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Information on EC 6.1.1.15 - proline-tRNA ligase and Organism(s) Escherichia coli and UniProt Accession P16659
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6.1.1.15 proline-tRNA ligaseSpecify your search results
Word Map
- 6.1.1.15
- synthetases
- aminoacylation
- halofuginone
-
ala-trnapro
-
anticodons
-
mischarged
-
aarss
-
misactivated
-
multisynthetase
-
misacylated
-
trans-editing
-
cys-trnapro
- trnacys
- thrrs
-
mistranslation
- thermautotrophicus
-
multi-trna
- glnrs
- leucyl-trna
- lysyl-trna
- leurs
- asprs
- febrifugine
-
post-transfer
-
transcript-selective
- drug development
- pharmacology
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
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, class ii prolyl-trna synthetase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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
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
-
-
-
-
Prolyl-tRNA synthetase
-
-
ProRS
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
bi uni ping pong mechanism
-
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
ATP is the first substrate to enter into the reaction sequence and prolyl-tRNA is the last product to dissociate from the enzyme
-
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
two-step reaction, Asp350 is involved in the pre-transfer editing of alanine
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
esterification
Aminoacylation
esterification
-
-
-
-
Aminoacylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-proline:tRNAPro ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY
9055-68-9
-
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-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
very low activity
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + cis-4-hydroxyproline + tRNAPro
AMP + diphosphate + cis-4-hydroxyprolyl-tRNAPro
-
-
-
-
?
ATP + trans-4-hydroxyproline + tRNAPro
AMP + diphosphate + trans-4-hydroxyprolyl-tRNAPro
-
-
-
-
?
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
-
enzyme possesses both pre- and post-transfer hydrolytic editing activity to prevent from misincorporation of alanine into proteins
-
?
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
-
the enzyme performs 1. misacetylation of tRNAPro, 2. hydrolysis of the misactivated Ala-AMP, i.e. pre-transfer editing, independent of tRNA, and 3. deacetylation of the mischarged Ala-tRNAPro, i.e. post-transfer editing
-
?
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
-
L-alanine is a poor substrate
-
-
?
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
-
mutant K279A, low activity
-
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
-
-
-
r
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
misacetylation, no editing of the misactivated Cys-tRNAPro
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
ir
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
r
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
4-hydroxy-L-proline can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
no deacetylation by the wild-type enzyme, but mutants H369C and H369A is able to deacetylate Pro-tRNAPro
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
editing mechanism, the aminoacylation active site plays a significant role in preserving the fidelity of translation by acting as a filter that selectively releases non-cognate adenylates into solution, while protecting the cognate adenylate from hydrolysis, overview, scheme showing proposed pre-transfer and posttransfer editing pathways, overview
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
the enzyme recognizes specific bases of tRNAPro in both the anticodon domain, which mediate initial complex formation, and in the acceptor stem, which is proximal to the site of catalysis, analysis of the molecular interaction between ProRS and the acceptor stem of cognate tRNAPro interaction involves the critical residue R144 in the active site and G72 in the acceptor stem, aminoacylation of G72A-tRNAPro is reduced 170fold compared to wild-type tRNAPro when assayed with wild-type ProRS, whereas only a 2.6fold decrease is observed with mutant R144K ProRS, activity of wild-type and mutant enzymes with wild-type and mutant tRNAs, overview
-
-
?
additional information
?
-
-
3-thiaproline, 4-thiaproline and 4-selenaproline can replace proline in the ATP-diphosphate exchange. 4-Thiaproline and 4-selenaproline show a much higher Km
-
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction, no activity with L-cysteine
-
?
additional information
?
-
-
determination of Pro-AMP and Ala-AMP hydrolysis activities of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
no activity with 3,4-phenyl-L-proline and pipecolic acid
-
-
?
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-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,4-Dehydroproline
-
competitive inhibition of proline transfer to tRNA, no inhibition of proline-dependent ATP-diphosphate exchange
5'-O-[N-(L-alanyl)-sulfamoyl]adenosine
-
a non-hydrolyzable adenylate analogue, a potent inhibitor of the ATP-diphosphate exchange reaction
5'-O-[N-(L-Prolyl)-sulfamoyl]adenosine
-
a non-hydrolyzable adenylate analogue
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2 - 37
trans-4-hydroxyproline
-
pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation
additional information
additional information
-
wild-type and mutant enzyme kinetics
-
53
cis-4-hydroxyproline
-
pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation
55
cis-4-hydroxyproline
-
pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation
140
L-alanine
-
pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation
0.18
L-proline
-
wild type enzyme, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
0.22
L-proline
-
mutant enzyme H302A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
0.25
L-proline
-
pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation
0.3
L-proline
-
mutant enzyme G412A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
0.33
L-proline
-
mutant enzyme D198A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
0.45
L-proline
-
mutant enzyme N305A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
0.62
L-proline
-
mutant enzyme H302A/G412A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
0.76
L-proline
-
mutant enzyme F415A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
1.03
L-proline
-
mutant enzyme E234A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
3.4
L-proline
-
mutant enzyme E218A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
50
L-proline
-
pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation
0.000131
tRNAPro
-
pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, aminoacylation
0.01414
tRNAPro
-
pH 7.0, 37°C, recombinant wild-type enzyme, aminoacylation
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15
trans-4-hydroxyproline
-
pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation
additional information
additional information
-
the rate of AMP formation of K279A ProRS in the presence of alanine is 0.034 s-1, which is at least 20 times faster than the rate of nonenzymatic hydrolysis
-
0.056
cis-4-hydroxyproline
-
pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation
21
cis-4-hydroxyproline
-
pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation
1.7
L-alanine
-
pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation
0.131
L-proline
-
mutant enzyme F415A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
0.61
L-proline
-
mutant enzyme N305A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
4.4
L-proline
-
mutant enzyme E218A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
6.7
L-proline
-
mutant enzyme E234A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
6.98
L-proline
-
mutant enzyme D198A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
7.3
L-proline
-
mutant enzyme H302A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
10.7
L-proline
-
mutant enzyme H302A/G412A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
12
L-proline
-
pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation
12.6
L-proline
-
wild type enzyme, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
12.8
L-proline
-
mutant enzyme G412A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
70
L-proline
-
pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation
0.0091
tRNAPro
-
pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, aminoacylation
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.17
L-proline
-
mutant enzyme F415A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
1.3
L-proline
-
mutant enzyme E218A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
1.4
L-proline
-
mutant enzyme N305A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
6.5
L-proline
-
mutant enzyme E234A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
17
L-proline
-
mutant enzyme H302A/G412A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
21
L-proline
-
mutant enzyme D198A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
33
L-proline
-
mutant enzyme H302A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
43
L-proline
-
mutant enzyme G412A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
71
L-proline
-
wild type enzyme, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000043 - 0.000088
5'-O-[N-(L-alanyl)-sulfamoyl]adenosine
-
ATP-diphosphate exchange reaction, pH 7.0, 37°C, recombinant wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
activities of wild-type and mutant enzymes, pre-transfer editing activity, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E218A
the mutant activates proline but with a decreased kcat (3fold) and elevated KM value (15fold). Overall proline activation efficiency of this mutant is decreased 45fold compared to the wild type enzyme. The mutant also can charge L-proline onto tRNAPro, albeit with 3fold reduced efficiency
G217A
the kcat/KM of the mutant is reduced 7fold relative to the wild type enzyme. In contrast, alanine activation by the G217A mutant is not affected compared to the wild type enzyme. A 2fold decrease in alanine activation s observed for the mutant compared to the wild type enzyme. The mutant also can charge L-proline onto tRNAPro, albeit with 3fold reduced efficiency
C443A
-
mutagenesis of C443 to amino acids Ala, Gly and Ser results in significant decreases, 16fold to 225fold in kcat/KmPro, as measured by the ATP-diphosphate exchange assay. The Ala and Gly mutations have relatively small effect, 4fold to 7fold, on the overall aminoacylation reaction, while the activity of the C443 mutant in this same assay is substantially reduced, 80fold
C443G
-
mutagenesis of C443 to amino acids Ala, Gly and Ser results in significant decreases, 16fold to 225fold in kcat/KmPro, as measured by the ATP-diphosphate exchange assay. The Ala and Gly mutations have relatively small effect, 4fold to 7fold, on the overall aminoacylation reaction, while the activity of the C443 mutant in this same assay is substantially reduced, 80fold
C443S
-
mutagenesis of C443 to amino acids Ala, Gly and Ser results in significant decreases, 16fold to 225fold in kcat/KmPro, as measured by the ATP-diphosphate exchange assay. The Ala and Gly mutations have relatively small effect, 4fold to 7fold, on the overall aminoacylation reaction, while the activity of the C443 mutant in this same assay is substantially reduced, 80fold
D198A
-
the overall aminoacylation activity of the mutant is reduced 5.5fold
D350A
-
site-directed mutagenesis, subdomain III mutant, residual remaining aminoaclyation activity, no pre-transfer editing activity
D378A
-
site-directed mutagenesis, subdomain III mutant, reduced aminoaclyation and pre-transfer editing activity
D386A
-
site-directed mutagenesis, subdomain III mutant, reduced aminoaclyation and pre-transfer editing activity
D394A
-
site-directed mutagenesis, subdomain III mutant, reduced aminoaclyation and pre-transfer editing activity
E303A
-
the mutation results in 3fold decrease in L-proline activation. The mutant exhibits a small decrease in the aminoacylation efficiency
E303D
-
the mutation results in 3.1fold decrease in L-proline activation. The mutant exhibits a small decrease in the aminoacylation efficiency
E303K
-
the mutation results in 4.2fold decrease in L-proline activation. The mutant exhibits a small decrease in the aminoacylation efficiency
F415A
-
the aminoacylation activity of the mutant is nearly abolished with rates 70fold slower than the wild type
H302A/G412A
-
the overall aminoacylation activity of the mutant is reduced 5.5fold
H369A
-
site-directed mutagenesis, subdomain III mutant, highly reduced reduced aminoaclyation and pre-transfer editing activity, deacetylates Pro-tRNAPro
H369C
-
site-directed mutagenesis, subdomain III mutant, highly reduced reduced aminoaclyation and pre-transfer editing activity, deacetylates Pro-tRNAPro
K279A
K279E
-
the mutation results in 2.7fold reduced L-proline activation. The mutant exhibits wild type aminoacylation efficiency
K279E/E303K
-
the mutant shows 2.3fold reduced L-proline activation. The mutant exhibits wild type aminoacylation efficiency
L266A
-
the mutant shows negligible in L-alanine deacylation at room temperature
N305A
-
the aminoacylation activity of the mutant is nearly abolished with rates 70fold slower than the wild type
R144K
-
site-directed mutagenesis, the mutant shows 480fold reduced activity compared to the wild-type enzyme
R144L
-
site-directed mutagenesis, the mutant shows 870fold reduced activity compared to the wild-type enzyme
R146C
-
site-directed mutagenesis, the mutant shows 79fold reduced activity compared to the wild-type enzyme
T257A
-
site-directed mutagenesis, subdomain I mutant, reduced aminoaclyation and pre-transfer editing activity
V143C
-
site-directed mutagenesis, the mutant shows 3fold reduced activity compared to the wild-type enzyme
additional information
-
replacement of 163 residues of the INS domain, amino acids 232-394, with either an 8-residue Gly6Ser2 linker or a 16-residue Gly12Ser4 linker by PCR amplification of the full-length plasmid pCS-M1S
K279A
-
site-directed mutagenesis, subdomain II mutant, reduced aminoaclyation and pre-transfer editing activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
-
enzyme is a target for design of antibiotics targeting the editing active site since eukaryotic enzyme types are not able to edit misactivated alanine on tRNAPro
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heacock, D.; Forsyth, C.J.; Shiba, K.; Musier-Forsyth, K.
Synthesis and aminoacyl-tRNA synthetase inhibitory activity of prolyl adenylate analogs
Bioorg. Chem.
24
273-289
1996
Escherichia coli
-
Stehlin, C.; Heacock, D.H.; Liu, H.; Musier-Forsyth, K.
Chemical modification and site-directed mutagenesis of the single cysteine in motif 3 of class II Escherichia coli prolyl-tRNA synthetase
Biochemistry
36
2932-2938
1997
Escherichia coli
Busiello, V.; Di Girolamo, M.; Cini, C.; De Marco, C.
beta-Selenaproline as competitive inhibitor of proline activation
Biochim. Biophys. Acta
606
347-352
1980
Escherichia coli, Rattus norvegicus
Jeannin, G.; Burkard, G.; Weil, J.H.
Aminoacylation of Phaseolus vulgaris cytoplasmic, chloroplastic and mitochondrial tRNAsPro and tRNAsLys by homologous and heterologous enzymes
Biochim. Biophys. Acta
442
24-31
1976
Escherichia coli, Phaseolus vulgaris
Papas, T.S.; Mehler, A.H.
Kinetic studies of the prolyl transfer ribonucleic acid synthetase of Escherichia coli. Order of addition of substrates and release of products
J. Biol. Chem.
246
5924-5928
1971
Escherichia coli
Norton, S.J.
Purification and properties of the prolyl RNA synthetase of Escherichia coli
Arch. Biochem. Biophys.
106
147-152
1964
Escherichia coli, Escherichia coli 9723
Wong, F.C.; Beuning, P.J.; Nagan, M.; Shiba, K.; Musier-Forsyth, K.
Functional role of the prokaryotic proline-tRNA synthetase insertion domain in amino acid editing
Biochemistry
41
7108-7115
2002
Escherichia coli
Beuning, P.J.; Musier-Forsyth, K.
Species-specific differences in amino acid editing by class II prolyl-tRNA synthetase
J. Biol. Chem.
276
30779-30785
2001
Escherichia coli, Homo sapiens, Methanocaldococcus jannaschii
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
Hati, S.; Ziervogel, B.; Sternjohn, J.; Wong, F.C.; Nagan, M.C.; Rosen, A.E.; Siliciano, P.G.; Chihade, J.W.; Musier-Forsyth, K.
Pre-transfer editing by class II prolyl-tRNA synthetase: role of aminoacylation active site in 'selective release' of noncognate amino acids
J. Biol. Chem.
281
27862-27872
2006
Saccharomyces cerevisiae, Escherichia coli, Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Methanococcus maripaludis
Burke, B.; An, S.; Musier-Forsyth, K.
Functional guanine-arginine interaction between tRNAPro and prolyl-tRNA synthetase that couples binding and catalysis
Biochim. Biophys. Acta
1784
1222-1225
2008
Escherichia coli
Splan, K.E.; Ignatov, M.E.; Musier-Forsyth, K.
Transfer RNA modulates the editing mechanism used by class II prolyl-tRNA synthetase
J. Biol. Chem.
283
7128-7134
2008
Escherichia coli, Homo sapiens, Methanocaldococcus jannaschii
Sanford, B.; Cao, B.; Johnson, J.M.; Zimmerman, K.; Strom, A.M.; Mueller, R.M.; Bhattacharyya, S.; Musier-Forsyth, K.; Hati, S.
Role of coupled dynamics in the catalytic activity of prokaryotic-like prolyl-tRNA synthetases
Biochemistry
51
2146-2156
2012
Escherichia coli (P16659), Escherichia coli
Johnson, J.M.; Sanford, B.L.; Strom, A.M.; Tadayon, S.N.; Lehman, B.P.; Zirbes, A.M.; Bhattacharyya, S.; Musier-Forsyth, K.; Hati, S.
Multiple pathways promote dynamical coupling between catalytic domains in Escherichia coli prolyl-tRNA synthetase
Biochemistry
52
4399-4412
2013
Escherichia coli
Bartholow, T.G.; Sanford, B.L.; Cao, B.; Schmit, H.L.; Johnson, J.M.; Meitzner, J.; Bhattacharyya, S.; Musier-Forsyth, K.; Hati, S.
Strictly conserved lysine of prolyl-tRNA synthetase editing domain facilitates binding and positioning of misacylated tRNAPro
Biochemistry
53
1059-1068
2014
Escherichia coli
Kumar, S.; Das, M.; Hadad, C.M.; Musier-Forsyth, K.
Substrate specificity of bacterial prolyl-tRNA synthetase editing domain is controlled by a tunable hydrophobic pocket
J. Biol. Chem.
287
3175-3184
2012
Escherichia coli
Saravanan Prabhu, N.; Ayyadurai, N.; Deepankumar, K.; Chung, T.; Lim, D.; Yun, H.
Reassignment of sense codons: Designing and docking of proline analogs for Escherichia coli prolyl-tRNA synthetase to expand the genetic code
J. Mol. Catal. B
78
57-64
2012
Escherichia coli
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