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Information on EC 6.1.1.15 - proline-tRNA ligase and Organism(s) Thermus thermophilus and UniProt Accession Q5SM28

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Thermus thermophilus
UNIPROT: Q5SM28 not found.
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Word Map
The taxonomic range for the selected organisms is: Thermus thermophilus
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
Global RNA synthesis factor
Pro-tRNA synthetase
Proline translase
Proline--tRNA ligase
Prolyl RNA synthetase
Prolyl-transfer ribonucleate synthetase
Prolyl-transfer ribonucleic acid synthetase
Prolyl-transfer RNA synthetase
Prolyl-tRNA synthetase
ProRS
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
Aminoacylation
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-proline:tRNAPro ligase (AMP-forming)
-
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-cysteine + tRNA
AMP + diphosphate + L-cysteinyl-tRNA
show the reaction diagram
in later work it is shown that cysteine is attached to tRNA(Pro) and thus constitutes a misaminoacylation event and not a dual specificity
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Thermus thermophilus prolyl-tRNA synthetase exhibits a cysteinyl-tRNA synthetase activity although the organism also encodes a canonical cysteinyl-tRNA synthetase
-
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
L-cysteine
-
recombinant enzyme, pH 7.2, 60°C
0.15
L-proline
-
recombinant enzyme, pH 7.2, 60°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
L-cysteine
-
recombinant enzyme, pH 7.2, 60°C
35
L-proline
-
recombinant enzyme, pH 7.2, 60°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis
-
enzyme complexed with 2 different tRNAPro isoacceptors, 2 weeks, 32% saturated ammonium sulfate, X-ray diffraction structure determination at 2.8-3.1 A resolution, superior quality crystal are obtained within 5-6 months by slowly precipitation and growth, crystal packing analysis
-
native enzyme or enzyme complexed with L-proline, tRNAPro isoacceptors, ATP-Mn2+, prolyl-adenylate intermediate, or prolyl-adenylate analogue Pro-AMS, preparation by soaking of native enzyme crystals in ligand solutions, X-ray diffraction structure determination at 2.85-3.0 A resolution
-
purified free enzyme or complexed with 3 tRNAPro isoacceptors, precipitant is 32% ammonium sulfate at pH 7.5, X-ray diffraction structure determination at 3.5 A resolution, and analysis
-
X-ray diffraction structure determination at 2.43-2.85 A of crystals formed by the free enzyme or the enzyme complexed with tRNAPro
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from overexpression in Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yaremchuk, A.; Kriklivyi, I.; Cusack, S.; Tukalo, M.
Improved crystals of Thermus thermophilus prolyl-tRNA synthetase complexed with cognate tRNA obtained by crystallization from precipitate
Acta Crystallogr. Sect. D
56
197-199
2000
Thermus thermophilus
Manually annotated by BRENDA team
Yaremchuk, A.; Cusack, S.; Tukalo, M.
Crystal structure of a eukaryote/archaeon-like protyl-tRNA synthetase and its complex with tRNAPro(CGG)
EMBO J.
19
4745-4758
2000
Thermus thermophilus
Manually annotated by BRENDA team
Jacquin-Becker, C.; Ahel, I.; Ambrogelly, A.; Ruan, B.; Soll, D.; Stathopoulos, C.
Cysteinyl-tRNA formation and prolyl-tRNA synthetase
FEBS Lett.
514
34-36
2002
Thermus thermophilus, Giardia intestinalis, Methanocaldococcus jannaschii, Methanococcus maripaludis
Manually annotated by BRENDA team
Ahel, I.; Stathopoulos, C.; Ambrogelly, A.; Sauerwald, A.; Toogood, H.; Hartsch, T.; Soll, D.
Cysteine activation is an inherent in vitro property of prolyl-tRNA synthetases
J. Biol. Chem.
277
34743-34748
2002
Aquifex aeolicus, Borreliella burgdorferi, Saccharomyces cerevisiae, Acetoanaerobium sticklandii, Deinococcus radiodurans, Escherichia coli, Thermus thermophilus, Magnetospirillum magnetotacticum, Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Rhodopseudomonas palustris, Novosphingobium aromaticivorans, Cytophaga hutchinsonii
Manually annotated by BRENDA team
Yaremchuk, A.; Tukalo, M.; Grotli, M.; Cusack, S.
A succession of substrate induced conformational changes ensures the amino acid specificity of Thermus thermophilus prolyl-tRNA synthetase: comparison with histidyl-tRNA synthetase
J. Mol. Biol.
309
989-1002
2001
Thermus thermophilus
Manually annotated by BRENDA team
Cusack, S.; Yaremchuk, A.; Krikliviy, I.; Tukalo, M.
tRNAPro anticodon recognition by Thermus thermophilus prolyl-tRNA synthetase
Structure
6
101-108
1998
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Manually annotated by BRENDA team
Feng, L.; Stathopoulos, C.; Ahel, I.; Mitra, A.; Tumbula-Hansen, D., Hartsch, T.; Sll, D.
Aminoacyl-tRNA formation in the extreme thermophile Thermus thermophilus
Extremophiles
6
167-174
2002
Thermus thermophilus (Q5SM28), Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (Q5SM28)
Manually annotated by BRENDA team