Information on EC 6.1.1.15 - proline-tRNA ligase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.1.1.15
-
RECOMMENDED NAME
GeneOntology No.
proline-tRNA ligase
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
Aminoacylation
esterification
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Aminoacyl-tRNA biosynthesis
-
-
proline metabolism
-
-
tRNA charging
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-
SYSTEMATIC NAME
IUBMB Comments
L-proline:tRNAPro ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9055-68-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Aeropyrum pernix DSM 11879
-
SwissProt
Manually annotated by BRENDA team
bacterial enzyme type
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Borrelia burgdorferi
archaeal enzyme type
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
strain 9723
-
-
Manually annotated by BRENDA team
synonym Giardia lamblia
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Methanothermobacter thermautotrophicum
MuLV, produced in murine cells
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
purified multisynthetase complex, the enzyme is a bifunctional glutamyl-/prolyl-tRNA synthetase
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
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Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 4-amino-L-proline + tRNAPro
?
show the reaction diagram
-
-
-
-
?
ATP + 4-difluoro-L-proline + tRNAPro
?
show the reaction diagram
-
-
-
-
?
ATP + 4-fluoro-L-proline + tRNAPro
?
show the reaction diagram
-
-
-
-
?
ATP + 4-hydroxy-L-proline + tRNAPro
?
show the reaction diagram
-
-
-
-
?
ATP + azetidine-2-carboxylic acid + tRNAPro
?
show the reaction diagram
-
-
-
-
?
ATP + beta-thia-L-proline + tRNAPro
?
show the reaction diagram
-
-
-
-
?
ATP + cis-4-hydroxyproline + tRNAPro
AMP + diphosphate + cis-4-hydroxyprolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + dehydro-L-proline + tRNAPro
?
show the reaction diagram
-
-
-
-
?
ATP + gamma-thia-L-proline + tRNAPro
?
show the reaction diagram
-
-
-
-
?
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
show the reaction diagram
ATP + L-cysteine + tRNA
AMP + diphosphate + L-cysteinyl-tRNA
show the reaction diagram
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
show the reaction diagram
Methanothermobacter thermautotrophicum
-
-
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram
ATP + L-cysteine + tRNAs
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
ATP + trans-4-hydroxyproline + tRNAPro
AMP + diphosphate + trans-4-hydroxyprolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram
-
two-step reaction
-
r
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(2-chloro-thiophene)-4-quinolinecarboxylic acid
2-(3,4-dichloro-phenyl)-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-5,7-dichloro-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-5-methyl-7-chloro-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6,8-dimethyl-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-(4-hydroxyphenyl)-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-(trifluoromethoxy)-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-alkenyl-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-amino-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-bromo-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-bromo-8-(trifluoromethyl)-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-chloro-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-chloro-8-hydroxymethyl-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-chloro-8-methyl-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-iodo-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-methyl-8-chloro-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-7-bromo-8-methyl-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-7-fluoro-8-methyl-4-quinolinecarboxylic acid
2-(4-methoxy-phenyl)-4-quinolinecarboxylic acid
2-(4-[trifluoromethyl]-phenyl)-4-quinolinecarboxylic acid
2-furyl-4-quinolinecarboxylic acid
2-naphthyl-4-quinolinecarboxylic acid
2-phenyl-4-quinolinecarboxylic acid
2-pyridyl-4-quinolinecarboxylic acid
2-Pyrrolidinone
-
-
3,4-Dehydroproline
3-pyrroline
3-Selenaproline
4-Methylene-DL-proline
-
weak
5'-O-(N-[prolyl]-sulphamoyl) adenosine
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
cis(exo)-3,4-Methano-L-proline
cis-3-Hydroxy-L-proline
cysteamine
-
inhibition of Cys-tRNAPro formation
cysteinyl-sulfamoyl-adenylate
Methanothermobacter thermautotrophicum
-
i.e. Cys-AMS, intermediate analogue, competitive inhibition
D-cysteine-DL-homocysteine
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inhibition of Cys-tRNAPro formation
DL-Proline amide
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-
febrifugine
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-
-
halofuginone
iodoacetamide
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more than 90% protection by 10 mM ATP or 10 mM ATP + 10 mM Pro
L-azetidine-2-carboxylic acid
L-cysteine
-
competitive inhibition of prolylation. A 40fold excess over L-proline concentration reduces the prolylation activity by 80%, no inhibition of mutant P100A
L-cysteine ethyl ester
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inhibition of Cys-tRNAPro formation
L-cysteine methyl ester
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inhibition of Cys-tRNAPro formation
L-proline
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competitive inhibition of cysteinylation. A 40fold excess over L-cysteine concentration reduces the cysteinylation activity by over 80%, no inhibition of mutant E103A
L-thiazolidine-4-carboxylic acid
N-acetyl-L-cysteine
-
inhibition of Cys-tRNAPro formation
N-ethylglycine
-
weak
N-Methyl-L-alanine
-
weak
N-methylglycine
p-chloromercuribenzoate
proline analogues
-
-
-
prolyl-sulfamoyl-adenylate
Methanothermobacter thermautotrophicum
-
i.e. Pro-AMS, intermediate analogue, competitive inhibition
Pyrrole
Pyrrolidine
tetrahydrofuran
Tetrahydrothiophen
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tRNA
-
stimulates l-cysteine activation 2-3fold
additional information
Methanothermobacter thermautotrophicum
-
a complex between ProRS and leucyl-tRNA synthetase, LeuRS, in Methanothermobacter thermautotrophicus enhances tRNAPro aminoacylation, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.28 - 2.2
3,4-dehydro-DL-proline
1.4
3-thiaproline
6.25 - 55
4-selenaproline
66
4-thiaproline
-
ATP-diphosphate exchange
0.049 - 0.6
ATP
2 - 7.1
cis(exo)-3,4-Methano-L-proline
53 - 55
cis-4-hydroxyproline
12.5
gamma-thiaproline
-
ATP-diphosphate exchange
79 - 1360
L-alanine
1.43 - 5.3
L-azetidine-2-carboxylic acid
0.01 - 0.26
L-cysteine
0.137 - 0.625
L-Pro
0.0046 - 50
L-proline
20 - 50
L-thiazolidine-4-carboxylic acid
-
ATP-diphosphate exchange
68
N-Methyl-L-alanine
-
ATP-diphosphate exchange
45 - 300
N-methylglycine
0.12 - 3.1
Pro
20
thiazolidine-4-carboxylic acid
-
ATP-diphosphate exchange
2 - 37
trans-4-hydroxyproline
-
pH 7.0, 37C, recombinant wild-type enzyme, amino acid activation
0.00003 - 14.14
tRNAPro
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.7 - 81
ATP
0.056 - 21
cis-4-hydroxyproline
0.11 - 3.52
L-alanine
0.003 - 0.8
L-cysteine
0.024 - 210
L-proline
15
trans-4-hydroxyproline
Escherichia coli
-
pH 7.0, 37C, recombinant wild-type enzyme, amino acid activation
0.0091 - 10.8
tRNAPro
additional information
additional information
Escherichia coli
-
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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0024 - 0.00513
L-alanine
10.7
L-cysteine
Methanococcus maripaludis
Q6LZD3
pH 7.0, 37C
74
0.17 - 12000
L-proline
19330
tRNAPro
Methanocaldococcus jannaschii
-
pH 7.0, 37C
2671
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000043 - 0.000088
5'-O-[N-(L-alanyl)-sulfamoyl]adenosine
-
ATP-diphosphate exchange reaction, pH 7.0, 37C, recombinant wild-type enzyme
0.000025
cysteinyl-sulfamoyl-adenylate
Methanothermobacter thermautotrophicum
-
versus L-proline, pH 7.5, 35C
0.00005
prolyl-sulfamoyl-adenylate
Methanothermobacter thermautotrophicum
-
versus L-proline, pH 7.5, 35C
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.101
-
-
0.615
-
enzyme form associated with glutamyl-tRNA synthetase
1.26
-
free enzyme form
1.655
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 7.8
7.6 - 7.9
-
ATP-diphosphate exchange
7.9 - 8.3
-
ATP-diphosphate exchange
8.4 - 8.7
-
ATP-diphosphate exchange
8.4 - 8.8
-
ATP-diphosphate exchange
8.8 - 9.2
-
ATP-diphosphate exchange
9 - 9.4
-
ATP-diphosphate exchange