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
tRNA charging
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proline metabolism
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Aminoacyl-tRNA biosynthesis
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
archaeal enzyme type
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Manually annotated by BRENDA team
bacterial enzyme type
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
archaeal enzyme type
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
archaeal enzyme type
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Giardia intestinalis WB / CC 30957
synonym Giardia lamblia
A8BR89
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
archaeal enzyme type
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-
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
MuLV, produced in murine cells
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Manually annotated by BRENDA team
gene proS
UniProt
Manually annotated by BRENDA team
gene proS
UniProt
Manually annotated by BRENDA team
archaeal enzyme type
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-
Manually annotated by BRENDA team
purified multisynthetase complex, the enzyme is a bifunctional glutamyl-/prolyl-tRNA synthetase
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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SwissProt
Manually annotated by BRENDA team
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
purified class IIa enzyme
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
adenosine 5'-(beta,gamma-imido)triphosphate + L-proline + tRNAPro
?
show the reaction diagram
ATP + 4-amino-L-proline + tRNAPro
?
show the reaction diagram
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-
-
-
?
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
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-
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?
ATP + cis-4-hydroxyproline + tRNAPro
AMP + diphosphate + cis-4-hydroxyprolyl-tRNAPro
show the reaction diagram
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-
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?
ATP + dehydro-L-proline + tRNAPro
?
show the reaction diagram
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-
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?
ATP + gamma-thia-L-proline + tRNAPro
?
show the reaction diagram
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-
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?
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
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-
-
?
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
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-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
show the reaction diagram
ATP + L-proline + L-tRNAAla
AMP + diphosphate + L-prolyl-tRNAAla
show the reaction diagram
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-
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?
ATP + L-proline + L-tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
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-
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?
ATP + L-proline + L-tRNAProAla
AMP + diphosphate + L-prolyl-tRNAProAla
show the reaction diagram
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-
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-
?
ATP + L-proline + tRNAGlu
AMP + diphosphate + L-prolylyl-tRNAGlu
show the reaction diagram
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
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-
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?
additional information
?
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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
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?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram
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two-step reaction
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r
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
show the reaction diagram
ATP + L-proline + tRNAGlu
AMP + diphosphate + L-prolylyl-tRNAGlu
show the reaction diagram
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
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2-[4-(4-fluorophenyl)-5-[[(4-fluorophenyl)carbamoyl]amino]-3-(trifluoromethyl)-1H-pyrazol-1-yl]acetamide
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3,4-Dehydroproline
3-(3,3-dimethylbutanamido)-N-[(naphthalen-1-yl)methyl]pyrazine-2-carboxamide
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3-pyrroline
3-Selenaproline
3-[(cyclohexanecarbonyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)pyrazine-2-carboxamide
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3-[4-(4-fluorophenyl)-5-[[(4-fluorophenyl)carbamoyl]amino]-1-methyl-1H-pyrazol-3-yl]propanamide
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4-(4-fluorophenyl)-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-amine
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4-(4-fluorophenyl)-5-[[(4-fluorophenyl)carbamoyl]amino]-1-methyl-1H-pyrazole-3-carboxamide
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4-Methylene-DL-proline
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weak
5'-O-(N-[prolyl]-sulphamoyl) adenosine
5'-O-[N-(L-alanyl)-sulfamoyl]adenosine
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a non-hydrolyzable adenylate analogue, a potent inhibitor of the ATP-diphosphate exchange reaction
5'-O-[N-(L-Prolyl)-sulfamoyl]adenosine
6-fluoro-febrifugine
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7-bromo-6-chloro-3-[3-[hydroxy-2-piperidinyl]-2-oxopropyl]-4-quinazolinone
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azetidine-2-carboxylic acid
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at 0.2 mM isozyme ProRS-Org is inhibited by 25%
cis(exo)-3,4-Methano-L-proline
cis-3-hydroxy-L-proline
cysteamine
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inhibition of Cys-tRNAPro formation
cysteinyl-sulfamoyl-adenylate
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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
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
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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-(2,4-difluorophenyl)-N'-[4-(4-fluorophenyl)-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]urea
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N-(3-fluorophenyl)-N'-[4-(4-fluorophenyl)-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]urea
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N-(4-fluorophenyl)-N'-[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]urea
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N-(4-fluorophenyl)-N'-[1-methyl-3-(trifluoromethyl)-4-[3-(trifluoromethyl)phenyl]-1H-pyrazol-5-yl]urea
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N-(4-fluorophenyl)-N'-[4-(4-fluorophenyl)-1-(2-hydroxyethyl)-3-(trifluoromethyl)-1H-pyrazol-5-yl]urea
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N-(4-fluorophenyl)-N'-[4-(4-fluorophenyl)-1-methyl-1H-pyrazol-5-yl]urea
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N-(4-fluorophenyl)-N'-[4-(4-fluorophenyl)-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]urea
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N-(4-fluorophenyl)-N'-[4-(4-fluorophenyl)-1-methyl-3-[2-(morpholin-4-yl)ethyl]-1H-pyrazol-5-yl]urea
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N-(4-fluorophenyl)-N'-[4-(4-fluorophenyl)-3-(2-hydroxyethyl)-1-methyl-1H-pyrazol-5-yl]urea
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N-(4-fluorophenyl)-N'-[4-(4-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazol-5-yl]urea
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N-(4-fluorophenyl)-N'-[4-[2-(2-hydroxyethyl)phenyl]-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]urea
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N-(4-fluorophenyl)-N'-[4-[2-(hydroxymethyl)phenyl]-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]urea
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N-(4-fluorophenyl)-N'-[4-[3-(2-hydroxyethyl)phenyl]-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]urea
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N-([3-[5-[[(4-fluorophenyl)carbamoyl]amino]-1-methyl-3-(trifluoromethyl)-1H-pyrazol-4-yl]phenyl]methyl)methanesulfonamide
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N-acetyl-L-cysteine
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inhibition of Cys-tRNAPro formation
N-Boc-halofuginone
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less than 20% inhibition at 1 mM
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N-ethylglycine
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weak
N-Methyl-L-alanine
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weak
N-methylglycine
N-[(4-chlorophenyl)methyl]-3-[(cyclohexanecarbonyl)amino]pyrazine-2-carboxamide
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N-[3-(2-cyanoethyl)-4-(4-fluorophenyl)-1-methyl-1H-pyrazol-5-yl]-N'-(4-fluorophenyl)urea
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N-[3-(cyanomethyl)-4-(4-fluorophenyl)-1-methyl-1H-pyrazol-5-yl]-N'-(4-fluorophenyl)urea
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N-[3-cyano-4-(4-fluorophenyl)-1-methyl-1H-pyrazol-5-yl]-N'-(4-fluorophenyl)urea
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N-[3-[2-(dimethylamino)ethyl]-4-(4-fluorophenyl)-1-methyl-1H-pyrazol-5-yl]-N'-(4-fluorophenyl)urea
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N-[4-(3,4-difluorophenyl)-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]-N'-(4-fluorophenyl)urea
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N-[4-(4-fluorophenyl)-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]-N'-(4-methoxyphenyl)urea
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N-[4-(4-fluorophenyl)-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]-N'-[2-(morpholin-4-yl)pyridin-4-yl]urea
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N-[4-bromo-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]-N'-(4-fluorophenyl)urea
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NH4Cl
p-chloromercuribenzoate
proline analogues
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prolyl-sulfamoyl-adenylate
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i.e. Pro-AMS, intermediate analogue, competitive inhibition
Pyrrole
Pyrrolidine
TCMDC-124506
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competitive inhibitor
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tetrahydrofebrifugine
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tetrahydrofuran
Tetrahydrothiophen
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tRNA
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stimulates l-cysteine activation 2-3fold
additional information
-
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
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pH 7.0, 37C, recombinant wild-type enzyme, amino acid activation
0.00003 - 14.14
tRNAPro
additional information
additional information
-