6.1.1.11: serine-tRNA ligase
This is an abbreviated version!
For detailed information about serine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.11
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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
-
handheld
-
albomycins
-
citrate-reduced
-
molecular biology
-
nanostars
-
selenophosphate
- 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
-
handheld
- albomycins
-
citrate-reduced
- molecular biology
-
nanostars
- selenophosphate
Reaction
Synonyms
62 kDa RNA-binding protein, bacterial SerRS, bacterial type seryl-tRNA synthetase, bacterial-type SerRS, bMbSerRS, methanogenic SerRS, methanogenic type seryl-tRNA synthetase, methanogenic-type SerRS, methanogenic-type SerRSs, methanogenic-type seryl-tRNA synthetase, mMbSerRS, mSerRS, mtSerRS, SARS, SCSerS, Serine transfer RNA synthetase, Serine translase, Serine--tRNA ligase, SerRS, SerRS1, SerRS2, SerRSmt, serS, SERSEC, seryl tRNA synthetase, Seryl-transfer ribonucleate synthetase, Seryl-transfer ribonucleic acid synthetase, Seryl-transfer RNA synthetase, Seryl-tRNA synthetase, seryl-tRNA synthetase 1, seryl-tRNA synthetase 2, seryl-tRNA-synthetase, SerZMo, STS, subclass IIa dimeric SerRS, SvsR, Synthetase, seryl-transfer ribonucleate, tRNASer/seryl-tRNA synthetase, ttSerRS, TT_C0520, VlmL, ZmSerS
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6.1.1.11 serine-tRNA ligaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 6.1.1.11 - serine-tRNA ligase
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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
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
-
-
-
?
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 + 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 (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(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 + tRNASerCGA
AMP + diphosphate + L-seryl-tRNASerCGA
-
-
-
-
?
ATP + L-threonine + tRNASer
AMP + diphosphate + L-threonyl-tRNASer
-
very weak activity
-
-
?
formycin 5'-triphosphate + L-serine + tRNASer
formycin 5'-monophosphate + diphosphate + L-seryl-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
-
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
Escherichia coli B / ATCC 11303
-
-
-
?
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
-
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
-
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
-
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
-
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
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
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
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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
-
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
?
-
-
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
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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
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additional information
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Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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
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additional information
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no activity with tRNASer from Arabidopsis thaliana, the enzyme also performs the ATP-diphosphate exchange reaction
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