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Information on EC 6.1.1.11 - serine-tRNA ligase
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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
- silver
- nanoparticles
- aminoacyl-trna
- aminoacylation
-
serylation
-
colloid
- selenocysteine
-
anticodon
- trnasec
-
aarss
- lysyl-trna
-
roughened
- phenylalanyl-trna
-
isoacceptors
- selenophosphate
-
nanoprobes
-
langmuir-blodgett
- molecular biology
- trnatyr
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
62 kDa RNA-binding protein
mMbSerRS
mtSerRS
SARS
Serine transfer RNA synthetase
Serine translase
Serine--tRNA ligase
SerRS
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 synthetases
STS
Synthetase, seryl-transfer ribonucleate
ttSerRS
TT_C0520
VlmL
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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Serine--tRNA ligase
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SerRS
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SerRS
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two different types: bacterial-type SerRS and highly divergent SerRS
SerRSmt
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SERSEC
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Seryl-transfer ribonucleate synthetase
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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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Seryl-tRNA synthetase
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Synthetase, seryl-transfer ribonucleate
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer
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-
-
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ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer
subtrate recognition mechanism
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ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer
catalytic mechanism, specificity of substrate binding is mediated by the amino acids in motif 2 loop
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ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer
tRNA substrate discrimination mechanism
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ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer
the tRNA recognition mechanism of mammalian mitochondrial enzymediffers considerably from that of its prokaryotic counterpart
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ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer
the tRNA recognition mechanism of mammalian mitochondrial enzyme differs considerably from that of its prokaryotic counterpart
ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer
the tRNA recognition mechanism of mammalian mitochondrial enzyme differs considerably from that of its prokaryotic counterpart
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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
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ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer
reaction mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Aminoacylation
esterification
Aminoacylation
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esterification
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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.
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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
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
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-
-
-
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
-
-
-
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ATP + L-cysteine + tRNASer
AMP + diphosphate + L-cysteinyl-tRNASer
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very weak activity
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-
?
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
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-
?
ATP + L-serine + tRNAPyl
AMP + diphosphate + L-seryl-tRNAPyl
-
-
-
-
?
ATP + L-serine + tRNASec
AMP + diphosphate + L-seryl-tRNASe
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selenocysteine-incorporating tRNA wild-type and deletion mutants, secondary structures
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?
ATP + L-serine + tRNASecUCA
AMP + diphosphate + L-seryl-tRNASecUCA
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SerRS also aminoacylates tRNASec with serine as the first step for the incorporation of selenocysteine into proteins
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-
?
ATP + L-serine + tRNASer (Escherichia coli)
AMP + diphosphate + L-seryl-tRNASer (Escherichia coli)
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-
-
-
?
ATP + L-serine + tRNASer (Saccharomyces cerevisiae)
AMP + diphosphate + L-seryl-tRNASer (Saccharomyces cerevisiae)
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-
-
-
?
ATP + L-serine + tRNASerCGA
AMP + diphosphate + L-seryl-tRNASerCGA
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-
-
-
?
ATP + L-threonine + tRNASer
AMP + diphosphate + L-threonyl-tRNASer
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very weak activity
-
-
?
formycin 5'-triphosphate + L-serine + tRNASer
formycin 5'-monophosphate + diphosphate + L-seryl-tRNASer
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-
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ATP + L-serine + tRNASec
AMP + diphosphate + L-seryl-tRNASec
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15.8% activity compared to tRNASer
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?
ATP + L-serine + tRNASec
AMP + diphosphate + L-seryl-tRNASec
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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
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-
?
ATP + L-serine + tRNASec
AMP + diphosphate + L-seryl-tRNASec
Q4CW46
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
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?
ATP + L-serine + tRNASec
AMP + diphosphate + L-seryl-tRNASec
Q4CW46
SerRS also aminoacylates tRNASec with serine as the first step for the incorporation of selenocysteine into proteins
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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D-Ser can replace L-Ser in ATP-diphosphate exchange
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ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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the enzyme selectively recognizes tRNASer on the basis of its characteristic tertiary structure rather than the nucleotides specific to tRNASer
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ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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the enzyme only recognizes cognate tRNA
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
Escherichia coli B / ATCC 11303
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ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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100% activity
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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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
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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serylates tRNASer from methanobacteria, Escherichia coli and Saccharomyces cerevisiae
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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the seryl-tRNA synthetase recognizes eukaryotic and bacterial tRNASer, in addition to the homologous tRNASer and tRNASec
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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serylates tRNASer from methanobacteria, Escherichia coli and Saccharomyces cerevisiae
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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the seryl-tRNA synthetase recognizes eukaryotic and bacterial tRNASer, in addition to the homologous tRNASer and tRNASec
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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-
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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-
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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serylates tRNASer from methanobacteria and Escherichia coli, no activity with tRNASer from Saccharomyces cerevisiae
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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-
-
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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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
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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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
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?
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
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
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?
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
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ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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enzyme aminoacylates E. coli tRNA with Ser much more poorly than its homologous tRNAs
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ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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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
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ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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amino acids within motif 2 loop are involved in specific binding of L-serine and ATP to the enzyme
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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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
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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formation of a seryl adenylate intermediate, mechanism of discrimination between cognate and noncognate amino acids, quantitative computational analysis, overview
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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role of Pex21p in enhancing cognate tRNA binding by SerRS
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-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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-
-
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ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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-
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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
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?
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
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
Q4CW46
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
Q4CW46
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 + 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
?
-
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high abundance in middle silk gland may result from an adaption of this organ for the production of the serine-rich protein, sericin
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-
additional information
?
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substrate specificity with diverse mutant variants of tRNASerUGA and tRNASerGCU with the recombinant mitochondrial isozyme, overview
-
?
additional information
?
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-
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
-
-
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additional information
?
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in contrast to the bacterial-type SerRS the methanogenic SerRS shows no detectable charging of tRNApyrrolysine (tRNAPyl)
-
-
-
additional information
?
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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
?
-
-
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
?
-
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
-
-
-
additional information
?
-
-
no activity with tRNASer from Arabidopsis thaliana, the enzyme also performs the ATP-diphosphate exchange reaction
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-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
Q4CW46
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 + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
Q9NP81
-
-
?
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
Q8TVD2
-
-
-
?
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
Q9JJL8
-
-
?
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
-
-
-
?
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
P95689
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
Q82KS8
-
-
-
r
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
Q9ZBX1
-
-
-
r
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
D0UD38, D0UD39
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
Q84F26
-
-
-
r
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
P34945
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
P34945
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
P34945
-
-
-
?
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
Q4CW46
responsible for the serylation of both tRNASer and tRNASec
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
O82110
tRNASer from Escherichia coli
-
?
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
?
-
-
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
?
-
-
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
?
-
Q84F26
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
binding of ATP leads to the stabilization of a motif 2 loop that interacts with the tRNA acceptor stem
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Zn2+
Mg2+
-
two Mg2+ binding sites, which influence the aminoacylation of tRNASer, possibly via different Mg2+-ATP complexes
Mn2+
-
the enzyme complexes: 1. with ATP and Mn2+, 2. containing seryl-adenylate in the active site, 3. between the enzyme, Ap4A and Mn2+, exhibit a common Mn2+-site in which the cation is coordinated by two active-site residues in addition to the alpha-phosphate group from the bound ligands
Zn2+
-
absolute requirement of the metal ion for enzymatic activity, active site binding structure, tetra-coordinated by Cys306, Glu355 and Cys461, binds the amino group of the serine substrate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(E)-3-(3-ethynyl-4-hydroxyphenyl)-1-(2-hydroxy-4-methoxy-3-(3-methylbut-2-en-1-yl)phenyl)prop-2-en-1-one
-
-
Mg2+
-
inhibition by dead-end complex formation between the ternary complex, E-ATP-Ser, and either free Mg2+ or Mg2P2O7
serinamide
-
inhibition of methanogenic type seryl-tRNA synthetase, no inhibition of bacterial type seryl-tRNA synthetase
additional information
-
Trypanosoma brucei is highly sensitive to the action of specific selenoprotein inhibitors
-
5'-O-[N-(L-Seryl)-sulfamoyl]adenosine
-
stable analogue of aminoacyl adenylate intermediate
DL-Serine hydroxamate
-
inhibition constant for Saccharomyces cerevisiae enzyme is 90fold higher than for Escherichia coli enzyme
DL-Serine hydroxamate
-
inhibition constant for Saccharomyces cerevisiae enzyme is 90fold higher than for Escherichia coli enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Pex21p
-
the enzyme interacts with the peroxisome biogenesis-related factor Pex21p, the C-terminally appended domain of yeast seryl-tRNA synthetase does not participate in substrate binding, but instead is required for association with Pex21p, Pex21p does not directly bind tRNA, and nor does it possess a tRNA-binding motif, but it instead participates in the formation of a specific ternary complex with seryl-tRNA synthetase and tRNASer, strengthening the interaction of seryl-tRNA synthetase with its cognate tRNASer, overview
-
tRNASer
-
promotes the binding of the other substrates, probably due to a conformational change in motif 2 region
tRNASer
-
binding to the enzyme enhances the discrimination of the amino acid substrate and the activity, and diminishes the rate of misactivation of threonine, all due to a conformational chage in the enzymes active site
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alkalosis
Mutations in the mitochondrial seryl-tRNA synthetase cause hyperuricemia, pulmonary hypertension, renal failure in infancy and alkalosis, HUPRA syndrome.
Breast Neoplasms
Surface-enhanced resonance Raman scattering nanostars for high-precision cancer imaging.
Breast Neoplasms
Through tissue imaging of a live breast cancer tumour model using handheld surface enhanced spatially offset resonance Raman spectroscopy (SESORRS).
Cystic Fibrosis
Simple multiplex genotyping by surface-enhanced resonance Raman scattering.
Cystic Fibrosis
Surface enhanced resonance Raman scattering (SERRS)--a first example of its use in multiplex genotyping.
Deafness
Characterization and tRNA recognition of mammalian mitochondrial seryl-tRNA synthetase.
Deafness
Novel coding-region polymorphisms in mitochondrial seryl-tRNA synthetase (SARSM) and mitoribosomal protein S12 (RPMS12) genes in DFNA4 autosomal dominant deafness families.
Glioblastoma
An EGFRvIII targeted dual-modal gold nanoprobe for imaging-guided brain tumor surgery.
Glioblastoma
High Precision Imaging of Microscopic Spread of Glioblastoma with a Targeted Ultrasensitive SERRS Molecular Imaging Probe.
Hypertension, Pulmonary
Mutations in the mitochondrial seryl-tRNA synthetase cause hyperuricemia, pulmonary hypertension, renal failure in infancy and alkalosis, HUPRA syndrome.
Hypertension, Pulmonary
Splicing Defect in Mitochondrial Seryl-tRNA Synthetase Gene Causes Progressive Spastic Paresis Instead of HUPRA Syndrome.
Liver Diseases
PreS1 peptide-functionalized gold nanostructures with SERRS tags for efficient liver cancer cell targeting.
Liver Neoplasms
PreS1 peptide-functionalized gold nanostructures with SERRS tags for efficient liver cancer cell targeting.
Malaria
Magnetic field enriched surface enhanced resonance Raman spectroscopy for early malaria diagnosis.
Malaria
Optimization of Fe3O4@Ag nanoshells in magnetic field-enriched surface-enhanced resonance Raman scattering for malaria diagnosis.
Malaria
Surface-enhanced resonance Raman scattering of hemoproteins and those in complicated biological systems.
Muscle Spasticity
Splicing Defect in Mitochondrial Seryl-tRNA Synthetase Gene Causes Progressive Spastic Paresis Instead of HUPRA Syndrome.
Neoplasm Metastasis
Tissue factor-specific ultra-bright SERRS nanostars for Raman detection of pulmonary micrometastases.
Neoplasm Micrometastasis
Tissue factor-specific ultra-bright SERRS nanostars for Raman detection of pulmonary micrometastases.
Neoplasms
Au@pNIPAM SERRS Tags for Multiplex Immunophenotyping Cellular Receptors and Imaging Tumor Cells.
Neoplasms
Bioimaging: Au@pNIPAM SERRS Tags for Multiplex Immunophenotyping Cellular Receptors and Imaging Tumor Cells (Small 33/2015).
Neoplasms
Chelator-Free Radiolabeling of SERRS Nanoparticles for Whole-Body PET and Intraoperative Raman Imaging.
Neoplasms
Graphene oxide-encoded Ag nanoshells with single-particle detection sensitivity towards cancer cell imaging based on SERRS.
Neoplasms
High Precision Imaging of Microscopic Spread of Glioblastoma with a Targeted Ultrasensitive SERRS Molecular Imaging Probe.
Neoplasms
High-speed Raman-encoded molecular imaging of freshly excised tissue surfaces with topically applied SERRS nanoparticles.
Neoplasms
Non-invasive In Vivo Imaging of Cancer Using Surface-Enhanced Spatially Offset Raman Spectroscopy (SESORS).
Neoplasms
PreS1 peptide-functionalized gold nanostructures with SERRS tags for efficient liver cancer cell targeting.
Neoplasms
Quantitative ratiometric discrimination between noncancerous and cancerous prostate cells based on neuropilin-1 overexpression.
Neoplasms
Rational design of a chalcogenopyrylium-based surface-enhanced resonance Raman scattering nanoprobe with attomolar sensitivity.
Neoplasms
Safe core-satellite magneto-plasmonic nanostructures for efficient targeting and photothermal treatment of tumor cells.
Neoplasms
Sensitive Trimodal Magnetic Resonance Imaging-Surface-Enhanced Resonance Raman Scattering-Fluorescence Detection of Cancer Cells with Stable Magneto-Plasmonic Nanoprobes.
Neoplasms
Surface-enhanced resonance Raman scattering nanostars for high-precision cancer imaging.
Neoplasms
Surface-Enhanced Resonance Raman Scattering-Guided Brain Tumor Surgery Showing Prognostic Benefit in Rat Models.
Pancreatic Neoplasms
Surface-enhanced resonance Raman scattering nanostars for high-precision cancer imaging.
Paresis
Splicing Defect in Mitochondrial Seryl-tRNA Synthetase Gene Causes Progressive Spastic Paresis Instead of HUPRA Syndrome.
Prostatic Neoplasms
Surface-enhanced resonance Raman scattering nanostars for high-precision cancer imaging.
Renal Insufficiency
Mutations in the mitochondrial seryl-tRNA synthetase cause hyperuricemia, pulmonary hypertension, renal failure in infancy and alkalosis, HUPRA syndrome.
Renal Insufficiency
Splicing Defect in Mitochondrial Seryl-tRNA Synthetase Gene Causes Progressive Spastic Paresis Instead of HUPRA Syndrome.
Sarcoma
Surface-enhanced resonance Raman scattering nanostars for high-precision cancer imaging.
Stroke
In situ surface enhanced resonance Raman scattering (SERRS) spectroscopy of biro inks--long-term stability of colloid treated samples.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.35
DL-Serine hydroxamate
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
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
0.0004
mitochondrial tRNASer from yeast subtype 2
-
mitochondrial isozyme, pH 7.5, 30°C
-
0.0013
ATP
-
ATP-diphosphate exchange assay, wild-type enzyme, pH 7.2, 30°C, in presence of tRNASer
0.051
L-Ser
-
mutant ScSerRSDELTAC13 (deletion of 13 C-terminal residues), using yeast tRNA
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
0.016
L-serine
-
wild type enzyme, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.0257
L-serine
-
mutant enzyme P395A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.049
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
0.18
L-serine
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.2491
L-serine
-
mutant enzyme G402A/G405A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.45
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
0.45 - 0.89
Ser
-
serine-dependent ATP-diphosphate exchange, mutant enzymes
0.00004
tRNASer
-
wild-type enzyme, mutant SerRS11, and mutant SerRS12, pH 7.2, 30°C
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
0.0008628
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
additional information
additional information
-
kinetics for the ATP-diphosphate exchange reaction
-
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 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
-
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
-
additional information
additional information
-
Km values for tRNASer transcripts
-
additional information
additional information
-
Lineweaver-Burk plots for Ser and tRNASer are non-linear
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.14
L-threonine
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.5
mitochondrial tRNASer from yeast subtype 2
-
mitochondrial isozyme, pH 7.5, 30°C
-
0.04 - 1.97
ATP
-
serine-dependent ATP-diphosphate exchange, mutant enzymes
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; mutant SerRS12, pH 7.2, 30°C
0.47
L-Ser
-
mutant ScSerRSDELTAC13 (deletion of 13 C-terminal residues), using yeast 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
0.38
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
1.06
L-serine
-
wild type enzyme, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
2.5
L-serine
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
6.9
L-serine
-
mitochondrial isozyme, ATP-diphosphate exchange reaction, pH 7.2, 30°C
0.052 - 2.1
Ser
-
serine-dependent ATP-diphosphate exchange, mutant enzymes
0.1
tRNASer
-
pH 7.5, 50°C, recombinant MtSerRS in presence of recombinant MtArgRS
0.54
tRNASer
-
mutant ScSerRSDELTAC13 (deletion of 13 C-terminal residues), using yeast tRNA
1.1
tRNASer
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
1.28
tRNASer
-
mutant ZmcSerRSDELTAC12 (deletion of 12 C-terminal residues), using maize tRNA
1.43
tRNASer
-
mutant ZmcSerRSDELTAC18 (deletion of 18 C-terminal residues), using maize tRNA
6.08
tRNASerUGA
-
native wild-type enzyme, pH 8.5, 37°C; 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
-
turnover numbers for different tRNASer variants
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.04
DL-Serine hydroxamate
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.0027
L-cysteine
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.006
L-threonine
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.016
L-serine
-
wild type enzyme, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.0257
L-serine
-
mutant enzyme P395A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.049
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
0.2491
L-serine
-
mutant enzyme G402A/G405A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.9
L-serine
-
mutant enzyme F397P/A399G, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
13.9
L-serine
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
1275
tRNASer
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.21
5'-O-[N-(L-Seryl)-sulfamoyl]adenosine
-
recombinant wild-type enzyme, pH 7.2, 30°C
0.28
5'-O-[N-(L-Seryl)-sulfamoyl]adenosine
-
recombinant mutant SerRS11, pH 7.2, 30°C
3.1
5'-O-[N-(L-Seryl)-sulfamoyl]adenosine
-
recombinant mutant SerRS12, pH 7.2, 30°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0238
(E)-3-(3-ethynyl-4-hydroxyphenyl)-1-(2-hydroxy-4-methoxy-3-(3-methylbut-2-en-1-yl)phenyl)prop-2-en-1-one
Staphylococcus aureus
-
in 100 mM HEPES (pH 7.2), 10 mM MgCl2, 30 mM KCl, at 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
wild-type and mutant tRNA substrates, relative activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.4
7.5
7.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
25°C, acylation rate increases when pH is raised from 6.0 to 8.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two isozymes through poylmorphism at position 197, L197S
UniProt
brenda
wild-type and truncated mutants with a deletion of the N-terminal arm of the enzyme: SerRSDELTA35-97 and SerRSDELTA56-72
-
-
brenda
contains two serS genes that encode two different types of SerRSs: a bacterial-type SerRS present in most organisms, and a highly divergent SerRS only found in some methanogenic archaea
-
-
brenda
-
-
-
brenda
overexpression, wild-type and mutant lacking the 60 base pairs encoding the C-terminal peptide
-
-
brenda
wild-type and mutants with mutagenesis of a portion of the SES1 gene encoding the motif 2 loop
-
-
brenda
a valanimycin producing organism, strain MG456-hF10, genes vlmL and svsR, the latter is a housekeeping gene, gene SerRS
Uniprot
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
; transcription levels are much higher in middle and posterior silk gland than in anterior silk gland
brenda
-
middle, high abundance in this organ may result from an adaption of this organ to the production of the serine-rich protein, sericin
brenda
additional information
tissue expression analysis of enzyme TyrRS, the transcription level of TyrRS is significantly higher in silk gland than in other tissues
brenda
additional information
-
tissue expression analysis of enzyme TyrRS, the transcription level of TyrRS is significantly higher in silk gland than in other tissues
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
dual localization is established by the virtue of an ambiguous targeting peptid at the very N-terminus
brenda
-
dual localization is established by the virtue of an ambiguous targeting peptid at the very N-terminus
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
impairment of zygotic Sars function leads to a significant dilatation of the aortic arch vessels and aberrant branching of cranial and intersegmental vessels
physiological function
additional information
evolution
-
as a consequence of an N-terminal insertion and a C-terminal extra-sequence, the binding mode of tRNASer to hsSerRS differs from that in prokaryotes
evolution
-
although SerRSs from methanogenic archaea recognize tRNAsSer from all three domains of life in vitro, the toxicity presumably precludes the complementation of endogenous SerRS function in both, Escherichia coli and Saccharomyces cerevisiae
evolution
-
although SerRSs from methanogenic archaea recognize tRNAsSer from all three domains of life in vitro, the toxicity presumably precludes the complementation of endogenous SerRS function in both, Escherichia coli and Saccharomyces cerevisiae
evolution
-
the enzyme belongs to the class II, subclass IIa, of aminoacyl-tRNA sythetases
evolution
SerRS belongs to the class II aminoacyl-tRNA synthetases (aaRSs), evolutionary analysis of SerRS and TyrRS, overview
evolution
-
the enzyme belongs to the class II, subclass IIa, of aminoacyl-tRNA sythetases
-
evolution
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
the enzyme belongs to the class II, subclass IIa, of aminoacyl-tRNA sythetases
-
physiological function
seryl-tRNA synthetase is involved in vascular development
physiological function
-
seryl-tRNA synthetase possesses an angiogenesis-regulating capacity
physiological function
-
seryl-tRNA synthetase possesses an angiogenesis-regulating capacity
physiological function
-
seryl-tRNA synthetase is an essential enzyme for translation, also regulating vascular development
physiological function
aminoacyl-tRNA synthetases (aaRSs) for glycine, alanine, serine and tyrosine play important roles in fibroin synthesis
additional information
-
expression of methanogenic-type SerRSs is toxic for Escherichia coli cells
additional information
-
expression of methanogenic-type SerRSs is toxic for Escherichia coli cells
additional information
-
the 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 within the active site bound with adenylate. Presence of bound Mg2+ ions around tRNA and dynamically slow bound water are other common features of the enzyme, dynamics of dimeric ttSerRS bound with adenylate and tttRNASer with a focus to the molecular process of the dynamic development of the catalytically competent active site organization essential for the second step, molecular dynamic simulations, overview
additional information
-
the 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 within the active site bound with adenylate. Presence of bound Mg2+ ions around tRNA and dynamically slow bound water are other common features of the enzyme, dynamics of dimeric ttSerRS bound with adenylate and tttRNASer with a focus to the molecular process of the dynamic development of the catalytically competent active site organization essential for the second step, molecular dynamic simulations, overview
-
additional information
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
the 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 within the active site bound with adenylate. Presence of bound Mg2+ ions around tRNA and dynamically slow bound water are other common features of the enzyme, dynamics of dimeric ttSerRS bound with adenylate and tttRNASer with a focus to the molecular process of the dynamic development of the catalytically competent active site organization essential for the second step, molecular dynamic simulations, overview
-
Show AA Sequence and Transmembrane Helices (25624 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Candida albicans (strain SC5314 / ATCC MYA-2876)
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Methanosarcina barkeri (strain Fusaro / DSM 804)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Methanosarcina barkeri (strain Fusaro / DSM 804)
Methanosarcina barkeri (strain Fusaro / DSM 804)
Methanosarcina barkeri (strain Fusaro / DSM 804)
Methanosarcina barkeri (strain Fusaro / DSM 804)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)