0.283, kcat (1/sec) (tRNASer): 0.435
N435A/S437A
-
Km (mM) (L-Ser): 0.689, kcat (1/sec) (L-Ser): 0.576, Km (mM)(tRNASer): 0.509, kcat (1/sec) (tRNASer): 0.361
N435A/S437A/W396A
-
Km (mM) (L-Ser): 0.2879, kcat (1/sec) (L-Ser): 1.32, Km (mM)(tRNASer): 1.191, kcat (1/sec) (tRNASer): 0.175
P395A
-
the mutant shows 6.5fold reduced enzyme efficiency compared to the wild type
Q400A
-
the mutation produces only small kinetic effects: KM is elevated 2fold while kcat is reduced 2fold
R143A
-
mutated enzyme, serylation rate lowered
R147A
-
R147A replacement in helix 4 located in the N-terminal domain
R267A
-
Km (mM)(tRNASer): 0.0034, kcat (1/sec) (tRNASer): 0.032
R347A
-
Km (mM)(tRNASer): 0.0063, kcat (1/sec) (tRNASer): 0.0026
R38A
-
mutated enzyme, serylation rate lowered
R76A
-
mutated enzyme, serylation ability completely lost
R78A
-
mutated enzyme, retains the serylation ability comparable with the wild-type enzyme
R94A
-
mutated enzyme, significant drop in the serylation rate
S437A
-
Km (mM) (L-Ser): 0.573, kcat (1/sec) (L-Ser): 0.729, Km (mM)(tRNASer): 0.412, kcat (1/sec) (tRNASer): 0.396
W396A
-
Km (mM)(L-Ser): 0.2645, kcat (1/sec) (L-Ser): 0.287, Km (mM)(tRNASer): 0.760, kcat (1/sec) (tRNASer): 0.239
Y89A
-
mutated enzyme, retains the serylation ability comparable with the wild-type enzyme
A289V
-
mutations in the active site mutant SerRS11, mutant is less sensitive to inhibition by serine hydroxamate and 5'-O-[N-(L-seryl)-sulfamoyl]adenosine
D288Y
-
mutations in the active site mutant SerRS11, mutant is less sensitive to inhibition by serine hydroxamate and 5'-O-[N-(L-seryl)-sulfamoyl]adenosine
E281D/G291A
-
reduced activity compared to the wild-type enzyme
K287R
-
mutations in the active site mutant SerRS12, mutant is less sensitive to inhibition by serine hydroxamate and 5'-O-[N-(L-seryl)-sulfamoyl]adenosine
K287T
-
mutations in the active site mutant SerRS11, mutant is less sensitive to inhibition by serine hydroxamate and 5'-O-[N-(L-seryl)-sulfamoyl]adenosine
ScSerRSDELTAC13
-
mutant containing a deletion of 13 C-terminal residues, mutant is readily complement a ScSerRS null allele, Km and Kcat values comparable to wild-type, T50: 44.5°C, interaction with Pex21p is lost
ScSerRSDELTAC203
-
mutant containing a deletion of 20 C-terminal residues, mutant does not complement a ScSerRS null allele, T50: 44.5°C
DELTA2-22
-
in transformed protoplasts, transient expression of deletion mutant reveals GFP fluorescence throughout the cytosol, implying that the very N-terminal region is necessary for the correct targeting of SerZMo into mitochondria and chloroplasts
DELTA2-73
-
transient expression of the SerZMo fusion protein with fully truncated N-terminal extension DELTA2-73 SerZMo-GFP, give diffuse GFP fluorescence throughout the cytosol and shos no association with mitochondria or chloroplasts
DELTA81-511
-
mutant construct containing only the first 80 amino acids is expressed in chloroblasts and in mitochondria as shown by GFP-fusion protein
ZmcSerRSDELTAC12
-
mutant containing a deletion of 12 C-terminal residues, mutant readily complements a yeast SerRS null allele, Km and Kcat values comparable to wild-type
ZmcSerRSDELTAC18
-
mutant containing a deletion of 18 C-terminal residues, mutant readily complements a yeast SerRS null allele, Km and Kcat values comparable to wild-type, T50: 31.5°C, interaction with Pex21p is lost
ZmcSerRSDELTAC26
-
mutant containing a deletion of 26 C-terminal residues, mutant does not complement a yeast SerRS null allele, enzymatic activity of mutant protein is comparable to negative control. Expression of mutant protein is probably severly hindered due to intrinsic instability of the truncated protein
T429A
-
mutant, enzymatically inactive
T429A
the abnormal branching of intersegmental vessels in ko095 mutant is suppressed by the introduction of either wild-type or mutant T429A seryl-tRNA synthetase, T429A lacks the enzymatic activity that catalyzes aminoacylation of transfer RNA for serine
additional information
ko095, an embryonic lethal mutant with abnormal branching in the head and trunk blood vessels, the gene responsible for ko095 encodes seryl-tRNA synthetase with a nonsense mutation
additional information
-
ko095, an embryonic lethal mutant with abnormal branching in the head and trunk blood vessels, the gene responsible for ko095 encodes seryl-tRNA synthetase with a nonsense mutation
additional information
-
deletion of any but the anticodon domain of tRNASer and tRNASec causes a dramatic loss of serine acceptance
additional information
models of Pyrococcus horikoshii SerRS bound with the Thermus thermophilus and Pyrococcus horikoshii tRNA(Ser)s suggest that the helical domain of Pyrococcus horikoshii SerRS is involved in the extra arm binding. This region of SerRS has additional basic residues as compared with Thermus thermophilus SerRS, and a Trp residue specific to the archaeal/eukaryal SerRSs. Mutational analyses reveales that the basic and Trp residues are important for tRNA aminoacylation
additional information
-
models of Pyrococcus horikoshii SerRS bound with the Thermus thermophilus and Pyrococcus horikoshii tRNA(Ser)s suggest that the helical domain of Pyrococcus horikoshii SerRS is involved in the extra arm binding. This region of SerRS has additional basic residues as compared with Thermus thermophilus SerRS, and a Trp residue specific to the archaeal/eukaryal SerRSs. Mutational analyses reveales that the basic and Trp residues are important for tRNA aminoacylation
additional information
-
mutants with mutagenesis of portion of the SES1 gene encoding the motif 2 loop reavel elevated Km values for Ser and ATP accompanied by decreases in kcat
additional information
-
overexpressing, mutant lacking those 60 base pairs that encode the C-terminal peptide. The truncation mutant is less stable to heat inactivation at 42°C and binds tRNA with 3.6fold higher affinity, while the Km for Ser is 4fold increased relatively to the wild-type
additional information
-
construction of the active site mutants SerRS11 and SerRS12
additional information
-
construction of several deletion mutants of seryl-tRNA synthetase, deletion of the 13 C-terminal amino acids abolishes Pex21p binding to seryl-tRNA synthetase, overview
additional information
-
RNAi-mediated ablation of SerRS using stem-loop constructs containing the puromycin resistance gene, overview
additional information
-
ZmcSerRS does not bind yeast Pex21 protein. Although the yeast C-terminal SerRS extension is required for Pex21p binding, the maize counterpart with an appended yeast SerRS extension remains incapable of Pex21p binding, implying that additional regions of yeast SerRS also contribute to the interaction with the peroxin
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The structural basis for seryl-adenylate and Ap4A synthesis by seryl-tRNA synthetase
Structure
3
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1995
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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
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Bos taurus
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Gibbons, W.J., Jr.; Yan, Q.; Li, R.; Li, X.; Guan, M.X.
Genomic organization, expression, and subcellular localization of mouse mitochondrial seryl-tRNA synthetase
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Chimnaronk, S.; Gravers Jeppesen, M.; Suzuki, T.; Nyborg, J.; Watanabe, K.
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EMBO J.
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The unusual methanogenic seryl-tRNA synthetase recognizes tRNASer species from all three kingdoms of life
Eur. J. Biochem.
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Selective inhibition of divergent seryl-tRNA synthetases by serine analogues
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Methanosarcina barkeri
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Lukash, T.O.; Turkivska, H.V.; Negrutskii, B.S.; El'skaya, A.V.
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Korencic, D.; Polycarpo, C.; Weygand-Durasevic, I.; Soll, D.
Differential modes of transfer RNASer recognition in Methanosarcina barkeri
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Kim, Y.K.; Lee, J.Y.; Cho, H.S.; Lee, S.S.; Ha, H.J.; Kim, S.; Choi, D.; Pai, H.S.
Inactivation of organellar glutamyl- and seryl-tRNA synthetases leads to developmental arrest of chloroplasts and mitochondria in higher plants
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Rokov-Plavec, J.; Bilokapic, S.; Gruic-Sovulj, I.; Mocibob, M.; Glavan, F.; Brgles, M.; Weygand-Durasevic, I.
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Period. Biol.
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Foerster, C.; Brauer, A.B.; Fuerste, J.P.; Betzel, C.h.; Weber, M.; Cordes, F.; Erdmann, V.A.
Superposition of a tRNASer acceptor stem microhelix into the seryl-tRNA synthetase complex
Biochem. Biophys. Res. Commun.
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Thermus thermophilus (P34945)
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Bilokapic, S.; Maier, T.; Ahel, D.; Gruic-Sovulj, I.; Soell, D.; Weygand-Durasevic, I.; Ban, N.
Structure of the unusual seryl-tRNA synthetase reveals a distinct zinc-dependent mode of substrate recognition
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Methanosarcina barkeri
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Godinic, V.; Mocibob, M.; Rocak, S.; Ibba, M.; Weygand-Durasevic, I.
Peroxin Pex21p interacts with the C-terminal noncatalytic domain of yeast seryl-tRNA synthetase and forms a specific ternary complex with tRNA(Ser)
FEBS J.
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Saccharomyces cerevisiae
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Garg, R.P.; Gonzalez, J.M.; Parry, R.J.
Biochemical characterization of VlmL, a Seryl-tRNA synthetase encoded by the valanimycin biosynthetic gene cluster
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Streptomyces avermitilis (Q82KS8), Streptomyces viridifaciens (Q84F26), Streptomyces viridifaciens, Streptomyces coelicolor (Q9ZBX1), Streptomyces coelicolor
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Geslain, R.; Aeby, E.; Guitart, T.; Jones, T.E.; Castro de Moura, M.; Charriere, F.; Schneider, A.; Ribas de Pouplana, L.
Trypanosoma seryl-tRNA synthetase is a metazoan-like enzyme with high affinity for tRNASec
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Trypanosoma brucei, Trypanosoma cruzi (Q4CW46)
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McClendon, C.L.; Vaidehi, N.; Kam, V.W.; Zhang, D.; Goddard, W.A.
Fidelity of seryl-tRNA synthetase to binding of natural amino acids from HierDock first principles computations
Protein Eng. Des. Sel.
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Saccharomyces cerevisiae, Thermus thermophilus (P34945), Thermus thermophilus
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Mocibob, M.; Weygand-Durasevic, I.
The proximal region of a noncatalytic eukaryotic seryl-tRNA synthetase extension is required for protein stability in vitro and in vivo
Arch. Biochem. Biophys.
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Saccharomyces cerevisiae, Zea mays
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Bilokapic, S.; Rokov Plavec, J.; Ban, N.; Weygand-Durasevic, I.
Structural flexibility of the methanogenic-type seryl-tRNA synthetase active site and its implication for specific substrate recognition
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Methanosarcina barkeri
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Gundllapalli, S.; Ambrogelly, A.; Umehara, T.; Li, D.; Polycarpo, C.; Soell, D.
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Dual targeting of organellar seryl-tRNA synthetase to maize mitochondria and chloroplasts
Plant Cell Rep.
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Zea mays
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Garg, R.P.; Qian, X.L.; Alemany, L.B.; Moran, S.; Parry, R.J.
Investigations of valanimycin biosynthesis: elucidation of the role of seryl-tRNA
Proc. Natl. Acad. Sci. USA
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Streptomyces viridifaciens, Streptomyces viridifaciens MG456-hF10
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Itoh, Y.; Sekine, S.I.; Kuroishi, C.; Terada, T.; Shirouzu, M.; Kuramitsu, S.; Yokoyama, S.
Crystallographic and mutational studies of seryl-tRNA synthetase from the archaeon Pyrococcus horikoshii
RNA Biol.
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Pyrococcus horikoshii (O58441), Pyrococcus horikoshii
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Zeng, Y.; Roy, H.; Patil, P.B.; Ibba, M.; Chen, S.
Characterization of two seryl-tRNA synthetases in albomycin-producing Streptomyces sp. strain ATCC 700974
Antimicrob. Agents Chemother.
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Streptomyces sp. (D0UD38), Streptomyces sp. (D0UD39)
brenda
Eichert, A.; Fuerste, J.P.; Ulrich, A.; Betzel, C.; Erdmann, V.A.; Foerster, C.
Superposition of two tRNA(Ser) acceptor stem crystal structures: Comparison of structure, ligands and hydration
Biochem. Biophys. Res. Commun.
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Escherichia coli
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Fukui, H.; Hanaoka, R.; Kawahara, A.
Noncanonical activity of seryl-tRNA synthetase is involved in vascular development
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Danio rerio (Q6DRC0), Danio rerio
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Herzog, W.; Mueller, K.; Huisken, J.; Stainier, D.Y.
Genetic evidence for a noncanonical function of seryl-tRNA synthetase in vascular development
Circ. Res.
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Danio rerio, Homo sapiens
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Lesjak, S.; Weygand-Durasevic, I.
Recognition between tRNASer and archaeal seryl-tRNA synthetases monitored by suppression of bacterial amber mutations
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Methanosarcina barkeri
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Bilokapic, S.; Ivic, N.; Godinic-Mikulcic, V.; Piantanida, I.; Ban, N.; Weygand-Durasevic, I.
Idiosyncratic helix-turn-helix motif in Methanosarcina barkeri seryl-tRNA synthetase has a critical architectural role
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Methanosarcina barkeri
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Jaric, J.; Bilokapic, S.; Lesjak, S.; Crnkovic, A.; Ban, N.; Weygand-Durasevic, I.
Identification of amino acids in the N-terminal domain of atypical methanogenic-type Seryl-tRNA synthetase critical for tRNA recognition
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Methanosarcina barkeri
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Kawahara, A.; Stainier, D.Y.
Noncanonical activity of seryl-transfer RNA synthetase and vascular development
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Danio rerio, Homo sapiens
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Artero, J.B.; Teixeira, S.C.; Mitchell, E.P.; Kron, M.A.; Forsyth, V.T.; Haertlein, M.
Crystallization and preliminary X-ray diffraction analysis of human cytosolic seryl-tRNA synthetase
Acta Crystallogr. Sect. F
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Homo sapiens
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Rocha, R.; Barbosa Pereira, P.J.; Santos, M.A.; Macedo-Ribeiro, S.
Purification, crystallization and preliminary X-ray diffraction analysis of the seryl-tRNA synthetase from Candida albicans
Acta Crystallogr. Sect. F
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Candida albicans (Q9HGT6), Candida albicans
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Lesjak, S.; Boko, D.; Weygand-Durasevic, I.
Seryl-tRNA synthetases from methanogenic archaea: suppression of bacterial amber mutation and heterologous toxicity
Food Technol. Biotechnol.
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Methanocaldococcus jannaschii, Methanococcus maripaludis
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Godinic-Mikulcic, V.; Jaric, J.; Hausmann, C.D.; Ibba, M.; Weygand-Durasevic, I.
An archaeal tRNA-synthetase complex that enhances aminoacylation under extreme conditions
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Methanothermobacter thermautotrophicus
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Itoh, Y.; Sekine, S.I.; Yokoyama, S.
Crystallization and preliminary X-ray crystallographic analysis of bacterial tRNA(Sec) in complex with seryl-tRNA synthetase
Acta Crystallogr. Sect. F
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678-682
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Methanopyrus kandleri
brenda
Rokov-Plavec, J.; Lesjak, S.; Gruic-Sovulj, I.; Mocibob, M.; Dulic, M.; Weygand-Durasevic, I.
Substrate recognition and fidelity of maize seryl-tRNA synthetases
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Zea mays
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Eichert, A.; Oberthuer, D.; Betzel, C.; Gessner, R.; Erdmann, V.A.; Fuerste, J.P.; Foerster, C.
The seryl-tRNA synthetase/tRNASer acceptor stem interface is mediated via a specific network of water molecules
Biochem. Biophys. Res. Commun.
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Escherichia coli
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Dulic, M.; Pozar, J.; Bilokapic, S.; Weygand-Durasevic, I.; Gruic-Sovulj, I.
An idiosyncratic serine ordering loop in methanogen seryl-tRNA synthetases guides substrates through seryl-tRNASer formation
Biochimie
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Methanosarcina barkeri
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Battenberg, O.A.; Yang, Y.; Verhelst, S.H.; Sieber, S.A.
Target profiling of 4-hydroxyderricin in S. aureus reveals seryl-tRNA synthetase binding and inhibition by covalent modification
Mol. Biosyst.
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Staphylococcus aureus, Staphylococcus aureus NCTC 8325
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Xu, X.; Shi, Y.; Yang, X.L.
Crystal structure of human seryl-tRNA synthetase and Ser-SA complex reveals a molecular lever specific to higher eukaryotes
Structure
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Homo sapiens (P49591), Homo sapiens
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Kugimiya, A.; Matsuzaki, E.
Microfluidic analysis of serine levels using seryl-tRNA synthetase coupled with spectrophotometric detection
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Thermotoga maritima
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Ikromov, O.; Alkamal, I.; Magheli, A.; Ratert, N.; Sendeski, M.; Miller, K.; Krause, H.; Kempkensteffen, C.
Functional epigenetic analysis of prostate carcinoma a role for seryl-tRNA synthetase?
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Homo sapiens
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Dutta, S.; Nandi, N.
Classical molecular dynamics simulation of seryl tRNA synthetase and threonyl tRNA synthetase bound with tRNA and aminoacyl adenylate
J. Biomol. Struct. Dyn.
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Thermus thermophilus (P34945), Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (P34945), Thermus thermophilus DSM 7039 (P34945)
brenda
Dutta, S.; Nandi, N.
Dynamics of the active sites of dimeric seryl tRNA synthetase from Methanopyrus kandleri
J. Phys. Chem. B
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Methanopyrus kandleri (Q8TVD2), Methanopyrus kandleri
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Kekez, M.; Bauer, N.; Saric, E.; Rokov-Plavec, J.
Exclusive cytosolic localization and broad tRNASer specificity of Arabidopsis thaliana seryl-tRNA synthetase
J. Plant Biol.
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Arabidopsis thaliana
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Wang, C.; Guo, Y.; Tian, Q.; Jia, Q.; Gao, Y.; Zhang, Q.; Zhou, C.; Xie, W.
SerRS-tRNASec complex structures reveal mechanism of the first step in selenocysteine biosynthesis
Nucleic Acids Res.
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10534-10545
2015
Homo sapiens (P49591), Homo sapiens
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Holman, K.M.; Puppala, A.K.; Lee, J.W.; Lee, H.; Simonovic, M.
Insights into substrate promiscuity of human seryl-tRNA synthetase
RNA
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Homo sapiens (P49591), Homo sapiens
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Hu, J.; Tian, J.; Li, F.; Xue, B.; Hu, J.; Cheng, X.; Li, J.; Shen, W.; Li, B.
Clone and functional analysis of seryl-tRNA synthetase and tyrosyl-tRNA synthetase from silkworm, Bombyx mori
Sci. Rep.
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41563
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Bombyx mori, Bombyx mori (A0A1Q1NKM3)
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