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Information on EC 6.1.1.11 - serine-tRNA ligase and Organism(s) Staphylococcus aureus and UniProt Accession P95689

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EC Tree
IUBMB 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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This record set is specific for:
Staphylococcus aureus
UNIPROT: P95689
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Word Map
The taxonomic range for the selected organisms is: Staphylococcus aureus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62 kDa RNA-binding protein
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Serine transfer RNA synthetase
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Serine translase
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Serine--tRNA ligase
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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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Synthetase, seryl-transfer ribonucleate
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62 kDa RNA-binding protein
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-
-
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Serine transfer RNA synthetase
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-
-
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Serine translase
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-
-
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Serine--tRNA ligase
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-
-
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SerRS
-
-
-
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SerRSmt
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-
-
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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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-
-
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Seryl-transfer RNA synthetase
-
-
-
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Seryl-tRNA synthetase
Synthetase, seryl-transfer ribonucleate
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
-
-
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Aminoacylation
-
-
-
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PATHWAY SOURCE
PATHWAYS
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
L-serine:tRNASer ligase (AMP-forming)
This enzyme also recognizes tRNASec, the special tRNA for selenocysteine, and catalyses the formation of L-seryl-tRNASec, the substrate for EC 2.9.1.1, L-seryl-tRNASec selenium transferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-48-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
show the reaction diagram
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
show the reaction diagram
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
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4-hydroxyderricin
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-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
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in 100 mM HEPES (pH 7.2), 10 mM MgCl2, 30 mM KCl, at 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
class II enzyme
SwissProt
Manually annotated by BRENDA team
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bausch, N.; Seignovert, L.; Beaulande, M.; Leberman, R.; Hartlein, M.
Analysis and overexpression in Escherichia coli of a staphylococcal gene encoding seryl-tRNA synthetase
Biochim. Biophys. Acta
1397
169-174
1998
Staphylococcus aureus (P95689), Staphylococcus aureus
Manually annotated by BRENDA team
Battenberg, O.A.; Yang, Y.; Verhelst, S.H.; Sieber, S.A.
Target profiling of 4-hydroxyderricin in S. aureus reveals seryl-tRNA synthetase binding and inhibition by covalent modification
Mol. Biosyst.
9
343-351
2013
Staphylococcus aureus, Staphylococcus aureus NCTC 8325
Manually annotated by BRENDA team