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
6.1.1.15
-
RECOMMENDED NAME
GeneOntology No.
proline-tRNA ligase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
bi uni ping pong mechanism, 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
show the reaction diagram
dual substrate specificity
-
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
enzyme with dual substrate specificty which utilizes L-proline and L-cysteine as substrates, discriminating mechanism
-
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
induced fit substrate recognition, reaction mechanism, proline binding site structure
-
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
substrate binding mechanism, the two bases G35 and G36 are sufficient to uniquely identify the cognate tRNAPro
-
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
the C-terminal extremity folds back into the active site
-
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
two-step reaction, Asp350 is involved in the pre-transfer editing of alanine
-
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
one tRNA binds per dimeric enzyme, only 50% of active sites are active
-
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
class II synthetases are limited by a step prior to aminoacyl transfer
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Aminoacylation
-
-
-
-
Aminoacylation
-
-
Aminoacylation
-
-
Aminoacylation
-
-
Aminoacylation
-
-
Aminoacylation
-
-
Aminoacylation
-
-
Aminoacylation
-
-
Aminoacylation
-
-
Aminoacylation
-
-
Aminoacylation
-
-
esterification
-
-
-
-
esterification
-
-
esterification
-
-
esterification
-
-
esterification
-
-
esterification
-
-
esterification
-
-
esterification
-
-
esterification
-
-
esterification
-
-
esterification
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Aminoacyl-tRNA biosynthesis
-
-
proline metabolism
-
-
tRNA charging
-
-
SYSTEMATIC NAME
IUBMB Comments
L-proline:tRNAPro ligase (AMP-forming)
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
class II prolyl-tRNA synthetase
-
-
class II prolyl-tRNA synthetase
-
-
class II prolyl-tRNA synthetase
-
-
class II ProRS
-
-
dual-specificity prolyl-cysteinyl-tRNA synthetase
Q9GQI4
misleading
dual-specificity prolyl-tRNA synthetase
Q6LZD3
misleading
EPRS
-
-
Global RNA synthesis factor
-
-
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
glutamyl-/prolyl-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
ProCysRS
Q9GQI4
-
ProCysRS
Q58635
misleading
ProCysRS
Q58635
misleading
-
ProCysRS
Q6LZD3
-
Proline translase
-
-
-
-
Proline translase
-
-
Proline translase
-
-
Proline translase
-
-
Proline translase
-
-
Proline translase
-
-
Proline translase
-
-
Proline translase
-
-
Proline translase
-
-
Proline translase
-
-
Proline--tRNA ligase
-
-
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
proline/cysteine-tRNA ligase
Q58635
misleading
proline/cysteine-tRNA ligase
Q58635
misleading
-
Prolyl RNA synthetase
-
-
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
prolyl tRNA synthetase
-
-
prolyl-cysteinyl-tRNA synthetase
Q58635
misleading
prolyl-cysteinyl-tRNA synthetase
Q58635
misleading
-
Prolyl-transfer ribonucleate synthetase
-
-
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
Q831W7
-
Prolyl-tRNA synthetase
P16659
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
A8BR89
-
Prolyl-tRNA synthetase
Giardia intestinalis WB
A8BR89
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
P07814
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
Q58635
-
Prolyl-tRNA synthetase
Q58635
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
Q6N5P6
-
Prolyl-tRNA synthetase
-
-
ProRS
-
-
-
-
ProRS
Q9Y9G0
-
ProRS
Aeropyrum pernix DSM 11879
Q9Y9G0
-
-
ProRS
Q831W7
-
ProRS
P16659
-
ProRS
A8BR89
-
ProRS
Giardia intestinalis WB
A8BR89
-
-
ProRS
Q5SM28
-
PRS
P07814
-
glutamyl-prolyl tRNA synthetase
-
-
additional information
-
cf. EC 6.1.1.17
CAS REGISTRY NUMBER
COMMENTARY
9055-68-9
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain K1
-
-
Manually annotated by BRENDA team
Aeropyrum pernix DSM 11879
-
SwissProt
Manually annotated by BRENDA team
bacterial enzyme type
-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
bacterial enzyme type
-
-
Manually annotated by BRENDA team
class II enzyme, purified recombinant wild-type and mutant enzymes
-
-
Manually annotated by BRENDA team
strain 9723
-
-
Manually annotated by BRENDA team
wild-type enzyme and mutant enzymes C443A, C443G, and C443S
-
-
Manually annotated by BRENDA team
Escherichia coli 9723
strain 9723
-
-
Manually annotated by BRENDA team
enzyme with dual substrate specificity
-
-
Manually annotated by BRENDA team
synonym Giardia lamblia
UniProt
Manually annotated by BRENDA team
Giardia intestinalis WB
synonym Giardia lamblia
UniProt
Manually annotated by BRENDA team
isoform glutamyl-prolyl-tRNA synthetase
-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
enzyme with dual substrate specificity
-
-
Manually annotated by BRENDA team
enzyme with dual substrate specificity
-
-
Manually annotated by BRENDA team
MuLV, produced in murine cells
-
-
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
bacterial enzyme type
-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
class IIa synthetase of the eukaryote/archaeon-like structure type
-
-
Manually annotated by BRENDA team
enzyme with dual substrate specificity
-
-
Manually annotated by BRENDA team
strain HB8, purified class IIa enzyme
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
show the reaction diagram
-
-
-
-
r
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
show the reaction diagram
-
very low activity
-
?
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
show the reaction diagram
P16659
very low activity
-
-
?
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
show the reaction diagram
-
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
show the reaction diagram
-
misacetylation of tRNAPro, no editing
-
?
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
show the reaction diagram
-
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
show the reaction diagram
-
L-alanine is a poor substrate
-
-
?
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
show the reaction diagram
-
mutant K279A, low activity
-
-
?
ATP + L-cysteine + tRNA
AMP + diphosphate + L-cysteinyl-tRNA
show the reaction diagram
Q58635
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-cysteine + tRNA
AMP + diphosphate + L-cysteinyl-tRNA
show the reaction diagram
Q6LZD3
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-cysteine + tRNA
AMP + diphosphate + L-cysteinyl-tRNA
show the reaction diagram
Q5SM28
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-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. Addition of tRNA has a small threefold stimulatory effect on cysteine activation. The lack of a major role of tRNA in activation of cysteine suggests that the dual specificity enzyme must distinguish cysteine from proline directly, without the assistance of each cognate tRNA, to achieve the necessary specificity required for protein synthesis
-
-
?
ATP + L-cysteine + tRNA
AMP + diphosphate + L-cysteinyl-tRNA
show the reaction diagram
Q58635
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-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. Addition of tRNA has a small threefold stimulatory effect on cysteine activation. The lack of a major role of tRNA in activation of cysteine suggests that the dual specificity enzyme must distinguish cysteine from proline directly, without the assistance of each cognate tRNA, to achieve the necessary specificity required for protein synthesis
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
show the reaction diagram
-
-
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram
-
-
-
-
r
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram
-
two-step reaction
-
r
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram
-
dual-specificity enzyme
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram
-
dual-specificity enzyme, enzyme contains a discrete cysteine binding pocket
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram
-
misacetylation of tRNAPro, no editing
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram
-
two-step reaction, both steps are dependent on tRNACys
-
r
ATP + L-cysteine + tRNAs
AMP + diphosphate + L-cysteinyl-tRNA
show the reaction diagram
Q9GQI4
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 + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
ir
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
r
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
r
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Q831W7
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Q6N5P6
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Q58635
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Q6LZD3
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Q9GQI4
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
P16659
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
P07814
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
A8BR89
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
the chloroplastic-specific tRNAPro is not recognized by the cytoplasmic enzyme but can be charged by organellar or E. coli enzyme
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
N-methylglycine can replace proline in ATP-diphosphate exchange
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
L-azetidine-2-carboxylic acid can replace proline in ATP-diphosphate exchange (not)
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
L-azetidine-2-carboxylic acid can replace proline in ATP-diphosphate exchange (not)
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
L-azetidine-2-carboxylic acid can replace proline in ATP-diphosphate exchange (not)
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
L-azetidine-2-carboxylic acid can replace proline in ATP-diphosphate exchange (not)
-
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
L-azetidine-2-carboxylic acid can replace proline in ATP-diphosphate exchange (not)
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
4-hydroxy-L-proline can replace proline in ATP-diphosphate exchange
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
cis(exo)-3,4-methano-L-proline can replace proline on ATP-diphosphate exchange
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
the two tRNAsPro in the cytoplasm can be charged by the cytoplasmic enzyme, but not by the organellar enzyme or the E. coli enzyme
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
mitochondria-specific tRNAPro is not recognized by the cytoplasmic enzyme, but can be charged by the organellar or the E. coli enzyme
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
L-thiazolidine-4-carboxylic acid can replace proline in ATP-diphosphate exchange
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
L-thiazolidine-4-carboxylic acid can replace proline in ATP-diphosphate exchange
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
L-thiazolidine-4-carboxylic acid can replace proline in ATP-diphosphate exchange
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
two-step reaction
-
r
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
binding of L-proline and ATP causes conformational changes in the proline binding loop and motif 2 loop, formation of an activated prolyl-adenylate reaction intermediate, required for the final conformational ordering of a ten residue peptide, the ordered loop, close to the active site
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
initial docking state of the tRNAPro in which the anticodon stem-loop is engaged, particularly via the tRNAPro-specific bases G35 and G36, but the 3'-end does not enter the active site
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
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
show the reaction diagram
-
the C-terminal anticodon binding domain with an alpha/beta fold binds to the anticodon stem-loop from the major groove side
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
a complex between ProRS and leucyl-tRNA synthetase, LeuRS, in Methanothermobacter thermautotrophicus enhances tRNAPro aminoacylation, overview
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
a two-step reaction
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
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
show the reaction diagram
Q831W7
small-substrate recognition by the prokaryote-type ProRS, model for posttransfer editing conformation, overview
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Q6N5P6
small-substrate recognition by the prokaryote-type ProRS, model for posttransfer editing conformation, overview
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
neither GagPol nor prolyl-tRNA synthetase are required for packaging of tRNAPro into MuLV, tRNAPro is used as primer for reverse transcription
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
semi-synthetic human tRNAPro prepared by annealing a 5'-57-mer fragment to a 3'-16-mer. The 5'-57-mer is prepared by in vitro transcription
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
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
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
activation of proline does not require tRNA. The dual specificity enzyme must distinguish cysteine from proline directly, without the assistance of each cognate tRNA, to achieve the necessary specificity required for protein synthesis
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
mutations are introduced into the acceptor stem and the anticodon. Variants containing a single substitution of C72 or A73, or of one of the anticodon nucleotides, are created by site-directed mutagenesis. Substitution of A73 in Methanococcus jannaschii tRNAPro by any of the other three nucleotides has a small effect (about 10fold) on kcat/Km. The G73 substitution has the most severe effect (12.2fold), whereas the C73 or U73 substitution has a smaller effect (2-fold and 6-fold, respectively). A73 is much less significant for Methanococcus jannaschii tRNA recognition than it is for the Escherichia coli tRNA. The weak contribution of A73 to recognition by Methanococcus jannaschii ProRS, however, is comparable with that of C73 in the human system. Position 72 of Methanococcus jannaschii tRNAPro also has a minor role in aminoacylation. Substitution with any other nucleotide has a less than 10fold effect on kcat/Km. The U substitution results in the largest decrease (5.3fold), followed by the G substitution (2.2fold). The A substitution is well tolerated with only a 1.4fold decrease in kcat/Km. Substitution of U34 with A or G has no effect on aminoacylation, whereas substitution with C results in only a 1.3fold decrease. The anticodon nucleotide G35 of tRNAPro is a minor determinant for aminoacylation. Substitution of G35 with A has the largest effect (9fold), followed by the C substitution (8fold), and the U substitution (1.5fold). The most important specificity determinant in Methanococcus jannaschii tRNAPro is G36. Substitution with C alone reduces the kcat/Km of aminoacylation by 250fold, and substitution with A results in a nearly 40fold decrease. The exception is the U substitution, which maintains a kcat/Km that is similar to that of the wild-type tRNA. A representative aminoacylation assay of the C36, A36, and U36 mutants relative to that of the wild-type is shown
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Q9Y9G0
recognition elements of Aeropyrum pernix tRNAPro are determined to be G35 and G36 of anticodon, discriminator base A73, and G1-C72 base pair at acceptor stem end
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
the enzyme mischarges tRNAPro with alanine at a rate that is 6800fold reduced relative to charging with proline. The enzyme is able to hydrolyze misactivated alanine via both pretransfer and post-transfer editing pathways. Mischarging of a tRNAPro transcript with cysteine is also detected. The enzyme stimulates ATP hydrolysis activity with the noncognate amino acid alanine but not in the presence of proline
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
the unmodified transcript of Methanococcus jannaschii tRNAPro is mis-acylated with cysteine. The origin of mischarging is not at the anticodon or acceptor stem. Replacement of the D loop in the tRNA core with that of tRNACys suppresses mischarging with cysteine without compromising the activity of aminoacylation with proline. Prevention of mis-placement by alteration of the core structure or by nucleotide modifications in the tRNA illustrates a novel strategy of the dual-specificity synthetase
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Q5SM28
Thermus thermophilus prolyl-tRNA synthetase exhibits a cysteinyl-tRNA synthetase activity although the organism also encodes a canonical cysteinyl-tRNA synthetase
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Aeropyrum pernix DSM 11879
Q9Y9G0
recognition elements of Aeropyrum pernix tRNAPro are determined to be G35 and G36 of anticodon, discriminator base A73, and G1-C72 base pair at acceptor stem end
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Escherichia coli 9723
-
4-hydroxy-L-proline can replace proline in ATP-diphosphate exchange, 3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange
-
-
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Giardia intestinalis WB
A8BR89
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Q58635
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
mutations are introduced into the acceptor stem and the anticodon. Variants containing a single substitution of C72 or A73, or of one of the anticodon nucleotides, are created by site-directed mutagenesis. Substitution of A73 in Methanococcus jannaschii tRNAPro by any of the other three nucleotides has a small effect (about 10fold) on kcat/Km. The G73 substitution has the most severe effect (12.2fold), whereas the C73 or U73 substitution has a smaller effect (2-fold and 6-fold, respectively). A73 is much less significant for Methanococcus jannaschii tRNA recognition than it is for the Escherichia coli tRNA. The weak contribution of A73 to recognition by Methanococcus jannaschii ProRS, however, is comparable with that of C73 in the human system. Position 72 of Methanococcus jannaschii tRNAPro also has a minor role in aminoacylation. Substitution with any other nucleotide has a less than 10fold effect on kcat/Km. The U substitution results in the largest decrease (5.3fold), followed by the G substitution (2.2fold). The A substitution is well tolerated with only a 1.4fold decrease in kcat/Km. Substitution of U34 with A or G has no effect on aminoacylation, whereas substitution with C results in only a 1.3fold decrease. The anticodon nucleotide G35 of tRNAPro is a minor determinant for aminoacylation. Substitution of G35 with A has the largest effect (9fold), followed by the C substitution (8fold), and the U substitution (1.5fold). The most important specificity determinant in Methanococcus jannaschii tRNAPro is G36. Substitution with C alone reduces the kcat/Km of aminoacylation by 250fold, and substitution with A results in a nearly 40fold decrease. The exception is the U substitution, which maintains a kcat/Km that is similar to that of the wild-type tRNA. A representative aminoacylation assay of the C36, A36, and U36 mutants relative to that of the wild-type is shown
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
the unmodified transcript of Methanococcus jannaschii tRNAPro is mis-acylated with cysteine. The origin of mischarging is not at the anticodon or acceptor stem. Replacement of the D loop in the tRNA core with that of tRNACys suppresses mischarging with cysteine without compromising the activity of aminoacylation with proline. Prevention of mis-placement by alteration of the core structure or by nucleotide modifications in the tRNA illustrates a novel strategy of the dual-specificity synthetase
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
activation of proline does not require tRNA. The dual specificity enzyme must distinguish cysteine from proline directly, without the assistance of each cognate tRNA, to achieve the necessary specificity required for protein synthesis
-
-
?
ATP + trans-4-hydroxyproline + tRNAPro
AMP + diphosphate + trans-4-hydroxyprolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
ATP-diphosphate exchange
-
-
-
additional information
?
-
-
ATP-diphosphate exchange
-
-
-
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
?
-
-
enzyme does not perform deacetylation reaction of mischarged Cys-tRNAPro and Ala-tRNAPro, the enzyme also performs the ATP-diphosphate exchange reaction, no charging of tRNACys with L-cysteine
-
?
additional information
?
-
-
no activity with L-cysteine, the enzyme also performs the ATP-diphosphate exchange reaction, enzyme possesses no editing activity against L-alanine and to prevent from misincorporation of alanine into proteins
-
?
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
-
?
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
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction, the enzyme possesses a pre- and post-editing mechanism for alanine
-
?
additional information
?
-
-
aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
-
?
additional information
?
-
-
phylogenetic analysis
-
?
additional information
?
-
-
in addition to enzymic activity, glutamyl-prolyl-tRNA synthetase is phosphorylated in response to interferon-gamma, binds the ceruloplasmin 3'-untranslated region in an mRNP containing three additional proteins, and silences ceruloplasmin mRNA translation
-
-
-
additional information
?
-
Q831W7
comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, overview
-
-
-
additional information
?
-
Q6N5P6
comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, overview
-
-
-
additional information
?
-
-
the glutamyl-prolyl tRNA synthetase determines the specificity of the heterotetrameric GAIT complex suppressing translation of selected mRNAs in interferon-gamma-activated monocytic cells by binding to a 3' UTR element in target mRNAs, critical role of EPRS WHEP domains in targeting and regulating GAIT complex binding to RNA, mechanism, overview. The enzyme is essential in regulating inflammatory gene expression
-
-
-
additional information
?
-
-
aminoacylation specificity, the archaeal prolyl-tRNA synthetase that can aminoacylate archaeal tRNAPro with proline or cysteine, but does not aminoacylate archaeal tRNACys with cysteine, overview
-
-
-
additional information
?
-
-
determination of Pro-AMP and Ala-AMP hydrolysis activities of wild-type and mutant enzymes, overview
-
-
-
additional information
?
-
-
determination of Pro-AMP and Ala-AMP hydrolysis activities, overview
-
-
-
additional information
?
-
-
substrate specificity, reducing effects of diverse different phosphorothioate substitutions in the 3'-strand of human tRNAPro on aminoacylation efficiency, mechanism, overview
-
-
-
additional information
?
-
-
the upstream WHEP pair of EPRS directs high-affinity binding to GAIT element-bearing mRNAs, while the overlapping, downstream pair binds NSAP1, which inhibits mRNA binding. Interaction of EPRS with ribosomal protein L13a and GAPDH induces a conformational witch that rescues mRNA binding and restores translational control, interaction analysis, overview
-
-
-
additional information
?
-
-
no activity with 3,4-phenyl-L-proline and pipecolic acid
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
r
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
r
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Q831W7
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Q6N5P6
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Q58635
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Q6LZD3
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Q9GQI4
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
P16659
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
P07814
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
A8BR89
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
a complex between ProRS and leucyl-tRNA synthetase, LeuRS, in Methanothermobacter thermautotrophicus enhances tRNAPro aminoacylation, overview
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
neither GagPol nor prolyl-tRNA synthetase are required for packaging of tRNAPro into MuLV, tRNAPro is used as primer for reverse transcription
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Giardia intestinalis WB
A8BR89
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
Q58635
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
-
?
additional information
?
-
-
phylogenetic analysis
-
?
additional information
?
-
-
in addition to enzymic activity, glutamyl-prolyl-tRNA synthetase is phosphorylated in response to interferon-gamma, binds the ceruloplasmin 3'-untranslated region in an mRNP containing three additional proteins, and silences ceruloplasmin mRNA translation
-
-
-
additional information
?
-
-
the glutamyl-prolyl tRNA synthetase determines the specificity of the heterotetrameric GAIT complex suppressing translation of selected mRNAs in interferon-gamma-activated monocytic cells by binding to a 3' UTR element in target mRNAs, critical role of EPRS WHEP domains in targeting and regulating GAIT complex binding to RNA, mechanism, overview. The enzyme is essential in regulating inflammatory gene expression
-
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(2-chloro-thiophene)-4-quinolinecarboxylic acid
-
-
2-(2-chloro-thiophene)-4-quinolinecarboxylic acid
-
weak inhibition
2-(3,4-dichloro-phenyl)-4-quinolinecarboxylic acid
-
-
2-(3,4-dichloro-phenyl)-4-quinolinecarboxylic acid
-
weak inhibition
2-(4-bromo-phenyl)-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-4-quinolinecarboxylic acid
-
weak inhibition
2-(4-bromo-phenyl)-5,7-dichloro-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-5,7-dichloro-4-quinolinecarboxylic acid
-
weak inhibition
2-(4-bromo-phenyl)-5-methyl-7-chloro-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-5-methyl-7-chloro-4-quinolinecarboxylic acid
-
weak inhibition
2-(4-bromo-phenyl)-6,8-dimethyl-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-6,8-dimethyl-4-quinolinecarboxylic acid
-
weak inhibition
2-(4-bromo-phenyl)-6-(4-hydroxyphenyl)-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-6-(trifluoromethoxy)-4-quinolinecarboxylic acid
-
strong inhibition
2-(4-bromo-phenyl)-6-(trifluoromethoxy)-4-quinolinecarboxylic acid
-
weak inhibition
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
-
strong inhibition
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
-
; strong inhibition
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-hydroxymethyl-4-quinolinecarboxylic acid
-
weak inhibition
2-(4-bromo-phenyl)-6-chloro-8-methyl-4-quinolinecarboxylic acid
-
best inhibitor, species-selective
2-(4-bromo-phenyl)-6-chloro-8-methyl-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-6-iodo-4-quinolinecarboxylic acid
-
strong inhibition
2-(4-bromo-phenyl)-6-iodo-4-quinolinecarboxylic acid
-
weak inhibition
2-(4-bromo-phenyl)-6-methyl-8-chloro-4-quinolinecarboxylic acid
-
strong inhibition
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
-
weak inhibition
2-(4-[trifluoromethyl]-phenyl)-4-quinolinecarboxylic acid
-
weak inhibition
2-furyl-4-quinolinecarboxylic acid
-
weak inhibition
2-naphthyl-4-quinolinecarboxylic acid
-
-
2-naphthyl-4-quinolinecarboxylic acid
-
weak inhibition
2-phenyl-4-quinolinecarboxylic acid
-
weak inhibition
2-pyridyl-4-quinolinecarboxylic acid
-
weak inhibition
2-Pyrrolidinone
-
-
3,4-Dehydroproline
-
-
3,4-Dehydroproline
-
competitive inhibition of proline transfer to tRNA, no inhibition of proline-dependent ATP-diphosphate exchange
3-Selenaproline
-
competitive
4-Methylene-DL-proline
-
weak
5'-O-(N-[prolyl]-sulphamoyl) adenosine
Q831W7
i.e. ProAMS, a nonhydrolyzable analogue of the prolyl-adenylate
5'-O-(N-[prolyl]-sulphamoyl) adenosine
Q6N5P6
i.e. ProAMS, a nonhydrolyzable analogue of the prolyl-adenylate
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
-
-
5'-O-[N-(L-Prolyl)-sulfamoyl]adenosine
-
a non-hydrolyzable adenylate analogue
cis(exo)-3,4-Methano-L-proline
-
-
cis-3-Hydroxy-L-proline
-
weak
CsCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: above 2 M
CsCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.5 M
CsCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.51 M
CsCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 1.7 M
cysteamine
-
inhibition of Cys-tRNAPro formation
cysteinyl-sulfamoyl-adenylate
-
i.e. Cys-AMS, intermediate analogue, competitive inhibition
D-cysteine-DL-homocysteine
-
inhibition of Cys-tRNAPro formation
DL-Proline amide
-
-
febrifugine
-
-
-
halofuginone
P07814
strong inhibition at 0.001 mM
-
halofuginone
-
competitive inhibitor
-
iodoacetamide
-
more than 90% protection by 10 mM ATP or 10 mM ATP + 10 mM Pro
KCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: above 2 M
KCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.37 M
KCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.4 M
KCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 2.1 M
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
-
inhibition of Cys-tRNAPro formation
L-cysteine methyl ester
-
inhibition of Cys-tRNAPro formation
L-proline
-
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
-
-
LiCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 1.2 M
LiCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.25 M
LiCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.23 M
N-acetyl-L-cysteine
-
inhibition of Cys-tRNAPro formation
N-Ethylglycine
-
weak
N-Methyl-L-alanine
-
weak
N-methylglycine
-
weak
N-methylglycine
-
-
NaCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 1.5 M
NaCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.3 M
NaCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.27 M
NaCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 1.43 M
NH4Cl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 1.0 M
NH4Cl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.35 M
NH4Cl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.38 M
NH4Cl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 1.1 M
p-chloromercuribenzoate
-
ATP, tRNA, Pro or several analogues of Pro, protect against inhibition. Reactivation by sulfhydryl-reducing reagents, reactivation of Delonix enzyme is markedly temperature-dependent, Phaseolus enzyme is reactivated equally efficiently at all temperatures tested
p-chloromercuribenzoate
-
-
proline analogues
-
-
-
prolyl-sulfamoyl-adenylate
-
i.e. Pro-AMS, intermediate analogue, competitive inhibition
tetrahydrofuran
-
-
Tetrahydrothiophen
-
-
LiCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 1.2 M
additional information
-
no inhibition of Cys-tRNAPro formation by L-sulfinic acid, L-cysteic acid, S-methyl L-cysteine, and homocysteine thiolactone
-
additional information
-
MAZ1310 has no inhibitory effect on enzyme activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tRNA
-
stimulates l-cysteine activation 2-3fold
additional information
-
a complex between ProRS and leucyl-tRNA synthetase, LeuRS, in Methanothermobacter thermautotrophicus enhances tRNAPro aminoacylation, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.28
3,4-dehydro-DL-proline
-
ATP-diphosphate exchange
0.364
3,4-dehydro-DL-proline
-
ATP-diphosphate exchange
0.5
3,4-dehydro-DL-proline
-
ATP-diphosphate exchange
0.74
3,4-dehydro-DL-proline
-
ATP-diphosphate exchange
0.78
3,4-dehydro-DL-proline
-
ATP-diphosphate exchange
2.2
3,4-dehydro-DL-proline
-
ATP-diphosphate exchange
2.2
3,4-dehydro-DL-proline
-
ATP-diphosphate exchange, L-azetidine-2-carboxylic acid
1.4
3-thiaproline
-
ATP-diphosphate exchange
1.4
3-thiaproline
-
3,4-dehydro-DL-proline, , ATP-diphosphate exchange
6.25
4-selenaproline
-
ATP-diphosphate exchange
55
4-selenaproline
-
ATP-diphosphate exchange
66
4-thiaproline
-
ATP-diphosphate exchange
0.049
ATP
-
aminoacylation reaction with L-proline, recombinant wild-type enzyme, pH 7.0, 70C
0.06
ATP
-
aminoacylation reaction with L-cysteine, recombinant wild-type enzyme, pH 7.0, 70C
0.6
ATP
-
-
2 - 3
cis(exo)-3,4-Methano-L-proline
-
ATP-diphosphate exchange
4.6
cis(exo)-3,4-Methano-L-proline
-
ATP-diphosphate exchange
7.1
cis(exo)-3,4-Methano-L-proline
-
ATP-diphosphate exchange
53
cis-4-hydroxyproline
-
pH 7.0, 37C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation
55
cis-4-hydroxyproline
-
pH 7.0, 37C, recombinant wild-type enzyme, amino acid activation
12.5
gamma-thiaproline
-
ATP-diphosphate exchange
79
L-alanine
-
37C
140
L-alanine
-
37C
140
L-alanine
-
pH 7.0, 37C, recombinant wild-type enzyme, amino acid activation
454
L-alanine
P16659
mutant enzyme G217A, at pH 7.0 and 22C
685
L-alanine
P16659
wild type enzyme, at pH 7.0 and 22C
1360
L-alanine
P16659
mutant enzyme E218A, at pH 7.0 and 22C
1.43
L-azetidine-2-carboxylic acid
-
ATP-diphosphate exchange
2
L-azetidine-2-carboxylic acid
-
ATP-diphosphate exchange
5.3
L-azetidine-2-carboxylic acid
-
ATP-diphosphate exchange
0.01
L-cysteine
-
recombinant enzyme, pH 7.2, 37C
0.02
L-cysteine
-
recombinant enzyme, pH 7.2, 60C
0.022
L-cysteine
-
aminoacylation reaction, recombinant wild-type enzyme, pH 7.0, 70C
0.03
L-cysteine
-
recombinant enzyme, pH 7.2, 37C
0.05
L-cysteine
-
recombinant enzyme, pH 7.2, 60C
0.05
L-cysteine
-
ATP-diphosphate exchange, pH 7.5, 35C
0.0745
L-cysteine
Q6LZD3
pH 7.0, 37C
0.09
L-cysteine
-
recombinant enzyme, pH 7.2, 60C
0.09
L-cysteine
-
ATP-diphosphate exchange reaction, pH 7.5, 35C
0.17
L-cysteine
-
recombinant enzyme, pH 7.2, 37C
0.18
L-cysteine
-
recombinant enzyme, pH 7.2, 37C
0.19
L-cysteine
-
recombinant enzyme, pH 7.2, 37C
0.2
L-cysteine
-
recombinant enzyme, pH 7.2, 37C
0.26
L-cysteine
-
recombinant enzyme, pH 7.2, 37C
0.137
L-Pro
-
ATP-diphosphate exchange
0.182
L-Pro
-
ATP-diphosphate exchange
0.29
L-Pro
-
ATP-diphosphate exchange
0.43
L-Pro
-
ATP-diphosphate exchange
0.45
L-Pro
-
ATP-diphosphate exchange
0.625
L-Pro
-
ATP-diphosphate exchange
0.0046
L-proline
Q6LZD3
pH 7.0, 37C
0.012
L-proline
-
60C, pH not specified in the publication, ATP-diphosphate exchange assay
0.027
L-proline
-
aminoacylation reaction, recombinant wild-type enzyme, pH 7.0, 70C
0.05
L-proline
-
recombinant enzyme, pH 7.2, 37C
0.06
L-proline
-
recombinant enzyme, pH 7.2, 60C
0.061
L-proline
-
presence of bovine serum albumine and leucyl-tRNA synthetase, 50C, pH 7.5
0.067
L-proline
-
ATP-diphosphate exchange reaction, pH 7.5, 35C
0.067
L-proline
-
presence of bovine serum albumine, 50C, pH 7.5
0.08
L-proline
-
recombinant enzyme, pH 7.2, 37C
0.11
L-proline
-
recombinant enzyme, pH 7.2, 37C
0.14
L-proline
-
recombinant enzyme, pH 7.2, 37C
0.15
L-proline
-
recombinant enzyme, pH 7.2, 60C
0.15
L-proline
-
pH 7.5, 37C, mutant K279A
0.16
L-proline
-
recombinant enzyme, pH 7.2, 37C
0.17
L-proline
-
recombinant enzyme, pH 7.2, 37C
0.18
L-proline
-
37C
0.18
L-proline
-
wild type enzyme, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
0.18
L-proline
-
wild type enzyme, at pH 7.5 and 22C
0.19
L-proline
-
mutant enzyme K297E/E303K, at pH 7.5 and 22C
0.199
L-proline
-
mutant enzyme E303D, at pH 7.5 and 22C
0.216
L-proline
-
mutant enzyme E303A, at pH 7.5 and 22C
0.22
L-proline
-
mutant enzyme H302A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
0.22
L-proline
-
mutant enzyme K297E, at pH 7.5 and 22C
0.228
L-proline
P16659
wild type enzyme, at pH 7.0 and 22C
0.25
L-proline
-
37C
0.25
L-proline
-
pH 7.0, 37C, recombinant wild-type enzyme, amino acid activation
0.26
L-proline
-
recombinant enzyme, pH 7.2, 60C
0.28
L-proline
-
recombinant enzyme, pH 7.2, 60C
0.28
L-proline
-
recombinant enzyme, pH 7.2, 37C
0.285
L-proline
-
ATP-diphosphate exchange reaction, pH 7.5, 35C
0.29
L-proline
-
recombinant enzyme, pH 7.2, 37C
0.3
L-proline
-
mutant enzyme G412A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
0.3
L-proline
-
mutant enzyme E303K, at pH 7.5 and 22C
0.33
L-proline
-
mutant enzyme D198A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
0.427
L-proline
P16659
mutant enzyme G217A, at pH 7.0 and 22C
0.45
L-proline
-
mutant enzyme N305A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
0.62
L-proline
-
mutant enzyme H302A/G412A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
0.76
L-proline
-
mutant enzyme F415A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
1.03
L-proline
-
mutant enzyme E234A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
3.4
L-proline
P16659
mutant enzyme E218A, at pH 7.0 and 22C
3.4
L-proline
-
mutant enzyme E218A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
31
L-proline
-
pH 7.5, 37C, mutant K279A
50
L-proline
-
pH 7.0, 37C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation
68
N-Methyl-L-alanine
-
ATP-diphosphate exchange
45
N-methylglycine
-
ATP-diphosphate exchange
67
N-methylglycine
-
ATP-diphosphate exchange
100
N-methylglycine
-
ATP-diphosphate exchange
140
N-methylglycine
-
ATP-diphosphate exchange
300
N-methylglycine
-
approximate value, , ATP-diphosphate exchange
0.12
Pro
-
-
0.3
Pro
-
wild-type
0.4
Pro
-
ATP-diphosphate exchange
0.8
Pro
-
3-thiaproline, , ATP-diphosphate exchange
1.7
Pro
-
mutant C443A
2.4
Pro
-
mutant C443G
3.1
Pro
-
mutant C443S
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
tRNAPro
-
pH 7.0, 37C
0.0014
tRNAPro
-
presence of bovine serum albumine and leucyl-tRNA synthetase, 50C, pH 7.5
0.002
tRNAPro
-
pH 7.0, 55C, C-terminal deletion mutant
0.0022
tRNAPro
-
pH 7.0, 55C, wild-type
0.0022
tRNAPro
-
presence of leucyl-tRNA synthetase, 50C, pH 7.5
0.0024
tRNAPro
-
presence of bovine serum albumine, 50C, pH 7.5
0.0041
tRNAPro
-
50C, pH 7.5
0.131
tRNAPro
-
pH 7.0, 37C, recombinant mutant EcDELTAINS Gly12Ser4, aminoacylation
14.14
tRNAPro
-
pH 7.0, 37C, recombinant wild-type enzyme, aminoacylation
20 - 50
L-thiazolidine-4-carboxylic acid
-
ATP-diphosphate exchange
additional information
additional information
-
-
-
additional information
additional information
-
ProRS and leucyl-tRNA synthetase, LeuRS, interaction kinetics
-
additional information
additional information
-
single turnover and burst kinetics, steady-state kinetics, recombinant His-tagged enzyme, overview
-
additional information
additional information
-
wild-type and mutant enzyme kinetics
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.7
ATP
-
mutant C443S, ATP-diphosphate exchange
15
ATP
-
mutant C443G, ATP-diphosphate exchange
28
ATP
-
mutant C443A, ATP-diphosphate exchange
81
ATP
-
wild-type enzyme, ATP-diphosphate exchange
0.056
cis-4-hydroxyproline
-
pH 7.0, 37C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation
21
cis-4-hydroxyproline
-
pH 7.0, 37C, recombinant wild-type enzyme, amino acid activation
0.11
L-alanine
-
37C
1.7
L-alanine
-
37C
1.7
L-alanine
-
pH 7.0, 37C, recombinant wild-type enzyme, amino acid activation
2.18
L-alanine
P16659
mutant enzyme G217A, at pH 7.0 and 22C
3.26
L-alanine
P16659
mutant enzyme E218A, at pH 7.0 and 22C
3.52
L-alanine
P16659
wild type enzyme, at pH 7.0 and 22C
0.003
L-cysteine
-
recombinant enzyme, pH 7.2, 37C
0.014
L-cysteine
-
recombinant enzyme, pH 7.2, 37C
0.02
L-cysteine
-
aminoacylation reaction, recombinant wild-type enzyme, pH 7.0, 70C
0.02
L-cysteine
-
recombinant enzyme, pH 7.2, 60C
0.022
L-cysteine
-
recombinant enzyme, pH 7.2, 37C
0.025
L-cysteine
-
recombinant enzyme, pH 7.2, 37C
0.04
L-cysteine
-
recombinant enzyme, pH 7.2, 60C
0.065
L-cysteine
-
recombinant enzyme, pH 7.2, 37C
0.083
L-cysteine
-
recombinant enzyme, pH 7.2, 37C
0.09
L-cysteine
-
recombinant enzyme, pH 7.2, 60C
0.11
L-cysteine
-
recombinant enzyme, pH 7.2, 37C
0.12
L-cysteine
-
recombinant enzyme, pH 7.2, 37C
0.19
L-cysteine
-
recombinant enzyme, pH 7.2, 60C
0.39
L-cysteine
-
recombinant enzyme, pH 7.2, 37C
0.8
L-cysteine
Q6LZD3
pH 7.0, 37C
0.024
L-proline
-
pH 7.5, 37C, mutant K279A
0.09
L-proline
-
aminoacylation reaction, recombinant wild-type enzyme, pH 7.0, 70C
0.131
L-proline
-
mutant enzyme F415A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
0.23
L-proline
-
pH 7.5, 37C, mutant K279A
0.61
L-proline
-
mutant enzyme N305A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
0.9
L-proline
Q6LZD3
pH 7.0, 37C
3.37
L-proline
P16659
mutant enzyme G217A, at pH 7.0 and 22C
3.4
L-proline
-
recombinant enzyme, pH 7.2, 60C
4.4
L-proline
P16659
mutant enzyme E218A, at pH 7.0 and 22C
4.4
L-proline
-
mutant enzyme E218A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
4.6
L-proline
-
mutant enzyme E303D, at pH 7.5 and 22C
5.1
L-proline
-
mutant enzyme E303K, at pH 7.5 and 22C
5.2
L-proline
-
mutant enzyme E303A, at pH 7.5 and 22C
5.6
L-proline
-
recombinant enzyme, pH 7.2, 37C
5.7
L-proline
-
mutant enzyme K297E, at pH 7.5 and 22C
5.9
L-proline
-
mutant enzyme K297E/E303K, at pH 7.5 and 22C
6.7
L-proline
-
mutant enzyme E234A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
6.98
L-proline
-
mutant enzyme D198A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
7.3
L-proline
-
mutant enzyme H302A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
10.7
L-proline
-
mutant enzyme H302A/G412A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
12
L-proline
-
pH 7.0, 37C, 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 37C
12.6
L-proline
-
wild type enzyme, at pH 7.5 and 22C
12.7
L-proline
P16659
wild type enzyme, at pH 7.0 and 22C
12.8
L-proline
-
mutant enzyme G412A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
14
L-proline
-
recombinant enzyme, pH 7.2, 37C
15
L-proline
-
recombinant enzyme, pH 7.2, 60C
19
L-proline
-
recombinant enzyme, pH 7.2, 37C
26
L-proline
-
recombinant enzyme, pH 7.2, 37C
32
L-proline
-
recombinant enzyme, pH 7.2, 37C
34
L-proline
-
recombinant enzyme, pH 7.2, 37C
35
L-proline
-
recombinant enzyme, pH 7.2, 37C
35
L-proline
-
recombinant enzyme, pH 7.2, 60C
60
L-proline
-
recombinant enzyme, pH 7.2, 37C
63
L-proline
-
recombinant enzyme, pH 7.2, 60C
70
L-proline
-
37C
70
L-proline
-
pH 7.0, 37C, recombinant wild-type enzyme, amino acid activation
80
L-proline
-
37C
15
trans-4-hydroxyproline
-
pH 7.0, 37C, recombinant wild-type enzyme, amino acid activation
0.0091
tRNAPro
-
pH 7.0, 37C, recombinant mutant EcDELTAINS Gly12Ser4, aminoacylation
0.239
tRNAPro
-
pH 7.0, 37C, recombinant wild-type enzyme, aminoacylation
0.4
tRNAPro
-
pH 7.0, 55C, C-terminal deletion mutant
0.58
tRNAPro
-
pH 7.0, 37C
1.6
tRNAPro
-
pH 7.0, 55C, wild-type
1.8
tRNAPro
-
steady-state
2.9
tRNAPro
-
presence of bovine serum albumine, 50C, pH 7.5
5.1
tRNAPro
-
presence of leucyl-tRNA synthetase, 50C, pH 7.5
6.9
tRNAPro
-
presence of bovine serum albumine and leucyl-tRNA synthetase, 50C, pH 7.5
9.8
tRNAPro
-
single turnover overall aminoacylation
10.8
tRNAPro
-
single turnover of the transfer step
210
L-proline
-
60C, pH not specified in the publication, ATP-diphosphate exchange assay
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
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0024
L-alanine
P16659
mutant enzyme E218A, at pH 7.0 and 22C
103
0.0048
L-alanine
P16659
mutant enzyme G217A, at pH 7.0 and 22C
103
0.00513
L-alanine
P16659
wild type enzyme, at pH 7.0 and 22C
103
10.7
L-cysteine
Q6LZD3
pH 7.0, 37C
74
0.17
L-proline
-
mutant enzyme F415A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
243
1.29
L-proline
P16659
mutant enzyme E218A, at pH 7.0 and 22C
243
1.3
L-proline
-
mutant enzyme E218A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
243
1.4
L-proline
-
mutant enzyme N305A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
243
6.5
L-proline
-
mutant enzyme E234A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
243
7.89
L-proline
P16659
mutant enzyme G217A, at pH 7.0 and 22C
243
17
L-proline
-
mutant enzyme H302A/G412A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
243
17
L-proline
-
mutant enzyme E303K, at pH 7.5 and 22C
243
21
L-proline
-
mutant enzyme D198A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
243
23
L-proline
-
mutant enzyme E303D, at pH 7.5 and 22C
243
24
L-proline
-
mutant enzyme E303A, at pH 7.5 and 22C
243
26
L-proline
-
mutant enzyme K297E, at pH 7.5 and 22C
243
31
L-proline
-
mutant enzyme K297E/E303K, at pH 7.5 and 22C
243
33
L-proline
-
mutant enzyme H302A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
243
43
L-proline
-
mutant enzyme G412A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
243
55.7
L-proline
P16659
wild type enzyme, at pH 7.0 and 22C
243
71
L-proline
-
wild type enzyme, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37C
243
71
L-proline
-
wild type enzyme, at pH 7.5 and 22C
243
196
L-proline
Q6LZD3
pH 7.0, 37C
243
12000
L-proline
-
60C, pH not specified in the publication, ATP-diphosphate exchange assay
243
19330
tRNAPro
-
pH 7.0, 37C
2671
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, 37C, recombinant wild-type enzyme
0.00005
prolyl-sulfamoyl-adenylate
-
versus L-proline, pH 7.5, 35C
0.000025
cysteinyl-sulfamoyl-adenylate
-
versus L-proline, pH 7.5, 35C
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.101
-
-
0.615
-
enzyme form associated with glutamyl-tRNA synthetase
1.26
-
free enzyme form
1.655
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
activities of wild-type and mutant enzymes, pre-transfer editing activity, overview
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
Escherichia coli tRNAPro
7
-
aminoacylation assay at
7
Q6LZD3
assay at
7.2
-
ATP-diphosphate exchange assay at
7.5 - 7.8
-
ATP-diphosphate exchange
7.5
-
assay at
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
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
-
pH 6.0: about 30% of maximal activity, pH 9.0: about 40% of maximal activity
6.8 - 7.6
-
variation of the pH in this range has little effect on activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
even at 85C the enzyme retains its specificity towards its cognate substrate
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
major part, enzyme participates in a multienzyme complex, not as large and stable as the one from nucleus
Manually annotated by BRENDA team
-
2.9% of total activity in the cell, enzyme participates in a large and stable multienzyme complex
Manually annotated by BRENDA team
additional information
-
the particulate form of the synthetases reflect true association of the enzymes with a high molecular weight cellular component common to both tissues
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Giardia intestinalis (strain ATCC 50803 / WB clone C6)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
105000
-
gel filtration
661767
113000
-
gel filtration
661767
127000
-
gel filtration
166
133000
-
free form, gel filtration
163
155000
-
cytoplasmic, gel filtration
92
162000
-
mitochondrial, gel filtration
92
172000
-
-
694123
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 60000, SDS-PAGE
dimer
-
2 * 62000, SDS-PAGE
dimer
-
bifunctional enzyme
dimer
-
2 * 53300, calcultaed
dimer
-
2 * 55700, calculated
additional information
-
the largest subunit (MW 150000, by SDS-PAGE) of the mammalian high-MW complex may be a bifunctional protein exhibiting both glutamyl-tRNA synthetase and prolyl-tRNA synthetase activities
additional information
-
5SrRNA is probably present as a 5SrRNA-L5 protein complex in the macromolucular aminoacyl-tRNA synthetase complexes in rat liver
additional information
-
enzyme is part of a high molecular mass aminoacyl-tRNA synthetase complex, which has a coherent structure that can be visualized by electron microscopy
additional information
-
multienzyme complex organization and structure by visualization of immunologically stained sites
additional information
-
enzyme forms binary complex with aminoacyl-tRNA synthetase like protein YbaK and ternary complexes with YbaK and tRNA. Specificity of trans-editing by YbaK is ensured through formation of complexes
additional information
-
enzyme in vivo interacts with leucyl-tRNA synthetase, increasing its catalytic efficiency 5fold
additional information
-
glutamyl-prolyl-tRNA synthetase is a component of the interferon gamma-activated inhibitor of translation complex
additional information
Q6N5P6
comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, cognate and noncognate adenylate analogue complexes, overview
additional information
Q831W7
comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, overview
additional information
-
the human EPRS consists of four major domains: an N-terminal elongation factor-1Bgamma-like domain, an ERS catalytic domain, a 300 amino acid linker domain containing three tandem WHEP domains, and a C-terminal PRS catalytic domain
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
glutamyl-prolyl-tRNA synthetase is phosphorylated in response to interferon-gamma
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant selenomethionine-labelled enzyme, expressed in Escherichia coli
-
sitting drop vapor diffusion method, using 28% (w/v) PEG 3350, 0.2 M magnesium chloride, 0.1 M Tris-HCl pH 7.8, at 4C
A8BR89
complexed with ATP and L-proline or halofuginone, hanging drop vapor diffusion method, using 0.1 M sodium cacodylate, 1.0 M sodium citrate dibasic trihydrate pH 6.5
P07814
vapour-diffusion method, protein solution is mixed with an equal volume of well solution containing 0.2 M ammonium sulfate, 20-30% PEG 4000, 5 mM 2-mercaptoethanol, 0.1 M sodium acetate, pH 4.5, 12-25C, a few days, X-ray diffraction structure determination at 3.2 A resolution, and analysis
-
vapour diffusion method, equal volumes of 3.8 mg/ml protein solution and precipitant solution containing 20 mM Tris, pH 7.5, 5 mM 2-mercaptoethanol, 50-250 mM MgCl2, 20C, X-ray diffraction structure determination at 2.55-3.1 A, and analysis
-
purified recombinant His-tagged wild-type and selenomethionine-labeled enzymes, hanging drop vapour diffusion method, mixing of protein solution containing 5 mg/ml with an equal volume of the reservoir solution containing 0.1 M citric acid, pH 5.5, 15%-17% PEG 3000, cryoprotection by 20% ethylene glycol, for PrsRp-adenylate analog complex cocrystals, the enzyme is mixed first with 500 nM ProAMS or 100 nM CysAMS, and then with an equal volume of a solution containing 0.1 M citric acid, pH 5.5, 10%-11% PEG 3000, 15%-20% ethylene glycol, X-ray diffraction structure determination and analysis at 2.9 A resolution
Q6N5P6
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7.8
-
90C, 30 min, enzyme contains considerable activity, no activity retained after exposure to 95C
166
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2
-
complete loss of activity after 30 min, in absence of glycerol and mercaptoethanol
171
25
-
50% loss of ATP-diphosphate exchange activity after 5 min, without stabilizing reagent
174
51
-
50% loss of ATP-diphosphate exchange activity after 5 min, without stabilizing reagent
174
55
-
50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.002 mM ATP
174
56
-
50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.002 mM ATP
174
58
-
50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.02 mM Pro
174
59
-
50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.02 mM Pro
174
62
-
50% loss of activity after 5 min in Tris-HCl buffer
177
65
-
50% loss of ATP-diphosphate exchange activity after 5 min, without stabilizing reagent
174
67
-
50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.002 mM ATP + 0.02 mM Pro
174
73
-
50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.002 mM ATP
174
78
-
50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.002 mM ATP + 0.02 mM Pro
174
90
-
pH 6-7.8, 30 min, enzyme retains considerable activity
166
95
-
pH 6-7.8, 30 min, unstable
166
additional information
-
ATP, Pro and several Pro analogues prevent inactivation at 0C; inclusion of a polyol together with the sulfhydryl-reducing reagent appears to synergistically enhance the stability on storage at 2C; the enzyme from a number of higher plants that producing azetidine -2-carboxylic acid (A2C) is more rapidly inactivated in the cold than the enzyme from plants which do not contain A2C
171
additional information
-
at pH 6.5, 0.01 mM Mg2+ stabilizes against thermal inactivation; at pH 8, in absence of Mg2+, ATP does not protect against thermal inactivation; bovine serum albumin and glycerol partially protect against thermal denaturation at 45C and 50C respectively; furan and tetrahydrothiophen, protect only in presence of ATP against thermal inactivation; mercaptoethanol or DTT stabilizes against heat inactivation; Pro or ATP markedly stabilizes against heat inactivation; several analogues of Pro protect against thermal inactivation
173
additional information
-
above 60C, little protection by bovine serum albumin and glycerol; at pH 8, in absence of Mg2+, ATP does not protect against thermal inactivation; bovine serum albumin and glycerol partially protect against thermal denaturation at 45C and 50C respectively; furan and tetrahydrothiophen, protect only in presence of ATP against thermal inactivation; several analogues of Pro protect against thermal inactivation
173
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
at pH 6.5, 0.01 mM Mg2+ stabilizes against thermal inactivation
-
at pH 8, in absence of Mg2+, ATP does not protect against thermal inactivation
-
ATP, Pro and several Pro analogues prevent inactivation at 0C
-
bovine serum albumin and glycerol partially protect against thermal denaturation at 45C and 50C respectively
-
furan and tetrahydrothiophen, only in presence of ATP protect against thermal inactivation
-
inclusion of a polyol together with the sulfhydryl-reducing reagent appears to synergistically enhance the stability on storage at 2C
-
L-azetidine-2-carboxylic acid, cis(exo)-3,4-methano-L-proline, 3,4-dehydro-DL-proline, L-thiazolidine-4-carboxylic acid, N-methylglycine, N-methyl-L-alanine or trans-3-hydroxy-L-proline protect against inactivation at 70C and 40C
-
mercaptoethanol or DTT stabilizes against heat inactivation
-
Pro or ATP markedly stabilizes against heat inactivation
-
rapid and reversible photoinactivation in absence of methylene blue. ATP or Pro protects
-
several analogues of Pro protect against thermal inactivation
-
the time taken for 4 M urea to reduced the activity by 50% is increased in presence of 15% glycerol from 0.7 min to 7 min and from 0.3 min to 1.5 min for the Phaseolus and Delonix enzymes respectively
-
Pro or ATP markedly stabilizes against heat inactivation
-
above 60C, little protection by bovine serum albumin and glycerol
-
at pH 8, in absence of Mg2+, ATP does not protect against thermal inactivation
-
ATP, Pro and several Pro analogues prevent inactivation at 0C
-
bovine serum albumin and glycerol partially protect against thermal denaturation at 45C and 50C respectively
-
furan and tetrahydrothiophen, only in presence of ATP protect against thermal inactivation
-
inclusion of a polyol together with the sulfhydryl-reducing reagent appears to synergistically enhance the stability on storage at 2C
-
L-azetidine-2-carboxylic acid, cis(exo)-3,4-methano-L-proline, 3,4-dehydro-DL-proline, L-thiazolidine-4-carboxylic acid, N-methylglycine, N-methyl-L-alanine or trans-3-hydroxy-L-proline protect against inactivation at 70C and 40C
-
photoinactivation in presence of methylene blue or rose bengal. Pro or several imino analogues protect, ATP is ineffective. In absence of methylene blue the enzyme is stable to light
-
Pro or ATP markedly stabilizes against heat inactivation
-
several analogues of Pro protect against thermal inactivation
-
the time taken for 4 M urea to reduced the activity by 50% is increased in presence of 15% glycerol from 0.7 min to 7 min and from 0.3 min to 1.5 min for the Phaseolus and Delonix enzymes respectively
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0.1 M Tris-maleate KOH buffer, pH 7.0, about 80% loss of activity in ATP-diphosphate exchange
-
0.1 M Tris-maleate KOH buffer, pH 8.0, about 85% loss of activity in ATP-diphosphate exchange
-
-20C, pH 6.8, 40% v/v glycerol, enzyme concentrated by ultrafiltration
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from overexpression in Escherichia coli
-
recombinant enzyme from Escherichia coli strain M15 by ammonium sulfate fractionation and anion exchange chromatography
Q831W7
recombinant His-tagged enzyme from overexpression in Escherichia coli
-
Talon cobalt affinity resin column chromatography
-
Talon cobalt affinity resin column chromatography, and gel filtration
-
Ni-NTA column chromatography and Superdex 75 gel filtration
A8BR89
Ni-NTA affinity column chromatography and Superdex 200 gel filtration
P07814
recombinant His-tagged enzyme from overexpression in Escherichia coli
-
recombinant enzyme from Escherichia coli
-
recombinant from Escherichia coli
-
recombinant His-tagged enzyme from expression in Escherichia coli
-
recombinant His-tagged enzyme from overexpression in Escherichia coli
-
recombinant His-tagged wild-type and C-terminally truncated enzymes from overexpressing Escherichia coli
-
recombinant His-tagged enzyme from Escherichia coli
-
recombinant His-tagged enzyme from overexpression in Escherichia coli
-
recombinant His6-tagged ProRS from Escherichia coli strain BL21(DE3) by anion exchange chromatography, gel filtration, and ultrafiltration, co-purification of ProRS and leucyl-tRNA synthetase, LeuRS, overview
-
recombinant His-tagged enzyme from overexpression in Escherichia coli
-
2 forms: a free form and a form noncovalently associated with glutamyl-tRNA synthetase
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Q6N5P6
recombinant His-tagged enzyme from overexpression in Escherichia coli
-
recombinant His-tagged enzyme from overexpression in Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of the enzyme in Escherichia coli strain M15
Q831W7
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli SG13009 (pREP4) cells
-
gene proS, overexpression of wild-type and mutant His-tagged ProRS
-
expressed in Escherichia coli
A8BR89
overexpressed in Escherichia coli
Q9GQI4
expressed in Escherichia coli
-
expressed in Escherichia coli Rosetta 2 (DE3) pLysS cells
P07814
expression of C-terminally His-tagged, full-length EPRS
-
expression of the His-tagged enzyme in Escherichia coli BL21(DE3)
-
gene proS, expression in Escherichia coli strain BL21(DE3)
-
gene proS, overexpression in Escherichia coli
-
overexpression of wild-type and C-terminally truncated enzymes as His-tagged proteins in Escherichia coli
-
recombinant His-tagged wild-type and mutants from overexpressing Escherichia coli BL21
-
expression in Escherichia coli
Q6LZD3
gene proS, expression in Escherichia coli strain SG13009
-
expression as His-tagged enzyme in Escherichia coli
-
expression of ProRS and leucyl-tRNA synthetase, LeuRS, in a Saccharomyces cerevisiae two-hybrid system, expression of His6-tagged ProRS in Escherichia coli strain BL21(DE3)
-
gene proS, expression in Escherichia coli strain BL21(DE3)
-
heterologous archaeal prolyl-tRNA/prolyl-tRNA synthase pair, Archaeoglobus fulgidus tRNAPro (AftRNAPro)/Pyrococcus horikoshii ProRS (PhProRS), for UAA mutagenesis in Escherichia coli
-
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
Q6N5P6
gene proS, overexpression of His-tagged wild-type ProRS and truncation mutant ScDELTA183
-
expression in Escherichia coli
Q5SM28
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
E218A
P16659
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
E218A/N305A
-
inactive
E234A
-
the overall aminoacylation activity of the mutant is reduced 2fold
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
G217A
P16659
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
G412A
-
the overall aminoacylation activity of the mutant is reduced 7fold
H302A
-
the overall aminoacylation activity of the mutant is reduced 2fold
H302A/G412A
-
the overall aminoacylation activity of the mutant is reduced 5.5fold
H366A
-
the mutant shows loss in L-alanine deacylation activity
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
-
site-directed mutagenesis
K279A
-
site-directed mutagenesis, subdomain II mutant, reduced aminoaclyation and pre-transfer editing activity
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
N305A
-
the aminoacylation activity of the mutant is nearly abolished with rates 70fold slower than the wild type
N305A/G412A
-
inactive
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
A57G
-
site-directed mutagenesis, the A57G mutation introduces a BstBI restriction site within the gene, but has no effect on catalytic activity
F1097A
P07814
the mutant shows strongly decreased aminoacylation activity compared to the wild type enzyme
F1097W
P07814
the mutant shows increased aminoacylation activity compared to the wild type enzyme
R1152K
P07814
the mutant shows increased aminoacylation activity compared to the wild type enzyme
R1152L
P07814
the mutant shows strongly decreased aminoacylation activity compared to the wild type enzyme
E103A
-
abolished activity with L-proline
P100A
-
highly reduced activity with L-cysteine
P100A
-
unaltered thermostability, loss of 90% cysteinylation activity, unaltered prolylation activity compared to the wild-type enzyme
E103A
-
unaltered thermostability, no remaining prolylation activity, 5% remaining cysteinylation activity compared to the wild-type enzyme
-
L266A
-
the mutant shows negligible in L-alanine deacylation at room temperature
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
E103A
-
unaltered thermostability, no remaining prolylation activity, 5% remaining cysteinylation activity compared to the wild-type enzyme
additional information
-
the C-terminally truncated enzyme is 3fold less active with L-cysteine and 10fold less active with L-alanine compared too the wild-type enzyme
additional information
-
C-terminal deletion mutant lacking last 50 amino acids, little effect on kinetic parameters
P100A
-
unaltered thermostability, loss of 90% cysteinylation activity, unaltered prolylation activity compared to the wild-type enzyme
-
additional information
-
the dual-specific enzyme is sufficient for Cys-tRNACys production in a mutant disrupted in the gene encoing the canonical CysRS
additional information
-
development of a heterologous archaeal prolyl-tRNA/prolyl-tRNA synthase pair, Archaeoglobus fulgidus tRNAPro (AftRNAPro)/Pyrococcus horikoshii ProRS (PhProRS), for UAA mutagenesis in Escherichia coli. Modification of the anticodon-binding pocket of Pyrococcus horikoshii prolyl-tRNA synthase reestablishes its functional binding interaction with multiple anticodon-variants of tRNAPro
additional information
-
construction of a truncated Sc ProRS mutant lacking the N-terminal 183 residues, ScDELTA183, which shows reduced enzyme activity compared to the wild-type enzyme, overview
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