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Information on EC 6.1.1.15 - proline-tRNA ligase and Organism(s) Enterococcus faecalis and UniProt Accession Q831W7

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This record set is specific for:
Enterococcus faecalis
UNIPROT: Q831W7 not found.
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Word Map
The taxonomic range for the selected organisms is: Enterococcus faecalis
The enzyme appears in selected viruses and cellular organisms
Synonyms
prors, prolyl-trna synthetase, glutamyl-prolyl-trna synthetase, glutamyl-prolyl trna synthetase, gluprors, prolyl trna synthetase, prorstt, procysrs, bifunctional aminoacyl-trna synthetase, glutamyl-/prolyl-trna synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Prolyl-tRNA synthetase
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Global RNA synthesis factor
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-
-
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Pro-tRNA synthetase
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-
-
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Proline translase
-
-
-
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Proline--tRNA ligase
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-
-
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Prolyl RNA synthetase
-
-
-
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Prolyl-transfer ribonucleate synthetase
-
-
-
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Prolyl-transfer ribonucleic acid synthetase
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-
-
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Prolyl-transfer RNA synthetase
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-
-
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Prolyl-tRNA synthetase
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-
-
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ProRS
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
-
-
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Aminoacylation
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-proline:tRNAPro ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9055-68-9
-
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-proline + L-tRNAAla
AMP + diphosphate + L-prolyl-tRNAAla
show the reaction diagram
-
-
-
?
ATP + L-proline + L-tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + L-tRNAProAla
AMP + diphosphate + L-prolyl-tRNAProAla
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
additional information
?
-
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-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-O-(N-[prolyl]-sulphamoyl) adenosine
i.e. ProAMS, a nonhydrolyzable analogue of the prolyl-adenylate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G331A
the mutant shows 6.7fold increased activity compared to the wild type enzyme
G334A
the mutant shows 2.2fold increased activity compared to the wild type enzyme
H366A
the mutant shows 4.4fold increased activity compared to the wild type enzyme
I263A
the mutant shows 2.4fold increased activity compared to the wild type enzyme
I278A
the mutant shows 12.8fold increased activity compared to the wild type enzyme
I333A
the mutant shows 54.7fold increased activity compared to the wild type enzyme
K279A
the mutant shows 2006.3fold increased activity compared to the wild type enzyme
S280A
the mutant shows 2fold increased activity compared to the wild type enzyme
S332A
the mutant shows 1.1fold increased activity compared to the wild type enzyme
T257A
the mutant shows 1.1fold increased activity compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography and Ni-NTA agarose column chromatography
recombinant enzyme from Escherichia coli strain M15 by ammonium sulfate fractionation and anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)Star cells
expression of the enzyme in Escherichia coli strain M15
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Crepin, T.; Yaremchuk, A.; Tukalo, M.; Cusack, S.
Structures of two bacterial prolyl-tRNA synthetases with and without a cis-editing domain
Structure
14
1511-1525
2006
Enterococcus faecalis (Q831W7), Enterococcus faecalis, Rhodopseudomonas palustris (Q6N5P6), Rhodopseudomonas palustris
Manually annotated by BRENDA team
Boyarshin, K.S.; Priss, A.E.; Rayevskiy, A.V.; Ilchenko, M.M.; Dubey, I.Y.; Kriklivyi, I.A.; Yaremchuk, A.D.; Tukalo, M.A.
A new mechanism of post-transfer editing by aminoacyl-tRNA synthetases catalysis of hydrolytic reaction by bacterial-type prolyl-tRNA synthetase
J. Biomol. Struct. Dyn.
35
669-682
2017
Enterococcus faecalis (Q831W7), Enterococcus faecalis
Manually annotated by BRENDA team