Any feedback?
Information on EC 6.1.1.11 - serine-tRNA ligase and Organism(s) Homo sapiens and UniProt Accession Q9NP81
for references in articles please use BRENDA:EC6.1.1.11Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Word Map
- 6.1.1.11
-
raman
-
surface-enhanced
- nanoparticles
- silver
- aminoacyl-trna
- aminoacylation
-
serylation
-
colloid
- selenocysteine
-
anticodon
- trnasec
- asprs
-
isoacceptors
-
aarss
- lysyl-trna
-
roughened
- phenylalanyl-trna
- trnatyr
-
langmuir-blodgett
- alanyl-trna
-
handheld
- albomycins
-
citrate-reduced
- molecular biology
-
nanostars
- selenophosphate
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
serrs, seryl-trna synthetase, seryl trna synthetase, mtserrs, serrs2, mmbserrs, seryl-trna-synthetase, serzmo, serrs1, methanogenic serrs, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
62 kDa RNA-binding protein
SARS
Serine transfer RNA synthetase
Serine translase
Serine--tRNA ligase
SerRS
SerRSmt
SERSEC
Seryl-transfer ribonucleate synthetase
Seryl-transfer ribonucleic acid synthetase
Seryl-transfer RNA synthetase
Seryl-tRNA synthetase
Synthetase, seryl-transfer ribonucleate
62 kDa RNA-binding protein
-
-
-
-
Serine transfer RNA synthetase
-
-
-
-
Serine translase
-
-
-
-
Serine--tRNA ligase
-
-
-
-
SerRS
-
-
-
-
SerRSmt
-
-
-
-
SERSEC
-
-
-
-
Seryl-transfer ribonucleate synthetase
-
-
-
-
Seryl-transfer ribonucleic acid synthetase
-
-
-
-
Seryl-transfer RNA synthetase
-
-
-
-
Seryl-tRNA synthetase
-
-
-
-
Synthetase, seryl-transfer ribonucleate
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
esterification
Aminoacylation
esterification
-
-
-
-
Aminoacylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
L-serine:tRNASer ligase (AMP-forming)
This enzyme also recognizes tRNASec, the special tRNA for selenocysteine, and catalyses the formation of L-seryl-tRNASec, the substrate for EC 2.9.1.1, L-seryl-tRNASec selenium transferase.
CAS REGISTRY NUMBER
COMMENTARY
9023-48-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-serine + tRNASer
AMP + 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 + 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
-
?
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 + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00013
tRNASer
mutant enzyme DELTAG75-N97/DELTAG254-N261, at pH 7.5 and 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
tRNASer
mutant enzyme DELTAG75-N97/DELTAG254-N261, at pH 7.5 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
wild-type and mutant tRNA substrates, relative activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SYSM_HUMAN
518
0
58283
Swiss-Prot
Mitochondrion (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with 5'-O-(N-(L-seryl)-sulfamoyl)adenosine, sitting drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.2 M ammonium fluoride or ammonium formate, and 0.1 M HEPES pH 7.0
mutant enzymes E447K and E156T/R157S, sitting drop vapor diffusion method, using 12% (w/v) PEG 3350, 0.2 M NaCl and 0.1 MTris-HCl (pH 7.5)
purified hsSerRS, sitting-drop vapour diffusion method, 0.01875 ml of protein solution containing 10 mg/ml protein in HCl, pH 7.9, 100 mM NaCl, 10 mM MgCl2, 5% glycerol, 5 mM DTT, with 0.00625 ml of reservoir solution containing 100 mM ammonium sulfate, 22% w/v PEG 3350, 5% glycerol, 200 mM sodium formate pH 7.2, supplemented with 20% v/v glycerol, and equilibration against 0.5 ml of reservoir solution, 12°C, 2 weeks, X-ray diffraction structure determination and analysis at 3.1 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
E447K
the mutant shows increased activity compared to the wild type enzyme
P30G31Y
the mutation of the P30G31 dipeptide to a single tyrosine almost eliminates serylation activity
additional information
-
deletion of any but the anticodon domain of tRNASer and tRNASec causes a dramatic loss of serine acceptance
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, Q-HP column chromatography, and Superdex 200 gel filtration
Ni-NTA column chromatography, Resource Q column chromatography, and Superdex 200 gel filtration
Ni2+-affinity column chromatography, Resource-Q column chromatography, and Superdex 200 gel filtration
recombinant His-tagged hsSerRS from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, chromosomal localization at 19q13.1
expressed in Escherichia coli BL21(DE3) cells
hsSerRS DNA and amino acid sequence determination, analysis, and comparisons, expression as His-tagged enzyme in Escherichia coli coli BL21 (DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heckl, M.; Busch, K.; Gross, H.J.
Minimal tRNASer and tRNASec substrates for human seryl-tRNA synthetase: contribution of tRNA domains to serylation and tertiary structure
FEBS Lett.
427
315-319
1998
Homo sapiens
Yokogawa, T.; Shimada, N.; Takeuchi, N.; Benkowski, L.; Suzuki, T.; Omori, A.; Ueda, T.; Nishikawa, K.; Spremulli, L.L.; Watanabe, K.
Characterization and tRNA recognition of mammalian mitochondrial seryl-tRNA synthetase
J. Biol. Chem.
275
19913-19920
2000
Mus musculus (Q9JJL8), Mus musculus, Bos taurus (Q9N0F3), Bos taurus, Homo sapiens (Q9NP81), Homo sapiens
Herzog, W.; Mueller, K.; Huisken, J.; Stainier, D.Y.
Genetic evidence for a noncanonical function of seryl-tRNA synthetase in vascular development
Circ. Res.
104
1260-1266
2009
Danio rerio, Homo sapiens
Kawahara, A.; Stainier, D.Y.
Noncanonical activity of seryl-transfer RNA synthetase and vascular development
Trends Cardiovasc. Med.
19
179-182
2009
Danio rerio, Homo sapiens
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
66
1521-1524
2010
Homo sapiens
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
21
2078-2086
2013
Homo sapiens (P49591), Homo sapiens
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?
J. Biomark.
2014
362164
2014
Homo sapiens
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.
43
10534-10545
2015
Homo sapiens (P49591), Homo sapiens
EXTERNAL LINKS (specific for EC-Number 6.1.1.11)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
