Information on EC 6.1.1.15 - Proline-tRNA ligase:
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EC NUMBERCOMMENTARY
6.1.1.15-

RECOMMENDED NAMEGeneOntology No.
Proline-tRNA ligaseGO:0004827

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		ATP is the first substrate to enter into the reaction sequence and prolyl-tRNA is the last product to dissociate from the enzyme; bi uni ping pong mechanismEscherichia coli-175
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		-Thermus thermophilus-649132, 651296, 652298
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		enzyme with dual substrate specificity for L-proline and L-cysteine, Glu103 is critical for L-proline binding, Pro100 is critical for L-cysteine bindingMethanocaldococcus jannaschii-650058
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 alanineEscherichia coli-650167
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		-Homo sapiens-650558, 652154
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		-Candida albicans-650558
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		the C-terminal extremity folds back into the active siteThermus thermophilus-650975
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		-Giardia intestinalis-651296
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 mechanismMethanocaldococcus jannaschii-651296
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		-Methanococcus maripaludis-651296
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		-Oryctolagus cuniculus-651917
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		-Cricetulus griseus-652046
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		tRNA substrate recognition, bases A73 and G36 are importantMethanocaldococcus jannaschii-652131
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		-Escherichia coli-652154, 652298
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		enzyme shows dual substrate specificity with L-proline/tRNAPro and L-cysteine/tRNACysMethanocaldococcus jannaschii-652154
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		-Methanocaldococcus jannaschii-652298, 652299, 653591
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		-Aquifex aeolicus, Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Deinococcus radiodurans, Magnetospirillum magnetotacticum, Methanothermobacter thermautotrophicus, Novosphingobium aromaticivorans, Rhodopseudomonas palustris, Saccharomyces cerevisiae-652298
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		induced fit substrate recognition, reaction mechanism, proline binding site structureThermus thermophilus-652859
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		dual substrate specificityMethanothermobacter thermautotrophicus-653591
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 tRNAProThermus thermophilus-653918
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 activeMethanocaldococcus jannaschii, Methanothermobacter thermautotrophicus-661767
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		class II synthetases are limited by a step prior to aminoacyl transferDeinococcus radiodurans-675395

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
Aminoacylation----
AminoacylationThermus thermophilus--649132, 650975, 651296, 652298, 652859, 653918
AminoacylationMethanocaldococcus jannaschii--650058, 651296, 652131, 652154, 652298, 652299, 653591
AminoacylationEscherichia coli--650167, 652154, 652298
AminoacylationHomo sapiens--650558, 652154
AminoacylationCandida albicans--650558
AminoacylationGiardia intestinalis, Methanococcus maripaludis--651296
AminoacylationOryctolagus cuniculus--651917
AminoacylationCricetulus griseus--652046
AminoacylationMethanothermobacter thermautotrophicus--652298, 653591
AminoacylationAquifex aeolicus, Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Deinococcus radiodurans, Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans, Rhodopseudomonas palustris, Saccharomyces cerevisiae--652298
esterification----
esterificationThermus thermophilus--649132, 650975, 651296, 652298, 652859, 653918
esterificationMethanocaldococcus jannaschii--650058, 651296, 652131, 652154, 652298, 652299, 653591
esterificationEscherichia coli--650167, 652154, 652298
esterificationHomo sapiens--650558, 652154
esterificationCandida albicans--650558
esterificationGiardia intestinalis, Methanococcus maripaludis--651296
esterificationOryctolagus cuniculus--651917
esterificationCricetulus griseus--652046
esterificationMethanothermobacter thermautotrophicus--652298, 653591
esterificationAquifex aeolicus, Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Deinococcus radiodurans, Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans, Rhodopseudomonas palustris, Saccharomyces cerevisiae--652298

PATHWAYKEGG LinkMetaCyc Link
tRNA charging-TRNA-CHARGING-PWY

SYSTEMATIC NAMEIUBMB Comments
L-Proline:tRNAPro ligase (AMP-forming)-

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
class II prolyl-tRNA synthetaseEscherichia coli, Methanocaldococcus jannaschii, Methanococcus maripaludis, Methanothermobacter thermautotrophicus, Saccharomyces cerevisiae--674646
class II prolyl-tRNA synthetaseDeinococcus radiodurans--675395
class II prolyl-tRNA synthetaseHomo sapiens--694434
class II ProRSDeinococcus radiodurans--675395
Global RNA synthesis factor----
Global RNA synthesis factorThermus thermophilus--649132, 650975, 651296, 652298, 652859, 653918
Global RNA synthesis factorMethanocaldococcus jannaschii--650058, 651296, 652131, 652154, 652298, 652299, 653591
Global RNA synthesis factorEscherichia coli--650167, 652154, 652298
Global RNA synthesis factorHomo sapiens--650558, 652154
Global RNA synthesis factorCandida albicans--650558
Global RNA synthesis factorGiardia intestinalis, Methanococcus maripaludis--651296
Global RNA synthesis factorOryctolagus cuniculus--651917
Global RNA synthesis factorCricetulus griseus--652046
Global RNA synthesis factorMethanothermobacter thermautotrophicus--652298, 653591
Global RNA synthesis factorAquifex aeolicus, Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Deinococcus radiodurans, Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans, Rhodopseudomonas palustris, Saccharomyces cerevisiae--652298
GluProRSOryctolagus cuniculus--651917
glutamyl-/prolyl-tRNA synthetaseOryctolagus cuniculus--651917
Pro-tRNA synthetase----
Pro-tRNA synthetaseThermus thermophilus--649132, 650975, 651296, 652298, 652859, 653918
Pro-tRNA synthetaseMethanocaldococcus jannaschii--650058, 651296, 652131, 652154, 652298, 652299, 653591
Pro-tRNA synthetaseEscherichia coli--650167, 652154, 652298
Pro-tRNA synthetaseHomo sapiens--650558, 652154
Pro-tRNA synthetaseCandida albicans--650558
Pro-tRNA synthetaseGiardia intestinalis, Methanococcus maripaludis--651296
Pro-tRNA synthetaseOryctolagus cuniculus--651917
Pro-tRNA synthetaseCricetulus griseus--652046
Pro-tRNA synthetaseMethanothermobacter thermautotrophicus--652298, 653591
Pro-tRNA synthetaseAquifex aeolicus, Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Deinococcus radiodurans, Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans, Rhodopseudomonas palustris, Saccharomyces cerevisiae--652298
ProCysRSMethanocaldococcus jannaschii--650058
Proline translase----
Proline translaseThermus thermophilus--649132, 650975, 651296, 652298, 652859, 653918
Proline translaseMethanocaldococcus jannaschii--650058, 651296, 652131, 652154, 652298, 652299, 653591
Proline translaseEscherichia coli--650167, 652154, 652298
Proline translaseHomo sapiens--650558, 652154
Proline translaseCandida albicans--650558
Proline translaseGiardia intestinalis, Methanococcus maripaludis--651296
Proline translaseOryctolagus cuniculus--651917
Proline translaseCricetulus griseus--652046
Proline translaseMethanothermobacter thermautotrophicus--652298, 653591
Proline translaseAquifex aeolicus, Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Deinococcus radiodurans, Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans, Rhodopseudomonas palustris, Saccharomyces cerevisiae--652298
Proline--tRNA ligase----
Proline--tRNA ligaseThermus thermophilus--649132, 650975, 651296, 652298, 652859, 653918
Proline--tRNA ligaseMethanocaldococcus jannaschii--650058, 651296, 652131, 652154, 652298, 652299, 653591
Proline--tRNA ligaseEscherichia coli--650167, 652154, 652298
Proline--tRNA ligaseHomo sapiens--650558, 652154
Proline--tRNA ligaseCandida albicans--650558
Proline--tRNA ligaseGiardia intestinalis, Methanococcus maripaludis--651296
Proline--tRNA ligaseOryctolagus cuniculus--651917
Proline--tRNA ligaseCricetulus griseus--652046
Proline--tRNA ligaseMethanothermobacter thermautotrophicus--652298, 653591
Proline--tRNA ligaseAquifex aeolicus, Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Deinococcus radiodurans, Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans, Rhodopseudomonas palustris, Saccharomyces cerevisiae--652298
Prolyl RNA synthetase----
Prolyl RNA synthetaseThermus thermophilus--649132, 650975, 651296, 652298, 652859, 653918
Prolyl RNA synthetaseMethanocaldococcus jannaschii--650058, 651296, 652131, 652154, 652298, 652299, 653591
Prolyl RNA synthetaseEscherichia coli--650167, 652154, 652298
Prolyl RNA synthetaseHomo sapiens--650558, 652154
Prolyl RNA synthetaseCandida albicans--650558
Prolyl RNA synthetaseGiardia intestinalis, Methanococcus maripaludis--651296
Prolyl RNA synthetaseOryctolagus cuniculus--651917
Prolyl RNA synthetaseCricetulus griseus--652046
Prolyl RNA synthetaseMethanothermobacter thermautotrophicus--652298, 653591
Prolyl RNA synthetaseAquifex aeolicus, Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Deinococcus radiodurans, Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans, Rhodopseudomonas palustris, Saccharomyces cerevisiae--652298
prolyl-cysteinyl-tRNA synthetaseMethanocaldococcus jannaschii--650058
Prolyl-transfer ribonucleate synthetase----
Prolyl-transfer ribonucleate synthetaseThermus thermophilus--649132, 650975, 651296, 652298, 652859, 653918
Prolyl-transfer ribonucleate synthetaseMethanocaldococcus jannaschii--650058, 651296, 652131, 652154, 652298, 652299, 653591
Prolyl-transfer ribonucleate synthetaseEscherichia coli--650167, 652154, 652298
Prolyl-transfer ribonucleate synthetaseHomo sapiens--650558, 652154
Prolyl-transfer ribonucleate synthetaseCandida albicans--650558
Prolyl-transfer ribonucleate synthetaseGiardia intestinalis, Methanococcus maripaludis--651296
Prolyl-transfer ribonucleate synthetaseOryctolagus cuniculus--651917
Prolyl-transfer ribonucleate synthetaseCricetulus griseus--652046
Prolyl-transfer ribonucleate synthetaseMethanothermobacter thermautotrophicus--652298, 653591
Prolyl-transfer ribonucleate synthetaseAquifex aeolicus, Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Deinococcus radiodurans, Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans, Rhodopseudomonas palustris, Saccharomyces cerevisiae--652298
Prolyl-transfer ribonucleic acid synthetase----
Prolyl-transfer ribonucleic acid synthetaseThermus thermophilus--649132, 650975, 651296, 652298, 652859, 653918
Prolyl-transfer ribonucleic acid synthetaseMethanocaldococcus jannaschii--650058, 651296, 652131, 652154, 652298, 652299, 653591
Prolyl-transfer ribonucleic acid synthetaseEscherichia coli--650167, 652154, 652298
Prolyl-transfer ribonucleic acid synthetaseHomo sapiens--650558, 652154
Prolyl-transfer ribonucleic acid synthetaseCandida albicans--650558
Prolyl-transfer ribonucleic acid synthetaseGiardia intestinalis, Methanococcus maripaludis--651296
Prolyl-transfer ribonucleic acid synthetaseOryctolagus cuniculus--651917
Prolyl-transfer ribonucleic acid synthetaseCricetulus griseus--652046
Prolyl-transfer ribonucleic acid synthetaseMethanothermobacter thermautotrophicus--652298, 653591
Prolyl-transfer ribonucleic acid synthetaseAquifex aeolicus, Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Deinococcus radiodurans, Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans, Rhodopseudomonas palustris, Saccharomyces cerevisiae--652298
Prolyl-transfer RNA synthetase----
Prolyl-transfer RNA synthetaseThermus thermophilus--649132, 650975, 651296, 652298, 652859, 653918
Prolyl-transfer RNA synthetaseMethanocaldococcus jannaschii--650058, 651296, 652131, 652154, 652298, 652299, 653591
Prolyl-transfer RNA synthetaseEscherichia coli--650167, 652154, 652298
Prolyl-transfer RNA synthetaseHomo sapiens--650558, 652154
Prolyl-transfer RNA synthetaseCandida albicans--650558
Prolyl-transfer RNA synthetaseGiardia intestinalis, Methanococcus maripaludis--651296
Prolyl-transfer RNA synthetaseOryctolagus cuniculus--651917
Prolyl-transfer RNA synthetaseCricetulus griseus--652046
Prolyl-transfer RNA synthetaseMethanothermobacter thermautotrophicus--652298, 653591
Prolyl-transfer RNA synthetaseAquifex aeolicus, Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Deinococcus radiodurans, Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans, Rhodopseudomonas palustris, Saccharomyces cerevisiae--652298
Prolyl-tRNA synthetase----
Prolyl-tRNA synthetaseThermus thermophilus--649132, 650975, 651296, 652298, 652859, 653918
Prolyl-tRNA synthetaseMethanocaldococcus jannaschii--650058, 651296, 652131, 652154, 652298, 652299, 653591, 674646, 693220, 694001
Prolyl-tRNA synthetaseEscherichia coli--650167, 652154, 652298, 674646, 691088, 693220
Prolyl-tRNA synthetaseHomo sapiens--650558, 652154, 693220
Prolyl-tRNA synthetaseCandida albicans--650558
Prolyl-tRNA synthetaseMethanococcus maripaludis--651296, 674646
Prolyl-tRNA synthetaseGiardia intestinalis--651296
Prolyl-tRNA synthetaseOryctolagus cuniculus--651917
Prolyl-tRNA synthetaseCricetulus griseus--652046
Prolyl-tRNA synthetaseMethanothermobacter thermautotrophicus--652298, 653591, 674646, 674875, 694001
Prolyl-tRNA synthetaseSaccharomyces cerevisiae--652298, 674646
Prolyl-tRNA synthetaseDeinococcus radiodurans--652298, 675395
Prolyl-tRNA synthetaseRhodopseudomonas palustris--652298, 677155
Prolyl-tRNA synthetaseAquifex aeolicus, Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans--652298
Prolyl-tRNA synthetaseEnterococcus faecalisQ831W7-677155
Prolyl-tRNA synthetaseMethanopyrus kandleri--694001
ProRS----
ProRSThermus thermophilus--649132, 650975, 651296, 652298, 652859, 653918
ProRSMethanocaldococcus jannaschii--650058, 651296, 652131, 652154, 652298, 652299, 653591, 674646, 693220, 694001
ProRSEscherichia coli--650167, 652154, 652298, 674646, 691088, 693220
ProRSHomo sapiens--650558, 652154, 693220
ProRSCandida albicans--650558
ProRSMethanococcus maripaludis--651296, 674646
ProRSGiardia intestinalis--651296
ProRSOryctolagus cuniculus--651917
ProRSCricetulus griseus--652046
ProRSMethanothermobacter thermautotrophicus--652298, 653591, 674646, 674875, 694001
ProRSSaccharomyces cerevisiae--652298, 674646
ProRSDeinococcus radiodurans--652298, 675395
ProRSRhodopseudomonas palustris--652298, 677155
ProRSAquifex aeolicus, Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans--652298
ProRSEnterococcus faecalisQ831W7-677155
ProRSMethanopyrus kandleri--694001
ProRSTTThermus thermophilus--649132, 650975, 652859, 653918
glutamyl-prolyl tRNA synthetaseHomo sapiens--694123
additional informationHomo sapiens-cf. EC 6.1.1.17694123

CAS REGISTRY NUMBERCOMMENTARY
9055-68-9-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Aeropyrum pernixstrain K1660617--Manually annotated by BRENDA team
Aquifex aeolicusbacterial enzyme type652298--Manually annotated by BRENDA team
Asparagus officinalis-177--Manually annotated by BRENDA team
Beta vulgaris-174--Manually annotated by BRENDA team
Borrelia burgdorferiarchaeal enzyme type652298--Manually annotated by BRENDA team
Bos taurus-92--Manually annotated by BRENDA team
Candida albicans-650558--Manually annotated by BRENDA team
Clostridium sticklandiiarchaeal enzyme type652298--Manually annotated by BRENDA team
Convallaria majalis-174, 177--Manually annotated by BRENDA team
Cricetulus griseus-652046--Manually annotated by BRENDA team
Cytophaga hutchinsoniiarchaeal enzyme type652298--Manually annotated by BRENDA team
Deinococcus radiodurans-675395--Manually annotated by BRENDA team
Deinococcus radioduransarchaeal enzyme type652298--Manually annotated by BRENDA team
Delonix regia-171, 172, 173, 174--Manually annotated by BRENDA team
Enterococcus faecalis-677155Q831W7SwissProtManually annotated by BRENDA team
Escherichia coli-160, 168, 170, 175, 652154, 674646, 691088, 693220--Manually annotated by BRENDA team
Escherichia colibacterial enzyme type652298--Manually annotated by BRENDA team
Escherichia coliclass II enzyme, purified recombinant wild-type and mutant enzymes650167--Manually annotated by BRENDA team
Escherichia colistrain 9723176--Manually annotated by BRENDA team
Escherichia coliwild-type enzyme and mutant enzymes C443A, C443G, and C443S164--Manually annotated by BRENDA team
Escherichia coli 9723strain 9723176--Manually annotated by BRENDA team
Giardia intestinalisenzyme with dual substrate specificity651296--Manually annotated by BRENDA team
Haemophilus influenzae-662414--Manually annotated by BRENDA team
Hemerocallis fulva-174--Manually annotated by BRENDA team
Homo sapiens-161, 650558, 652154, 693220, 694123, 694434--Manually annotated by BRENDA team
Homo sapiensisoform glutamyl-prolyl-tRNA synthetase661440--Manually annotated by BRENDA team
Magnetospirillum magnetotacticumarchaeal enzyme type652298--Manually annotated by BRENDA team
Mammalia-161--Manually annotated by BRENDA team
Methanocaldococcus jannaschii-652154, 653591, 661767, 693220, 694001--Manually annotated by BRENDA team
Methanocaldococcus jannaschiiarchaeal enzyme type652298--Manually annotated by BRENDA team
Methanocaldococcus jannaschiienzyme with dual substrate specificity651296--Manually annotated by BRENDA team
Methanocaldococcus jannaschiieukaryotic-like enzyme type652131--Manually annotated by BRENDA team
Methanocaldococcus jannaschiigene proS652299, 674646--Manually annotated by BRENDA team
Methanocaldococcus jannaschiiprolyl-cysteinyl-tRNA synthetase, enzyme with dual specificity650058--Manually annotated by BRENDA team
Methanococcus maripaludisenzyme with dual substrate specificity651296--Manually annotated by BRENDA team
Methanococcus maripaludisgene proS674646--Manually annotated by BRENDA team
Methanopyrus kandleri-694001--Manually annotated by BRENDA team
Methanothermobacter thermautotrophicus-661767, 662383, 674875, 694001--Manually annotated by BRENDA team
Methanothermobacter thermautotrophicusarchaeal enzyme type652298--Manually annotated by BRENDA team
Methanothermobacter thermautotrophicusgene proS653591, 674646--Manually annotated by BRENDA team
Moloney murine leukemia virusMuLV, produced in murine cells693908--Manually annotated by BRENDA team
Mus musculus-126--Manually annotated by BRENDA team
Novosphingobium aromaticivoransarchaeal enzyme type652298--Manually annotated by BRENDA team
Oryctolagus cuniculuspurified multisynthetase complex, the enzyme is a bifunctional glutamyl-/prolyl-tRNA synthetase651917--Manually annotated by BRENDA team
Ovis aries-161--Manually annotated by BRENDA team
Parkinsonia aculeata-174--Manually annotated by BRENDA team
Phaseolus vulgaris-170, 171, 172, 173, 174, 177--Manually annotated by BRENDA team
Pisum sativum-177--Manually annotated by BRENDA team
Polygonatum multiflorum-174, 177--Manually annotated by BRENDA team
Ranunculus bulbosus-174--Manually annotated by BRENDA team
Rattus norvegicus-163, 165, 168, 169, 26--Manually annotated by BRENDA team
Rhodopseudomonas palustris-677155Q6N5P6SwissProtManually annotated by BRENDA team
Rhodopseudomonas palustrisbacterial enzyme type652298--Manually annotated by BRENDA team
Saccharomyces cerevisiae-674646--Manually annotated by BRENDA team
Saccharomyces cerevisiaearchaeal enzyme type652298--Manually annotated by BRENDA team
Thermus aquaticus-166--Manually annotated by BRENDA team
Thermus thermophilus-649132, 652859--Manually annotated by BRENDA team
Thermus thermophilusarchaeal enzyme type652298--Manually annotated by BRENDA team
Thermus thermophilusclass IIa synthetase of the eukaryote/archaeon-like structure type650975--Manually annotated by BRENDA team
Thermus thermophilusenzyme with dual substrate specificity651296--Manually annotated by BRENDA team
Thermus thermophilusstrain HB8, purified class IIa enzyme653918--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + cis-4-hydroxyproline + tRNAProAMP + diphosphate + cis-4-hydroxyprolyl-tRNAPro
show the reaction diagram		Escherichia coli--674646--?
ATP + L-alanine + tRNAProAMP + diphosphate + L-alanyl-tRNAPro
show the reaction diagram		Homo sapiens-very low activity652154-652154?
ATP + L-alanine + tRNAProAMP + diphosphate + L-alanyl-tRNAPro
show the reaction diagram		Escherichia coli, Methanocaldococcus jannaschii-enzyme possesses both pre- and post-transfer hydrolytic editing activity to prevent from misincorporation of alanine into proteins652154-652154?
ATP + L-alanine + tRNAProAMP + diphosphate + L-alanyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii-misacetylation of tRNAPro, no editing652299-652299?
ATP + L-alanine + tRNAProAMP + diphosphate + L-alanyl-tRNAPro
show the reaction diagram		Escherichia coli-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 editing650167-650167?
ATP + L-alanine + tRNAProAMP + diphosphate + L-alanyl-tRNAPro
show the reaction diagram		Escherichia coli-L-alanine is a poor substrate674646--?
ATP + L-alanine + tRNAProAMP + diphosphate + L-alanyl-tRNAPro
show the reaction diagram		Escherichia coli-mutant K279A, low activity693220--?
ATP + L-cysteine + tRNACysAMP + diphosphate + L-cysteinyl-tRNACys
show the reaction diagram		Methanothermobacter thermautotrophicus--653591-653591?
ATP + L-cysteine + tRNACysAMP + diphosphate + L-cysteinyl-tRNACys
show the reaction diagram		Methanocaldococcus jannaschii-dual specificity of the enzyme, no pre- and post-transfer hydrolytic editing activity652154-652154?
ATP + L-cysteine + tRNACysAMP + diphosphate + L-cysteinyl-tRNACys
show the reaction diagram		Methanocaldococcus jannaschii-two-step reaction mechanism, first step is the amino acid activation, formation of the intermediate Cys-AMP is dependent on tRNACys650058-650058?
ATP + L-cysteine + tRNAProAMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram		Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Methanopyrus kandleri--694001--?
ATP + L-cysteine + tRNAProAMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii-two-step reaction651296-651296r
ATP + L-cysteine + tRNAProAMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram		Giardia intestinalis, Methanococcus maripaludis-dual-specificity enzyme651296-651296?
ATP + L-cysteine + tRNAProAMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram		Thermus thermophilus-dual-specificity enzyme, enzyme contains a discrete cysteine binding pocket651296-651296?
ATP + L-cysteine + tRNAProAMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii-misacetylation of tRNAPro, no editing652299-652299?
ATP + L-cysteine + tRNAProAMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram		Thermus thermophilus, Escherichia coli, Saccharomyces cerevisiae, Methanothermobacter thermautotrophicus, Rhodopseudomonas palustris, Clostridium sticklandii, Methanocaldococcus jannaschii, Deinococcus radiodurans, Borrelia burgdorferi, Aquifex aeolicus, Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans, Cytophaga hutchinsonii-misacetylation, no editing of the misactivated Cys-tRNAPro652298-652298?
ATP + L-cysteine + tRNAProAMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii-two-step reaction, both steps are dependent on tRNACys651296-651296r
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Phaseolus vulgaris--171-171-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Phaseolus vulgaris--172-172-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Phaseolus vulgaris--173-173-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Cricetulus griseus--652046-652046?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Mammalia--161-161-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Thermus aquaticus--166-166-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Delonix regia--171-171-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Delonix regia--172-172-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Delonix regia--173-173-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Polygonatum multiflorum--174-174-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Polygonatum multiflorum--177-177-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Thermus thermophilus--649132-649132?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Thermus thermophilus--650975-650975?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Thermus thermophilus--651296-651296?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Thermus thermophilus--652298-652298?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Thermus thermophilus--652859-652859?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Thermus thermophilus--653918-653918?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli--160-160-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli--164-164-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli--168-168-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli--170-170-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli--175-175-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli--650167-650167?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli--652154-652154?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli--652298-652298?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli--674646, 691088, 693220--?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli--652154-652154ir
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Homo sapiens--161-161-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Homo sapiens--650558-650558?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Homo sapiens--652154-652154?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Homo sapiens--693220, 694123, 694434--?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Rattus norvegicus--26-26-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Rattus norvegicus--163-163-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Rattus norvegicus--165-165-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Rattus norvegicus--168-168-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Rattus norvegicus--169-169-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Saccharomyces cerevisiae--652298-652298?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Saccharomyces cerevisiae--674646--?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Bos taurus--92-92-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Oryctolagus cuniculus--651917-651917?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanothermobacter thermautotrophicus--652298-652298?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanothermobacter thermautotrophicus--653591-653591?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanothermobacter thermautotrophicus--661767, 662383, 674646, 674875, 694001--?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Ovis aries--161-161-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Giardia intestinalis--651296-651296?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Rhodopseudomonas palustris--652298-652298?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Candida albicans--650558-650558?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Clostridium sticklandii--652298-652298?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii--650058-650058?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii--652131-652131?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii--652154-652154?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii--652298-652298?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii--652299-652299?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii--653591-653591?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii--661767, 674646, 693220, 694001--?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii--651296-651296r
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanopyrus kandleri--694001--?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanococcus maripaludis--651296-651296?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanococcus maripaludis--674646--?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Moloney murine leukemia virus--693908--?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Deinococcus radiodurans--652298-652298?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Deinococcus radiodurans--675395--?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Borrelia burgdorferi, Aquifex aeolicus, Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans, Cytophaga hutchinsonii--652298-652298?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Enterococcus faecalisQ831W7-677155--?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Rhodopseudomonas palustrisQ6N5P6-677155--?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Phaseolus vulgaris-the chloroplastic-specific tRNAPro is not recognized by the cytoplasmic enzyme but can be charged by organellar or E. coli enzyme170-170-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Phaseolus vulgaris, Delonix regia, Hemerocallis fulva, Ranunculus bulbosus, Beta vulgaris, Parkinsonia aculeata, Convallaria majalis-N-methylglycine can replace proline in ATP-diphosphate exchange174-174-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Phaseolus vulgaris-L-azetidine-2-carboxylic acid can replace proline in ATP-diphosphate exchange (not)174-174-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Phaseolus vulgaris-L-azetidine-2-carboxylic acid can replace proline in ATP-diphosphate exchange (not)177-177-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Hemerocallis fulva, Ranunculus bulbosus, Beta vulgaris-L-azetidine-2-carboxylic acid can replace proline in ATP-diphosphate exchange (not)174-174-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Asparagus officinalis-L-azetidine-2-carboxylic acid can replace proline in ATP-diphosphate exchange (not)177---
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Pisum sativum-L-azetidine-2-carboxylic acid can replace proline in ATP-diphosphate exchange (not)177-177-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli-4-hydroxy-L-proline can replace proline in ATP-diphosphate exchange176-176-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Delonix regia, Parkinsonia aculeata, Convallaria majalis-cis(exo)-3,4-methano-L-proline can replace proline on ATP-diphosphate exchange174-174-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Phaseolus vulgaris-the two tRNAsPro in the cytoplasm can be charged by the cytoplasmic enzyme, but not by the organellar enzyme or the E. coli enzyme170-170-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Phaseolus vulgaris-3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange174-174-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Phaseolus vulgaris-3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange177-177-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Delonix regia, Hemerocallis fulva, Ranunculus bulbosus, Beta vulgaris, Parkinsonia aculeata, Convallaria majalis-3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange174-174-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Convallaria majalis-3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange177-177-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli-3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange176-176-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Phaseolus vulgaris-mitochondria-specific tRNAPro is not recognized by the cytoplasmic enzyme, but can be charged by the organellar or the E. coli enzyme170-170-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Phaseolus vulgaris-L-thiazolidine-4-carboxylic acid can replace proline in ATP-diphosphate exchange174-174-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Phaseolus vulgaris-L-thiazolidine-4-carboxylic acid can replace proline in ATP-diphosphate exchange177-177-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Delonix regia, Ranunculus bulbosus, Beta vulgaris, Parkinsonia aculeata-L-thiazolidine-4-carboxylic acid can replace proline in ATP-diphosphate exchange174-174-
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii-two-step reaction651296-651296r
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Thermus thermophilus-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 site652859-652859?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Thermus thermophilus-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 site650975-650975?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii-L-proline is the preferred substrate, two-step reaction mechanism, first step is the amino acid activation, intermediate Pro-AMP can be formed in absence of tRNAPro650058-650058?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli-no deacetylation by the wild-type enzyme, but mutants H369C and H369A is able to deacetylate Pro-tRNAPro650167-650167?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii-substitution of base 73 from A to G,C, or U decreases the enzyme activity 12.2, 2, and 6fold, respectively, the tRNAPro of Methanococcus jannashii shows prokaryotic features in the acceptor stem652131-652131?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Thermus thermophilus-the C-terminal anticodon binding domain with an alpha/beta fold binds to the anticodon stem-loop from the major groove side653918-653918?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Cricetulus griseus-the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm652046-652046?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanothermobacter thermautotrophicus-a complex between ProRS and leucyl-tRNA synthetase, LeuRS, in Methanothermobacter thermautotrophicus enhances tRNAPro aminoacylation, overview674875--?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Deinococcus radiodurans-a two-step reaction675395--?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli-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, overview674646--?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Enterococcus faecalisQ831W7small-substrate recognition by the prokaryote-type ProRS, model for posttransfer editing conformation, overview677155--?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Rhodopseudomonas palustrisQ6N5P6small-substrate recognition by the prokaryote-type ProRS, model for posttransfer editing conformation, overview677155--?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Moloney murine leukemia virus-neither GagPol nor prolyl-tRNA synthetase are required for packaging of tRNAPro into MuLV, tRNAPro is used as primer for reverse transcription693908--?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Homo sapiens-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 transcription694434--?
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli-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, overview691088--?
ATP + trans-4-hydroxyproline + tRNAProAMP + diphosphate + trans-4-hydroxyprolyl-tRNAPro
show the reaction diagram		Escherichia coli--674646--?
additional information?-Escherichia coli-ATP-diphosphate exchange160, 168---
additional information?-Rattus norvegicus-ATP-diphosphate exchange168---
additional information?-Escherichia coli, Rattus norvegicus-3-thiaproline, 4-thiaproline and 4-selenaproline can replace proline in the ATP-diphosphate exchange. 4-Thiaproline and 4-selenaproline show a much higher Km168---
additional information?-Methanocaldococcus jannaschii-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-cysteine652299-652299?
additional information?-Homo sapiens-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 proteins652154-652154?
additional information?-Thermus thermophilus-the enzyme also performs the ATP-diphosphate exchange reaction652298-652298?
additional information?-Escherichia coli-the enzyme also performs the ATP-diphosphate exchange reaction650167-650167?
additional information?-Escherichia coli, Saccharomyces cerevisiae, Methanothermobacter thermautotrophicus-the enzyme also performs the ATP-diphosphate exchange reaction652298-652298?
additional information?-Methanothermobacter thermautotrophicus-the enzyme also performs the ATP-diphosphate exchange reaction653591-653591?
additional information?-Rhodopseudomonas palustris, Clostridium sticklandii-the enzyme also performs the ATP-diphosphate exchange reaction652298-652298?
additional information?-Methanocaldococcus jannaschii-the enzyme also performs the ATP-diphosphate exchange reaction650058-650058?
additional information?-Methanocaldococcus jannaschii-the enzyme also performs the ATP-diphosphate exchange reaction652154-652154?
additional information?-Methanocaldococcus jannaschii, Deinococcus radiodurans, Borrelia burgdorferi, Aquifex aeolicus, Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans, Cytophaga hutchinsonii-the enzyme also performs the ATP-diphosphate exchange reaction652298-652298?
additional information?-Escherichia coli-the enzyme also performs the ATP-diphosphate exchange reaction, no activity with L-cysteine652154-652154?
additional information?-Methanocaldococcus jannaschii-the enzyme also performs the ATP-diphosphate exchange reaction, the enzyme possesses a pre- and post-editing mechanism for alanine651296-651296?
additional information?-Methanocaldococcus jannaschii-tRNA substrate specificity, overview652131-652131?
additional information?-Cricetulus griseus-aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I652046-652046?
additional information?-Methanocaldococcus jannaschii-phylogenetic analysis651296-651296?
additional information?-Homo sapiens-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 translation661440---
additional information?-Enterococcus faecalisQ831W7comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, overview677155---
additional information?-Rhodopseudomonas palustrisQ6N5P6comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, overview677155---
additional information?-Homo sapiens-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 expression694123---
additional information?-Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Methanopyrus kandleri-aminoacylation specificity, the archaeal prolyl-tRNA synthetase that can aminoacylate archaeal tRNAPro with proline or cysteine, but does not aminoacylate archaeal tRNACys with cysteine, overview694001---
additional information?-Escherichia coli-determination of Pro-AMP and Ala-AMP hydrolysis activities of wild-type and mutant enzymes, overview693220---
additional information?-Homo sapiens, Methanocaldococcus jannaschii-determination of Pro-AMP and Ala-AMP hydrolysis activities, overview693220---
additional information?-Homo sapiens-substrate specificity, reducing effects of diverse different phosphorothioate substitutions in the 3'-strand of human tRNAPro on aminoacylation efficiency, mechanism, overview694434---
additional information?-Homo sapiens-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, overview694123---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
ATP + L-cysteine + tRNAProAMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii-two-step reaction651296-651296
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Thermus thermophilus--649132-649132
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Thermus thermophilus--650975-650975
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Thermus thermophilus--651296-651296
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Thermus thermophilus--652298-652298
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Thermus thermophilus--652859-652859
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Thermus thermophilus--653918-653918
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli--650167-650167
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli--652154-652154
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli--652298-652298
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Escherichia coli--674646, 691088, 693220--
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Homo sapiens--650558-650558
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Homo sapiens--652154-652154
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Homo sapiens--693220, 694123, 694434--
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Saccharomyces cerevisiae--652298-652298
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Saccharomyces cerevisiae--674646--
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Oryctolagus cuniculus--651917-651917
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanothermobacter thermautotrophicus--652298-652298
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanothermobacter thermautotrophicus--653591-653591
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanothermobacter thermautotrophicus--674646, 694001--
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Giardia intestinalis--651296-651296
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Rhodopseudomonas palustris--652298-652298
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Candida albicans--650558-650558
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Clostridium sticklandii--652298-652298
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii--650058-650058
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii--652131-652131
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii--652154-652154
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii--652298-652298
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii--652299-652299
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii--653591-653591
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii--674646, 693220, 694001--
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanocaldococcus jannaschii--651296-651296
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanopyrus kandleri--694001--
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanococcus maripaludis--651296-651296
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanococcus maripaludis--674646--
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Deinococcus radiodurans--652298-652298
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Deinococcus radiodurans--675395--
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Borrelia burgdorferi, Aquifex aeolicus, Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans, Cytophaga hutchinsonii--652298-652298
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Enterococcus faecalisQ831W7-677155--
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Rhodopseudomonas palustrisQ6N5P6-677155--
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Cricetulus griseus-the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm652046-652046
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Methanothermobacter thermautotrophicus-a complex between ProRS and leucyl-tRNA synthetase, LeuRS, in Methanothermobacter thermautotrophicus enhances tRNAPro aminoacylation, overview674875--
ATP + L-proline + tRNAProAMP + diphosphate + L-prolyl-tRNAPro
show the reaction diagram		Moloney murine leukemia virus-neither GagPol nor prolyl-tRNA synthetase are required for packaging of tRNAPro into MuLV, tRNAPro is used as primer for reverse transcription693908--
additional information?-Cricetulus griseus-aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I652046-652046
additional information?-Methanocaldococcus jannaschii-phylogenetic analysis651296-651296
additional information?-Homo sapiens-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 translation661440--
additional information?-Homo sapiens-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 expression694123--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
ATPThermus thermophilus--649132, 650975, 651296, 652298, 652859, 653918 2D-image
ATPMethanocaldococcus jannaschii--650058, 651296, 652131, 652154, 652298, 652299, 653591, 674646, 693220, 694001 2D-image
ATPEscherichia coli--650167, 652154, 652298, 674646, 693220 2D-image
ATPHomo sapiens--650558, 652154, 693220, 694123, 694434 2D-image
ATPCandida albicans--650558 2D-image
ATPMethanococcus maripaludis--651296, 674646 2D-image
ATPGiardia intestinalis--651296 2D-image
ATPOryctolagus cuniculus--651917 2D-image
ATPCricetulus griseus--652046 2D-image
ATPMethanothermobacter thermautotrophicus--652298, 653591, 674646, 674875, 694001 2D-image
ATPSaccharomyces cerevisiae--652298, 674646 2D-image
ATPDeinococcus radiodurans--652298, 675395 2D-image
ATPAquifex aeolicus, Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans, Rhodopseudomonas palustris--652298 2D-image
ATPEnterococcus faecalisQ831W7binding structure and complex formation with cognate tRNA, overview677155 2D-image
ATPRhodopseudomonas palustrisQ6N5P6binding structure and complex formation with cognate tRNA, overview677155 2D-image
ATPMoloney murine leukemia virus--693908 2D-image
ATPMethanopyrus kandleri--694001 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Mg2+Phaseolus vulgaris, Polygonatum multiflorum-required177
Mg2+Methanothermobacter thermautotrophicus--674646, 674875, 694001
Mg2+Methanocaldococcus jannaschii--674646, 693220, 694001
Mg2+Escherichia coli--674646, 693220
Mg2+Methanococcus maripaludis, Saccharomyces cerevisiae--674646
Mg2+Deinococcus radiodurans--675395
Mg2+Enterococcus faecalisQ831W7-677155
Mg2+Rhodopseudomonas palustrisQ6N5P6-677155
Mg2+Homo sapiens--693220, 694123, 694434
Mg2+Moloney murine leukemia virus--693908
Mg2+Methanopyrus kandleri--694001
Mn2+Phaseolus vulgaris, Polygonatum multiflorum-can partially replace Mg2+ in activation177
Zn2+Thermus thermophilus-enzyme contains a unique additional zinc-binding domain650975
Zn2+Thermus thermophilus--652859
Zn2+Methanocaldococcus jannaschii, Methanothermobacter thermautotrophicus-chelated by 4 cysteine residues in the C-terminus653591

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2-(2-chloro-thiophene)-4-quinolinecarboxylic acidCandida albicans--650558 2D-image
2-(2-chloro-thiophene)-4-quinolinecarboxylic acidHomo sapiens-weak inhibition650558 2D-image
2-(3,4-dichloro-phenyl)-4-quinolinecarboxylic acidCandida albicans--650558 2D-image
2-(3,4-dichloro-phenyl)-4-quinolinecarboxylic acidHomo sapiens-weak inhibition650558 2D-image
2-(4-bromo-phenyl)-4-quinolinecarboxylic acidCandida albicans--650558 2D-image
2-(4-bromo-phenyl)-4-quinolinecarboxylic acidHomo sapiens-weak inhibition650558 2D-image
2-(4-bromo-phenyl)-5,7-dichloro-4-quinolinecarboxylic acidCandida albicans--650558 2D-image
2-(4-bromo-phenyl)-5,7-dichloro-4-quinolinecarboxylic acidHomo sapiens-weak inhibition650558 2D-image
2-(4-bromo-phenyl)-5-methyl-7-chloro-4-quinolinecarboxylic acidCandida albicans--650558 2D-image
2-(4-bromo-phenyl)-5-methyl-7-chloro-4-quinolinecarboxylic acidHomo sapiens-weak inhibition650558 2D-image
2-(4-bromo-phenyl)-6,8-dimethyl-4-quinolinecarboxylic acidCandida albicans--650558 2D-image
2-(4-bromo-phenyl)-6,8-dimethyl-4-quinolinecarboxylic acidHomo sapiens-weak inhibition650558 2D-image
2-(4-bromo-phenyl)-6-(4-hydroxyphenyl)-4-quinolinecarboxylic acidCandida albicans, Homo sapiens--650558 2D-image
2-(4-bromo-phenyl)-6-(trifluoromethoxy)-4-quinolinecarboxylic acidCandida albicans-strong inhibition650558 2D-image
2-(4-bromo-phenyl)-6-(trifluoromethoxy)-4-quinolinecarboxylic acidHomo sapiens-weak inhibition650558 2D-image
2-(4-bromo-phenyl)-6-alkenyl-4-quinolinecarboxylic acidCandida albicans, Homo sapiens--650558 2D-image
2-(4-bromo-phenyl)-6-amino-4-quinolinecarboxylic acidCandida albicans, Homo sapiens--650558 2D-image
2-(4-bromo-phenyl)-6-bromo-4-quinolinecarboxylic acidCandida albicans-strong inhibition650558 2D-image
2-(4-bromo-phenyl)-6-bromo-4-quinolinecarboxylic acidHomo sapiens--650558 2D-image
2-(4-bromo-phenyl)-6-bromo-8-(trifluoromethyl)-4-quinolinecarboxylic acidCandida albicans, Homo sapiens--650558 2D-image
2-(4-bromo-phenyl)-6-chloro-4-quinolinecarboxylic acidCandida albicans-; strong inhibition650558 2D-image
2-(4-bromo-phenyl)-6-chloro-4-quinolinecarboxylic acidHomo sapiens--650558 2D-image
2-(4-bromo-phenyl)-6-chloro-8-hydroxymethyl-4-quinolinecarboxylic acidCandida albicans--650558 2D-image
2-(4-bromo-phenyl)-6-chloro-8-hydroxymethyl-4-quinolinecarboxylic acidHomo sapiens-weak inhibition650558 2D-image
2-(4-bromo-phenyl)-6-chloro-8-methyl-4-quinolinecarboxylic acidCandida albicans-best inhibitor, species-selective650558 2D-image
2-(4-bromo-phenyl)-6-chloro-8-methyl-4-quinolinecarboxylic acidHomo sapiens--650558 2D-image
2-(4-bromo-phenyl)-6-iodo-4-quinolinecarboxylic acidCandida albicans-strong inhibition650558 2D-image
2-(4-bromo-phenyl)-6-iodo-4-quinolinecarboxylic acidHomo sapiens-weak inhibition650558 2D-image
2-(4-bromo-phenyl)-6-methyl-8-chloro-4-quinolinecarboxylic acidCandida albicans-strong inhibition650558 2D-image
2-(4-bromo-phenyl)-6-methyl-8-chloro-4-quinolinecarboxylic acidHomo sapiens--650558 2D-image
2-(4-bromo-phenyl)-7-bromo-8-methyl-4-quinolinecarboxylic acidCandida albicans, Homo sapiens--650558 2D-image
2-(4-bromo-phenyl)-7-fluoro-8-methyl-4-quinolinecarboxylic acidCandida albicans, Homo sapiens--650558 2D-image
2-(4-methoxy-phenyl)-4-quinolinecarboxylic acidCandida albicans, Homo sapiens-weak inhibition650558 2D-image
2-(4-[trifluoromethyl]-phenyl)-4-quinolinecarboxylic acidCandida albicans, Homo sapiens-weak inhibition650558 2D-image
2-furyl-4-quinolinecarboxylic acidCandida albicans, Homo sapiens-weak inhibition650558 2D-image
2-naphthyl-4-quinolinecarboxylic acidCandida albicans--650558 2D-image
2-naphthyl-4-quinolinecarboxylic acidHomo sapiens-weak inhibition650558 2D-image
2-phenyl-4-quinolinecarboxylic acidCandida albicans, Homo sapiens-weak inhibition650558 2D-image
2-pyridyl-4-quinolinecarboxylic acidCandida albicans, Homo sapiens-weak inhibition650558 2D-image
2-PyrrolidinonePhaseolus vulgaris--174 2D-image
3,4-DehydroprolineDelonix regia, Phaseolus vulgaris--174 2D-image
3,4-DehydroprolineEscherichia coli-competitive inhibition of proline transfer to tRNA, no inhibition of proline-dependent ATP-diphosphate exchange176 2D-image
3-pyrrolineDelonix regia, Phaseolus vulgaris--174 2D-image
3-SelenaprolineEscherichia coli, Rattus norvegicus-competitive168 2D-image
4-Methylene-DL-prolineDelonix regia-weak174 2D-image
5'-O-(N-[prolyl]-sulphamoyl) adenosineEnterococcus faecalisQ831W7i.e. ProAMS, a nonhydrolyzable analogue of the prolyl-adenylate677155 2D-image
5'-O-(N-[prolyl]-sulphamoyl) adenosineRhodopseudomonas palustrisQ6N5P6i.e. ProAMS, a nonhydrolyzable analogue of the prolyl-adenylate677155 2D-image
5'-O-[N-(L-alanyl)-sulfamoyl]adenosineEscherichia coli-a non-hydrolyzable adenylate analogue, a potent inhibitor of the ATP-diphosphate exchange reaction674646 2D-image
5'-O-[N-(L-Prolyl)-sulfamoyl]adenosineEscherichia coli--160 2D-image
5'-O-[N-(L-Prolyl)-sulfamoyl]adenosineEscherichia coli-a non-hydrolyzable adenylate analogue674646 2D-image
cis(exo)-3,4-Methano-L-prolineDelonix regia, Phaseolus vulgaris--174 2D-image
cis-3-Hydroxy-L-prolineDelonix regia, Phaseolus vulgaris-weak174 2D-image
CsClBeta vulgaris-concentration required to inhibit ATP-diphosphate exchange by 50%: above 2 M174 2D-image
CsClDelonix regia-concentration required to inhibit ATP-diphosphate exchange by 50%: 0.5 M174 2D-image
CsClParkinsonia aculeata-concentration required to inhibit ATP-diphosphate exchange by 50%: 0.51 M174 2D-image
CsClPhaseolus vulgaris-concentration required to inhibit ATP-diphosphate exchange by 50%: 1.7 M174 2D-image
cysteamineMethanocaldococcus jannaschii-inhibition of Cys-tRNAPro formation652299 2D-image
cysteinyl-sulfamoyl-adenylateMethanothermobacter thermautotrophicus-i.e. Cys-AMS, intermediate analogue, competitive inhibition653591 2D-image
D-cysteine-DL-homocysteineMethanocaldococcus jannaschii-inhibition of Cys-tRNAPro formation652299 2D-image
DL-Proline amidePhaseolus vulgaris--174 2D-image
iodoacetamideEscherichia coli-more than 90% protection by 10 mM ATP or 10 mM ATP + 10 mM Pro164 2D-image
KClBeta vulgaris-concentration required to inhibit ATP-diphosphate exchange by 50%: above 2 M174 2D-image
KClDelonix regia-concentration required to inhibit ATP-diphosphate exchange by 50%: 0.37 M174 2D-image
KClParkinsonia aculeata-concentration required to inhibit ATP-diphosphate exchange by 50%: 0.4 M174 2D-image
KClPhaseolus vulgaris-concentration required to inhibit ATP-diphosphate exchange by 50%: 2.1 M174 2D-image
L-azetidine-2-carboxylic acidDelonix regia, Phaseolus vulgaris--174 2D-image
L-cysteineMethanocaldococcus jannaschii-competitive inhibition of prolylation, a 40fold excess over L-proline concentration reduces the prolylation activity by 80%, no inhibition of mutant P100A650058 2D-image
L-cysteine ethyl esterMethanocaldococcus jannaschii-inhibition of Cys-tRNAPro formation652299 2D-image
L-cysteine methyl esterMethanocaldococcus jannaschii-inhibition of Cys-tRNAPro formation652299 2D-image
L-prolineMethanocaldococcus jannaschii-competitive inhibition of cysteinylation, a 40fold excess over L-cysteine concentration reduces the cysteinylation activity by over 80%, no inhibition of mutant E103A650058 2D-image
L-thiazolidine-4-carboxylic acidDelonix regia, Phaseolus vulgaris--174 2D-image
LiClBeta vulgaris-concentration required to inhibit ATP-diphosphate exchange by 50%: 1.2 M174 2D-image
LiClDelonix regia-concentration required to inhibit ATP-diphosphate exchange by 50%: 0.25 M174 2D-image
LiClParkinsonia aculeata-concentration required to inhibit ATP-diphosphate exchange by 50%: 0.23 M174 2D-image
N-acetyl-L-cysteineMethanocaldococcus jannaschii-inhibition of Cys-tRNAPro formation652299 2D-image
N-EthylglycineDelonix regia-weak174 2D-image
N-Methyl-L-alaninePhaseolus vulgaris-weak174 2D-image
N-methylglycineDelonix regia-weak174 2D-image
N-methylglycinePhaseolus vulgaris--174 2D-image
NaClBeta vulgaris-concentration required to inhibit ATP-diphosphate exchange by 50%: 1.5 M174 2D-image
NaClDelonix regia-concentration required to inhibit ATP-diphosphate exchange by 50%: 0.3 M174 2D-image
NaClParkinsonia aculeata-concentration required to inhibit ATP-diphosphate exchange by 50%: 0.27 M174 2D-image
NaClPhaseolus vulgaris-concentration required to inhibit ATP-diphosphate exchange by 50%: 1.43 M174 2D-image
NH4ClBeta vulgaris-concentration required to inhibit ATP-diphosphate exchange by 50%: 1.0 M174 2D-image
NH4ClDelonix regia-concentration required to inhibit ATP-diphosphate exchange by 50%: 0.35 M174 2D-image
NH4ClParkinsonia aculeata-concentration required to inhibit ATP-diphosphate exchange by 50%: 0.38 M174 2D-image
NH4ClPhaseolus vulgaris-concentration required to inhibit ATP-diphosphate exchange by 50%: 1.1 M174 2D-image
p-chloromercuribenzoateDelonix regia, Phaseolus vulgaris-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 tested171 2D-image
p-chloromercuribenzoatePhaseolus vulgaris--177 2D-image
proline analoguesMethanocaldococcus jannaschii--651296-
prolyl-sulfamoyl-adenylateMethanothermobacter thermautotrophicus-i.e. Pro-AMS, intermediate analogue, competitive inhibition653591 2D-image
PyrroleDelonix regia, Phaseolus vulgaris--174 2D-image
PyrrolidineDelonix regia, Phaseolus vulgaris--174 2D-image
TetrahydrofuranDelonix regia, Phaseolus vulgaris--174 2D-image
TetrahydrothiophenDelonix regia, Phaseolus vulgaris--174 2D-image
LiClPhaseolus vulgaris-concentration required to inhibit ATP-diphosphate exchange by 50%: 1.2 M174 2D-image
additional informationMethanocaldococcus jannaschii-activity is not affected by addition of diphosphate650058-
additional informationMethanocaldococcus jannaschii-no inhibition of Cys-tRNAPro formation by L-sulfinic acid, L-cysteic acid, S-methyl L-cysteine, and homocysteine thiolactone652299-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
tRNAMethanocaldococcus jannaschii-stimulates l-cysteine activation 2-3fold651296 2D-image
tRNACysMethanocaldococcus jannaschii-promotes the L-cysteine activation650058 2D-image
additional informationMethanocaldococcus jannaschii-activity is not affected by addition of diphosphate650058-
additional informationMethanothermobacter thermautotrophicus-a complex between ProRS and leucyl-tRNA synthetase, LeuRS, in Methanothermobacter thermautotrophicus enhances tRNAPro aminoacylation, overview674875-

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.28-3,4-dehydro-DL-prolinePhaseolus vulgaris-ATP-diphosphate exchange174 2D-image
0.364-3,4-dehydro-DL-prolineRanunculus bulbosus-ATP-diphosphate exchange174 2D-image
0.5-3,4-dehydro-DL-prolineBeta vulgaris-ATP-diphosphate exchange174 2D-image
0.74-3,4-dehydro-DL-prolineHemerocallis fulva-ATP-diphosphate exchange174 2D-image
0.78-3,4-dehydro-DL-prolineDelonix regia-ATP-diphosphate exchange174 2D-image
2.2-3,4-dehydro-DL-prolineBeta vulgaris-ATP-diphosphate exchange174 2D-image
2.2-3,4-dehydro-DL-prolineParkinsonia aculeata-ATP-diphosphate exchange, L-azetidine-2-carboxylic acid174 2D-image
1.4-3-thiaprolineRattus norvegicus-ATP-diphosphate exchange168 2D-image
1.4-3-thiaprolineConvallaria majalis-3,4-dehydro-DL-proline, , ATP-diphosphate exchange174 2D-image
6.25-4-selenaprolineRattus norvegicus-ATP-diphosphate exchange168 2D-image
55-4-selenaprolineBos taurus-ATP-diphosphate exchange92 2D-image
66-4-thiaprolineEscherichia coli-ATP-diphosphate exchange168 2D-image
0.049-ATPMethanocaldococcus jannaschii-aminoacylation reaction with L-proline, recombinant wild-type enzyme, pH 7.0, 70°C650058 2D-image
0.06-ATPMethanocaldococcus jannaschii-aminoacylation reaction with L-cysteine, recombinant wild-type enzyme, pH 7.0, 70°C650058 2D-image
0.39-ATPMethanocaldococcus jannaschii-ATP-diphosphate exchange reaction with L-cysteine, recombinant wild-type enzyme, pH 7.2, 70°C650058 2D-image
0.465-ATPMethanocaldococcus jannaschii-ATP-diphosphate exchange reaction with L-proline, recombinant wild-type enzyme, pH 7.2, 70°C650058 2D-image
0.6-ATPEscherichia coli--176 2D-image
23cis(exo)-3,4-Methano-L-prolineConvallaria majalis-ATP-diphosphate exchange174 2D-image
4.6-cis(exo)-3,4-Methano-L-prolineDelonix regia-ATP-diphosphate exchange174 2D-image
7.1-cis(exo)-3,4-Methano-L-prolineParkinsonia aculeata-ATP-diphosphate exchange174 2D-image
53-cis-4-hydroxyprolineEscherichia coli-pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation674646 2D-image
55-cis-4-hydroxyprolineEscherichia coli-pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation674646 2D-image
12.5-gamma-thiaprolineRattus norvegicus-ATP-diphosphate exchange168 2D-image
31-L-alanineMethanocaldococcus jannaschii-60°C652154 2D-image
79-L-alanineHomo sapiens-37°C652154 2D-image
140-L-alanineEscherichia coli-37°C652154 2D-image
140-L-alanineEscherichia coli-pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation674646 2D-image
1.43-L-azetidine-2-carboxylic acidPhaseolus vulgaris-ATP-diphosphate exchange174 2D-image
2-L-azetidine-2-carboxylic acidRanunculus bulbosus-ATP-diphosphate exchange174 2D-image
5.3-L-azetidine-2-carboxylic acidHemerocallis fulva-ATP-diphosphate exchange174 2D-image
0.01-L-cysteineClostridium sticklandii, Deinococcus radiodurans-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.02-L-cysteineThermus thermophilus-recombinant enzyme, pH 7.2, 60°C652298 2D-image
0.022-L-cysteineMethanocaldococcus jannaschii-aminoacylation reaction, recombinant wild-type enzyme, pH 7.0, 70°C650058 2D-image
0.03-L-cysteineSaccharomyces cerevisiae-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.05-L-cysteineAquifex aeolicus, Methanothermobacter thermautotrophicus-recombinant enzyme, pH 7.2, 60°C652298 2D-image
0.05-L-cysteineMethanothermobacter thermautotrophicus-ATP-diphosphate exchange, pH 7.5, 35°C653591 2D-image
0.09-L-cysteineMethanocaldococcus jannaschii-ATP-diphosphate exchange reaction, recombinant wild-type enzyme, pH 7.2, 70°C650058 2D-image
0.09-L-cysteineMethanocaldococcus jannaschii-recombinant enzyme, pH 7.2, 60°C652298 2D-image
0.09-L-cysteineMethanocaldococcus jannaschii-ATP-diphosphate exchange reaction, pH 7.5, 35°C653591 2D-image
0.17-L-cysteineEscherichia coli, Rhodopseudomonas palustris-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.18-L-cysteineBorrelia burgdorferi-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.19-L-cysteineCytophaga hutchinsonii-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.2-L-cysteineNovosphingobium aromaticivorans-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.26-L-cysteineMagnetospirillum magnetotacticum-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.137-L-ProPhaseolus vulgaris-ATP-diphosphate exchange174 2D-image
0.182-L-ProDelonix regia-ATP-diphosphate exchange174 2D-image
0.29-L-ProRanunculus bulbosus-ATP-diphosphate exchange174 2D-image
0.43-L-ProParkinsonia aculeata-ATP-diphosphate exchange174 2D-image
0.45-L-ProBeta vulgaris, Convallaria majalis-ATP-diphosphate exchange174 2D-image
0.625-L-ProHemerocallis fulva-ATP-diphosphate exchange174 2D-image
0.012-L-prolineMethanocaldococcus jannaschii-60°C652154 2D-image
0.027-L-prolineMethanocaldococcus jannaschii-aminoacylation reaction, recombinant wild-type enzyme, pH 7.0, 70°C650058 2D-image
0.05-L-prolineClostridium sticklandii-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.06-L-prolineAquifex aeolicus-recombinant enzyme, pH 7.2, 60°C652298 2D-image
0.061-L-prolineMethanothermobacter thermautotrophicus-presence of bovine serum albumine and leucyl-tRNA synthetase, 50°C, pH 7.5662383 2D-image
0.067-L-prolineMethanothermobacter thermautotrophicus-ATP-diphosphate exchange reaction, pH 7.5, 35°C653591 2D-image
0.067-L-prolineMethanothermobacter thermautotrophicus-presence of bovine serum albumine, 50°C, pH 7.5662383 2D-image
0.08-L-prolineCytophaga hutchinsonii-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.11-L-prolineSaccharomyces cerevisiae-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.14-L-prolineMagnetospirillum magnetotacticum, Novosphingobium aromaticivorans-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.15-L-prolineThermus thermophilus-recombinant enzyme, pH 7.2, 60°C652298 2D-image
0.15-L-prolineEscherichia coli-pH 7.5, 37°C, mutant K279A693220 2D-image
0.16-L-prolineDeinococcus radiodurans-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.17-L-prolineBorrelia burgdorferi-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.18-L-prolineHomo sapiens-37°C652154 2D-image
0.25-L-prolineEscherichia coli-37°C652154 2D-image
0.25-L-prolineEscherichia coli-pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation674646 2D-image
0.26-L-prolineMethanothermobacter thermautotrophicus-recombinant enzyme, pH 7.2, 60°C652298 2D-image
0.28-L-prolineMethanocaldococcus jannaschii-recombinant enzyme, pH 7.2, 60°C652298 2D-image
0.28-L-prolineRhodopseudomonas palustris-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.285-L-prolineMethanocaldococcus jannaschii-ATP-diphosphate exchange reaction, recombinant wild-type enzyme, pH 7.2, 70°C650058 2D-image
0.285-L-prolineMethanocaldococcus jannaschii-ATP-diphosphate exchange reaction, pH 7.5, 35°C653591 2D-image
0.29-L-prolineEscherichia coli-recombinant enzyme, pH 7.2, 37°C652298 2D-image
31-L-prolineEscherichia coli-pH 7.5, 37°C, mutant K279A693220 2D-image
50-L-prolineEscherichia coli-pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation674646 2D-image
68-N-Methyl-L-alaninePhaseolus vulgaris-ATP-diphosphate exchange174 2D-image
45-N-methylglycineParkinsonia aculeata-ATP-diphosphate exchange174 2D-image
67-N-methylglycinePhaseolus vulgaris-ATP-diphosphate exchange174 2D-image
100-N-methylglycineHemerocallis fulva-ATP-diphosphate exchange174 2D-image
140-N-methylglycineRanunculus bulbosus-ATP-diphosphate exchange174 2D-image
300-N-methylglycineDelonix regia-approximate value, , ATP-diphosphate exchange174 2D-image
0.12-ProEscherichia coli--176 2D-image
0.3-ProEscherichia coli-wild-type164 2D-image
0.4-ProRattus norvegicus-ATP-diphosphate exchange168 2D-image
0.8-ProEscherichia coli-3-thiaproline, , ATP-diphosphate exchange168 2D-image
1.7-ProEscherichia coli-mutant C443A164 2D-image
2.4-ProEscherichia coli-mutant C443G164 2D-image
3.1-ProEscherichia coli-mutant C443S164 2D-image
20-thiazolidine-4-carboxylic acidPhaseolus vulgaris-ATP-diphosphate exchange174 2D-image
237trans-4-hydroxyprolineEscherichia coli-pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation674646 2D-image
0.0014-tRNAProMethanothermobacter thermautotrophicus-presence of bovine serum albumine and leucyl-tRNA synthetase, 50°C, pH 7.5662383 2D-image
0.002-tRNAProMethanocaldococcus jannaschii-pH 7.0, 55°C, C-terminal deletion mutant661767 2D-image
0.0022-tRNAProMethanocaldococcus jannaschii-pH 7.0, 55°C, wild-type661767 2D-image
0.0022-tRNAProMethanothermobacter thermautotrophicus-presence of leucyl-tRNA synthetase, 50°C, pH 7.5662383 2D-image
0.0024-tRNAProMethanothermobacter thermautotrophicus-presence of bovine serum albumine, 50°C, pH 7.5662383 2D-image
0.0041-tRNAProMethanothermobacter thermautotrophicus-50°C, pH 7.5662383 2D-image
0.131-tRNAProEscherichia coli-pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, aminoacylation674646 2D-image
14.14-tRNAProEscherichia coli-pH 7.0, 37°C, recombinant wild-type enzyme, aminoacylation674646 2D-image
2050L-thiazolidine-4-carboxylic acidDelonix regia-ATP-diphosphate exchange174 2D-image
additional information-additional informationRattus norvegicus--163-
additional information-additional informationMethanothermobacter thermautotrophicus-ProRS and leucyl-tRNA synthetase, LeuRS, interaction kinetics674875-
additional information-additional informationDeinococcus radiodurans-single turnover and burst kinetics, steady-state kinetics, recombinant His-tagged enzyme, overview675395-
additional information-additional informationEscherichia coli-wild-type and mutant enzyme kinetics691088-
additional information-additional informationHomo sapiens, Methanocaldococcus jannaschii--693220-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
3.7-ATPEscherichia coli-mutant C443S, ATP-diphosphate exchange164 2D-image
15-ATPEscherichia coli-mutant C443G, ATP-diphosphate exchange164 2D-image
28-ATPEscherichia coli-mutant C443A, ATP-diphosphate exchange164 2D-image
81-ATPEscherichia coli-wild-type enzyme, ATP-diphosphate exchange164 2D-image
0.056-cis-4-hydroxyprolineEscherichia coli-pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation674646 2D-image
21-cis-4-hydroxyprolineEscherichia coli-pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation674646 2D-image
0.11-L-alanineHomo sapiens-37°C652154 2D-image
1.7-L-alanineEscherichia coli-37°C652154 2D-image
1.7-L-alanineEscherichia coli-pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation674646 2D-image
2-L-alanineMethanocaldococcus jannaschii-60°C652154 2D-image
0.003-L-cysteineSaccharomyces cerevisiae-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.014-L-cysteineDeinococcus radiodurans-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.02-L-cysteineMethanocaldococcus jannaschii-aminoacylation reaction, recombinant wild-type enzyme, pH 7.0, 70°C650058 2D-image
0.02-L-cysteineMethanothermobacter thermautotrophicus-recombinant enzyme, pH 7.2, 60°C652298 2D-image
0.022-L-cysteineEscherichia coli-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.025-L-cysteineRhodopseudomonas palustris-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.04-L-cysteineMethanocaldococcus jannaschii-ATP-diphosphate exchange reaction, recombinant wild-type enzyme, pH 7.2, 70°C650058 2D-image
0.04-L-cysteineThermus thermophilus-recombinant enzyme, pH 7.2, 60°C652298 2D-image
0.065-L-cysteineNovosphingobium aromaticivorans-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.083-L-cysteineCytophaga hutchinsonii-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.09-L-cysteineAquifex aeolicus-recombinant enzyme, pH 7.2, 60°C652298 2D-image
0.11-L-cysteineMagnetospirillum magnetotacticum-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.12-L-cysteineBorrelia burgdorferi-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.19-L-cysteineMethanocaldococcus jannaschii-recombinant enzyme, pH 7.2, 60°C652298 2D-image
0.39-L-cysteineClostridium sticklandii-recombinant enzyme, pH 7.2, 37°C652298 2D-image
0.024-L-prolineEscherichia coli-pH 7.5, 37°C, mutant K279A693220 2D-image
0.09-L-prolineMethanocaldococcus jannaschii-aminoacylation reaction, recombinant wild-type enzyme, pH 7.0, 70°C650058 2D-image
0.23-L-prolineEscherichia coli-pH 7.5, 37°C, mutant K279A693220 2D-image
3.4-L-prolineMethanothermobacter thermautotrophicus-recombinant enzyme, pH 7.2, 60°C652298 2D-image
4.8-L-prolineMethanocaldococcus jannaschii-ATP-diphosphate exchange reaction, recombinant wild-type enzyme, pH 7.2, 70°C650058 2D-image
5.6-L-prolineSaccharomyces cerevisiae-recombinant enzyme, pH 7.2, 37°C652298 2D-image
12-L-prolineEscherichia coli-pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation674646 2D-image
14-L-prolineEscherichia coli, Rhodopseudomonas palustris-recombinant enzyme, pH 7.2, 37°C652298 2D-image
15-L-prolineAquifex aeolicus-recombinant enzyme, pH 7.2, 60°C652298 2D-image
19-L-prolineCytophaga hutchinsonii-recombinant enzyme, pH 7.2, 37°C652298 2D-image
26-L-prolineNovosphingobium aromaticivorans-recombinant enzyme, pH 7.2, 37°C652298 2D-image
32-L-prolineDeinococcus radiodurans-recombinant enzyme, pH 7.2, 37°C652298 2D-image
34-L-prolineBorrelia burgdorferi-recombinant enzyme, pH 7.2, 37°C652298 2D-image
35-L-prolineMagnetospirillum magnetotacticum-recombinant enzyme, pH 7.2, 37°C652298 2D-image
35-L-prolineThermus thermophilus-recombinant enzyme, pH 7.2, 60°C652298 2D-image
60-L-prolineClostridium sticklandii-recombinant enzyme, pH 7.2, 37°C652298 2D-image
63-L-prolineMethanocaldococcus jannaschii-recombinant enzyme, pH 7.2, 60°C652298 2D-image
70-L-prolineEscherichia coli-37°C652154 2D-image
70-L-prolineEscherichia coli-pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation674646 2D-image
80-L-prolineHomo sapiens-37°C652154 2D-image
15-trans-4-hydroxyprolineEscherichia coli-pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation674646 2D-image
0.0091-tRNAProEscherichia coli-pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, aminoacylation674646 2D-image
0.239-tRNAProEscherichia coli-pH 7.0, 37°C, recombinant wild-type enzyme, aminoacylation674646 2D-image
0.4-tRNAProMethanocaldococcus jannaschii-pH 7.0, 55°C, C-terminal deletion mutant661767 2D-image
1.6-tRNAProMethanocaldococcus jannaschii-pH 7.0, 55°C, wild-type661767 2D-image
1.8-tRNAProMethanothermobacter thermautotrophicus-50°C, pH 7.5662383 2D-image
1.8-tRNAProDeinococcus radiodurans-steady-state675395 2D-image
2.9-tRNAProMethanothermobacter thermautotrophicus-presence of bovine serum albumine, 50°C, pH 7.5662383 2D-image
5.1-tRNAProMethanothermobacter thermautotrophicus-presence of leucyl-tRNA synthetase, 50°C, pH 7.5662383 2D-image
6.9-tRNAProMethanothermobacter thermautotrophicus-presence of bovine serum albumine and leucyl-tRNA synthetase, 50°C, pH 7.5662383 2D-image
9.8-tRNAProDeinococcus radiodurans-single turnover overall aminoacylation675395 2D-image
10.8-tRNAProDeinococcus radiodurans-single turnover of the transfer step675395 2D-image
210-L-prolineMethanocaldococcus jannaschii-60°C652154 2D-image
additional information-additional informationEscherichia coli-the rate of AMP formation of K279A ProRS in the presence of alanine is 0.034 s-1, which is at least 20 times faster than the rate of nonenzymatic hydrolysis693220-

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
4.3e-068.8e-055'-O-[N-(L-alanyl)-sulfamoyl]adenosineEscherichia coli-ATP-diphosphate exchange reaction, pH 7.0, 37°C, recombinant wild-type enzyme674646 2D-image
5e-05-prolyl-sulfamoyl-adenylateMethanothermobacter thermautotrophicus-versus L-proline, pH 7.5, 35°C653591 2D-image
2.5e-05-cysteinyl-sulfamoyl-adenylateMethanothermobacter thermautotrophicus-versus L-proline, pH 7.5, 35°C653591 2D-image
additional information-additional informationCandida albicans--650558-

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.101-Delonix regia--174
0.11-Rattus norvegicus--26
0.615-Rattus norvegicus-enzyme form associated with glutamyl-tRNA synthetase163
1.26-Rattus norvegicus-free enzyme form163
1.655-Delonix regia--174
2.45-Rattus norvegicus--165
additional information-Thermus aquaticus--166
additional information-Escherichia coli--176
additional information-Cricetulus griseus--652046
additional information-Escherichia coli-activities of wild-type and mutant enzymes, pre-transfer editing activity, overview674646
additional information-Methanocaldococcus jannaschii, Methanococcus maripaludis, Methanothermobacter thermautotrophicus, Saccharomyces cerevisiae--674646
additional information-Escherichia coli--693220

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7-Thermus aquaticus-Escherichia coli tRNAPro166
7-Methanocaldococcus jannaschii-aminoacylation assay at650058, 652299
7-Methanocaldococcus jannaschii, Methanococcus maripaludis, Methanothermobacter thermautotrophicus, Saccharomyces cerevisiae-assay at674646
7-Escherichia coli, Homo sapiens, Methanocaldococcus jannaschii-assay at693220
7.2-Methanocaldococcus jannaschii-ATP-diphosphate exchange assay at650058
7.2-Aquifex aeolicus, Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Deinococcus radiodurans, Escherichia coli, Magnetospirillum magnetotacticum, Methanocaldococcus jannaschii, Methanothermobacter thermautotrophicus, Novosphingobium aromaticivorans, Rhodopseudomonas palustris, Saccharomyces cerevisiae, Thermus thermophilus-assay at652298
7.2-Methanocaldococcus jannaschii-ATP-diphosphate exchange assay at652299
7.57.8Phaseolus vulgaris, Ranunculus bulbosus-ATP-diphosphate exchange174
7.5-Cricetulus griseus-assay at652046
7.5-Methanocaldococcus jannaschii, Methanothermobacter thermautotrophicus-assay at653591
7.5-Methanothermobacter thermautotrophicus-assay at674875
7.5-Deinococcus radiodurans-assay at675395
7.67.9Hemerocallis fulva-ATP-diphosphate exchange174
7.98.3Beta vulgaris-ATP-diphosphate exchange174
7.9-Phaseolus vulgaris--177
8.48.7Convallaria majalis-ATP-diphosphate exchange174
8.48.8Polygonatum multiflorum-ATP-diphosphate exchange174
8.4-Polygonatum multiflorum--177
8.89.2Parkinsonia aculeata-ATP-diphosphate exchange174
99.4Delonix regia-ATP-diphosphate exchange174

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
69Thermus aquaticus-pH 6.0: about 30% of maximal activity, pH 9.0: about 40% of maximal activity166
6.87.6Escherichia coli-variation of the pH in this range has little effect on activity176

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
22-Methanothermobacter thermautotrophicus-assay at room temperature674875
22-Homo sapiens-assay at room temperature694434
35-Methanocaldococcus jannaschii, Methanothermobacter thermautotrophicus-assay at653591
37-Cricetulus griseus-assay at652046
37-Escherichia coli, Homo sapiens-assay at652154
37-Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Deinococcus radiodurans, Escherichia coli, Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans, Rhodopseudomonas palustris, Saccharomyces cerevisiae-assay at652298
37-Methanocaldococcus jannaschii, Methanococcus maripaludis, Methanothermobacter thermautotrophicus, Saccharomyces cerevisiae-assay at674646
37-Deinococcus radiodurans-assay at675395
37-Escherichia coli, Homo sapiens, Methanocaldococcus jannaschii-assay at693220
50-Methanocaldococcus jannaschii-assay at652299
6065Methanocaldococcus jannaschii-assay at652131
60-Methanocaldococcus jannaschii-assay at652154
60-Aquifex aeolicus, Methanocaldococcus jannaschii, Methanothermobacter thermautotrophicus, Thermus thermophilus-assay at652298
70-Methanocaldococcus jannaschii-assay at650058

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
additional information-Thermus aquaticus-even at 85°C the enzyme retains its specificity towards its cognate substrate166

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
erythroleukemia cellMus musculus--126Manually annotated by BRENDA team
liverOvis aries--161Manually annotated by BRENDA team
liverRattus norvegicus--163, 165, 168, 169, 26Manually annotated by BRENDA team
ovaryCricetulus griseus-cell line CRL-1781652046Manually annotated by BRENDA team
rhizomeConvallaria majalis, Polygonatum multiflorum-apices177Manually annotated by BRENDA team
seedConvallaria majalis, Phaseolus vulgaris, Pisum sativum--177Manually annotated by BRENDA team
skeletal muscleRattus norvegicus--169Manually annotated by BRENDA team
U-937 cellHomo sapiens-monocytic cell culture661440Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
chloroplastPhaseolus vulgaris--9507170Manually annotated by BRENDA team
cytoplasmPhaseolus vulgaris--5737170Manually annotated by BRENDA team
cytoplasmCricetulus griseus-major part, enzyme participates in a multienzyme complex, not as large and stable as the one from nucleus5737652046Manually annotated by BRENDA team
cytoplasmBos taurus--573792Manually annotated by BRENDA team
mitochondrionPhaseolus vulgaris--5739170Manually annotated by BRENDA team
nucleusCricetulus griseus-2.9% of total activity in the cell, enzyme participates in a large and stable multienzyme complex5634652046Manually annotated by BRENDA team
mitochondrionBos taurus--573992Manually annotated by BRENDA team
additional informationRattus norvegicus-the particulate form of the synthetases reflect true association of the enzymes with a high molecular weight cellular component common to both tissues-169Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
2j3l, downloadSCOP (2j3l)CATH (2j3l)Enterococcus faecalis (strain ATCC 700802 / V583)
2j3m, downloadSCOP (2j3m)CATH (2j3m)Enterococcus faecalis (strain ATCC 700802 / V583)
3ial, downloadSCOP (3ial)CATH (3ial)Giardia intestinalis (strain ATCC 50803 / WB clone C6)
1nj8, downloadSCOP (1nj8)CATH (1nj8)Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
1nj1, downloadSCOP (1nj1)CATH (1nj1)Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
1nj2, downloadSCOP (1nj2)CATH (1nj2)Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
1nj5, downloadSCOP (1nj5)CATH (1nj5)Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
1nj6, downloadSCOP (1nj6)CATH (1nj6)Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
2i4l, downloadSCOP (2i4l)CATH (2i4l)Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
2i4m, downloadSCOP (2i4m)CATH (2i4m)Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
2i4n, downloadSCOP (2i4n)CATH (2i4n)Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
2i4o, downloadSCOP (2i4o)CATH (2i4o)Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
105000-Methanocaldococcus jannaschii-gel filtration661767
113000-Methanothermobacter thermautotrophicus-gel filtration661767
127000-Thermus aquaticus-gel filtration166
133000-Rattus norvegicus-free form, gel filtration163
155000-Bos taurus-cytoplasmic, gel filtration92
162000-Bos taurus-mitochondrial, gel filtration92
172000-Homo sapiens--694123

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
dimerRattus norvegicus-2 * 60000, SDS-PAGE163
dimerThermus aquaticus-2 * 62000, SDS-PAGE166
dimerOryctolagus cuniculus-bifunctional enzyme651917
dimerMethanocaldococcus jannaschii-2 * 53300, calcultaed661767
dimerMethanothermobacter thermautotrophicus-2 * 55700, calculated661767
additional informationMus musculus-enzyme is part of a high molecular mass aminoacyl-tRNA synthetase complex, which has a coherent structure that can be visualized by electron microscopy126
additional informationMammalia-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 activities161
additional informationRattus norvegicus-5SrRNA is probably present as a 5SrRNA-L5 protein complex in the macromolucular aminoacyl-tRNA synthetase complexes in rat liver26
additional informationOryctolagus cuniculus-multienzyme complex organization and structure by visualization of immunologically stained sites651917
additional informationHomo sapiens-glutamyl-prolyl-tRNA synthetase is a component of the interferon gamma-activated inhibitor of translation complex661440
additional informationMethanothermobacter thermautotrophicus-enzyme in vivo interacts with leucyl-tRNA synthetase, increasing its catalytic efficiency 5fold662383
additional informationHaemophilus influenzae-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 complexes662414
additional informationEnterococcus faecalisQ831W7comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, overview677155
additional informationRhodopseudomonas palustrisQ6N5P6comparison 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, overview677155
additional informationHomo sapiens-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 domain694123

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
phosphoproteinHomo sapiens-glutamyl-prolyl-tRNA synthetase is phosphorylated in response to interferon-gamma661440

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
recombinant selenomethionine-labelled enzyme, expressed in Escherichia coliAeropyrum pernix-660617
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, 12-25°C, a few days, X-ray diffraction structure determination at 3.2 A resolution, and analysisMethanocaldococcus jannaschii-653591
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, 20°C, X-ray diffraction structure determination at 2.55-3.1 A, and analysisMethanothermobacter thermautotrophicus-653591
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 resolutionRhodopseudomonas palustrisQ6N5P6677155
crystal structure analysisThermus thermophilus-651296
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 analysisThermus thermophilus-649132
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 resolutionThermus thermophilus-652859
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 analysisThermus thermophilus-653918
X-ray diffraction structure determination at 2.43-2.85 A of crystals formed by the free enzyme or the enzyme complexed with tRNAProThermus thermophilus-650975

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
67.8Thermus aquaticus-90°C, 30 min, enzyme contains considerable activity, no activity retained after exposure to 95°C166

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
2-Delonix regia, Phaseolus vulgaris-complete loss of activity after 30 min, in absence of glycerol and mercaptoethanol171
25-Delonix regia, Parkinsonia aculeata-50% loss of ATP-diphosphate exchange activity after 5 min, without stabilizing reagent174
51-Ranunculus bulbosus-50% loss of ATP-diphosphate exchange activity after 5 min, without stabilizing reagent174
55-Parkinsonia aculeata-50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.002 mM ATP174
56-Delonix regia-50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.002 mM ATP174
58-Parkinsonia aculeata-50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.02 mM Pro174
59-Delonix regia-50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.02 mM Pro174
62-Phaseolus vulgaris-50% loss of activity after 5 min in Tris-HCl buffer177
65-Phaseolus vulgaris-50% loss of ATP-diphosphate exchange activity after 5 min, without stabilizing reagent174
67-Delonix regia, Parkinsonia aculeata-50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.002 mM ATP + 0.02 mM Pro174
73-Phaseolus vulgaris-50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.002 mM ATP174
78-Phaseolus vulgaris-50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.002 mM ATP + 0.02 mM Pro174
90-Thermus aquaticus-pH 6-7.8, 30 min, enzyme retains considerable activity166
95-Thermus aquaticus-pH 6-7.8, 30 min, unstable166
additional information-Delonix regia, Phaseolus vulgaris-ATP, Pro and several Pro analogues prevent inactivation at 0°C; inclusion of a polyol together with the sulfhydryl-reducing reagent appears to synergistically enhance the stability on storage at 2°C; 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 A2C171
additional information-Delonix regia-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 45°C and 50°C 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 inactivation173
additional information-Phaseolus vulgaris-above 60°C, 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 45°C and 50°C respectively; furan and tetrahydrothiophen, protect only in presence of ATP against thermal inactivation; several analogues of Pro protect against thermal inactivation173

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
at pH 6.5, 0.01 mM Mg2+ stabilizes against thermal inactivationDelonix regia-173
at pH 8, in absence of Mg2+, ATP does not protect against thermal inactivationDelonix regia-173
ATP, Pro and several Pro analogues prevent inactivation at 0°CDelonix regia-171
bovine serum albumin and glycerol partially protect against thermal denaturation at 45°C and 50°C respectivelyDelonix regia-173
furan and tetrahydrothiophen, only in presence of ATP protect against thermal inactivationDelonix regia-173
inclusion of a polyol together with the sulfhydryl-reducing reagent appears to synergistically enhance the stability on storage at 2°CDelonix regia-171
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 70°C and 40°CDelonix regia-174
mercaptoethanol or DTT stabilizes against heat inactivationDelonix regia-173
Pro or ATP markedly stabilizes against heat inactivationDelonix regia-173, 174
rapid and reversible photoinactivation in absence of methylene blue. ATP or Pro protectsDelonix regia-171
several analogues of Pro protect against thermal inactivationDelonix regia-173, 174
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 respectivelyDelonix regia-171
Pro or ATP markedly stabilizes against heat inactivationParkinsonia aculeata-174
above 60°C, little protection by bovine serum albumin and glycerolPhaseolus vulgaris-173
at pH 8, in absence of Mg2+, ATP does not protect against thermal inactivationPhaseolus vulgaris-173
ATP, Pro and several Pro analogues prevent inactivation at 0°CPhaseolus vulgaris-171
bovine serum albumin and glycerol partially protect against thermal denaturation at 45°C and 50°C respectivelyPhaseolus vulgaris-173
furan and tetrahydrothiophen, only in presence of ATP protect against thermal inactivationPhaseolus vulgaris-173
inclusion of a polyol together with the sulfhydryl-reducing reagent appears to synergistically enhance the stability on storage at 2°CPhaseolus vulgaris-171
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 70°C and 40°CPhaseolus vulgaris-174
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 lightPhaseolus vulgaris-172
Pro or ATP markedly stabilizes against heat inactivationPhaseolus vulgaris-173, 174
several analogues of Pro protect against thermal inactivationPhaseolus vulgaris-173, 174
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 respectivelyPhaseolus vulgaris-171

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
0.1 M Tris-maleate KOH buffer, pH 7.0, about 80% loss of activity in ATP-diphosphate exchangeDelonix regia-171
0.1 M Tris-maleate KOH buffer, pH 8.0, about 85% loss of activity in ATP-diphosphate exchangeDelonix regia-171
-20°C, pH 6.8, 40% v/v glycerol, enzyme concentrated by ultrafiltrationThermus aquaticus-166

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
recombinant His-tagged enzyme from overexpression in Escherichia coliAquifex aeolicus, Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Deinococcus radiodurans-652298
-Delonix regia-174
recombinant enzyme from Escherichia coli strain M15 by ammonium sulfate fractionation and anion exchange chromatographyEnterococcus faecalisQ831W7677155
-Escherichia coli-176
recombinant His-tagged enzyme from overexpression in Escherichia coliEscherichia coli, Magnetospirillum magnetotacticum-652298
recombinant enzyme from Escherichia coliMethanocaldococcus jannaschii-652131
recombinant from Escherichia coliMethanocaldococcus jannaschii-651296
recombinant His-tagged enzyme from expression in Escherichia coliMethanocaldococcus jannaschii-653591
recombinant His-tagged enzyme from overexpression in Escherichia coliMethanocaldococcus jannaschii-652298
recombinant His-tagged wild-type and C-terminally truncated enzymes from overexpressing Escherichia coliMethanocaldococcus jannaschii-652299
recombinant His-tagged wild-type and mutants from overexpressing Escherichia coli BL21Methanocaldococcus jannaschii-650058
recombinant His-tagged enzyme from Escherichia coliMethanothermobacter thermautotrophicus-653591
recombinant His-tagged enzyme from overexpression in Escherichia coliMethanothermobacter thermautotrophicus-652298
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, overviewMethanothermobacter thermautotrophicus-674875
recombinant His-tagged enzyme from overexpression in Escherichia coliNovosphingobium aromaticivorans-652298
-Phaseolus vulgaris-174, 177
-Polygonatum multiflorum-177
-Rattus norvegicus-165, 26
2 forms: a free form and a form noncovalently associated with glutamyl-tRNA synthetaseRattus norvegicus-163
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatographyRhodopseudomonas palustrisQ6N5P6677155
recombinant His-tagged enzyme from overexpression in Escherichia coliRhodopseudomonas palustris, Saccharomyces cerevisiae-652298
-Thermus aquaticus-166
recombinant His-tagged enzyme from overexpression in Escherichia coliThermus thermophilus-652298

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expression of the enzyme in Escherichia coli strain M15Enterococcus faecalisQ831W7677155
gene proS, overexpression of wild-type and mutant His-tagged ProRSEscherichia coli-674646
expression of C-terminally His-tagged, full-length EPRSHomo sapiens-694123
expression of the His-tagged enzyme in Escherichia coli BL21(DE3)Methanocaldococcus jannaschii-652131
gene proS, expression in Escherichia coli strain BL21(DE3)Methanocaldococcus jannaschii-674646
gene proS, overexpression in Escherichia coliMethanocaldococcus jannaschii-651296
overexpression of wild-type and C-terminally truncated enzymes as His-tagged proteins in Escherichia coliMethanocaldococcus jannaschii-652299
gene proS, expression in Escherichia coli strain SG13009Methanococcus maripaludis-674646
expression as His-tagged enzyme in Escherichia coliMethanothermobacter thermautotrophicus-653591
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)Methanothermobacter thermautotrophicus-674875
gene proS, expression in Escherichia coli strain BL21(DE3)Methanothermobacter thermautotrophicus-674646
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)Rhodopseudomonas palustrisQ6N5P6677155
gene proS, overexpression of His-tagged wild-type ProRS and truncation mutant ScDELTA183Saccharomyces cerevisiae-674646

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
C443AEscherichia coli-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, 80fold164
C443GEscherichia coli-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, 80fold164
C443SEscherichia coli-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, 80fold164
D350AEscherichia coli-site-directed mutagenesis, subdomain III mutant, residual remaining aminoaclyation activity, no pre-transfer editing activity650167
D378AEscherichia coli-site-directed mutagenesis, subdomain III mutant, reduced aminoaclyation and pre-transfer editing activity650167
D386AEscherichia coli-site-directed mutagenesis, subdomain III mutant, reduced aminoaclyation and pre-transfer editing activity650167
D394AEscherichia coli-site-directed mutagenesis, subdomain III mutant, reduced aminoaclyation and pre-transfer editing activity650167
H369AEscherichia coli-site-directed mutagenesis, subdomain III mutant, highly reduced reduced aminoaclyation and pre-transfer editing activity, deacetylates Pro-tRNAPro650167
H369CEscherichia coli-site-directed mutagenesis, subdomain III mutant, highly reduced reduced aminoaclyation and pre-transfer editing activity, deacetylates Pro-tRNAPro650167
K279AEscherichia coli-site-directed mutagenesis, subdomain II mutant, reduced aminoaclyation and pre-transfer editing activity650167
R144KEscherichia coli-site-directed mutagenesis, the mutant shows 480fold reduced activity compared to the wild-type enzyme691088
R144LEscherichia coli-site-directed mutagenesis, the mutant shows 870fold reduced activity compared to the wild-type enzyme691088
R146CEscherichia coli-site-directed mutagenesis, the mutant shows 79fold reduced activity compared to the wild-type enzyme691088
T257AEscherichia coli-site-directed mutagenesis, subdomain I mutant, reduced aminoaclyation and pre-transfer editing activity650167
V143CEscherichia coli-site-directed mutagenesis, the mutant shows 3fold reduced activity compared to the wild-type enzyme691088
A57GHomo sapiens-site-directed mutagenesis, the A57G mutation introduces a BstBI restriction site within the gene, but has no effect on catalytic activity694434
E103AMethanocaldococcus jannaschii-site-directed mutagenesis, unaltered thermostability, no remaining prolylation activity, 5% remaining cysteinylation activity compared to the wild-type enzyme650058
P100AMethanocaldococcus jannaschii-site-directed mutagenesis, unaltered thermostability, loss of 90% cysteinylation activity, unaltered prolylation activity compared to the wild-type enzyme650058
K279AEscherichia coli-site-directed mutagenesis693220
additional informationEscherichia coli-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-M1S674646
E103AMethanocaldococcus jannaschii-abolished activity with L-proline651296
additional informationMethanocaldococcus jannaschii-the C-terminally truncated enzyme is 3fold less active with L-cysteine and 10fold less active with L-alanine compared too the wild-type enzyme652299
additional informationMethanocaldococcus jannaschii-C-terminal deletion mutant lacking last 50 amino acids, little effect on kinetic parameters661767
P100AMethanocaldococcus jannaschii-highly reduced activity with L-cysteine651296
additional informationMethanococcus maripaludis-the dual-specific enzyme is sufficient for Cys-tRNACys production in a mutant disrupted in the gene encoing the canonical CysRS651296
additional informationSaccharomyces cerevisiae-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, overview674646

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
pharmacologyEscherichia coli-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 tRNAPro652154
pharmacologyMethanocaldococcus jannaschii-enzyme is a target for design of antibiotics targeting the active site since eukaryotic enzyme types are not able to edit misactivated alanine on tRNAPro652154

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
26Ogata, K.; Kurahashi, A.; Tanaka, S.; Ohsue, H.; Terao, K.Occurence of 5SrRNA in high molecular weight complexes of aminoacyl-tRNA synthetases in a rat liver supernatantJ. Biochem.1101030-10361991Rattus norvegicus PubMed
92Walker, E.J.; Treacy, G.B.; Jeffrey, P.D.Molecular weights of mitochondrial and cytoplasmic aminoacyl-tRNA synthetases of beef liver and their complexesBiochemistry221934-19411983Bos taurus PubMed
126Norcum, M.T.Isolation and electron microscopic characterization of the high molecular mass aminoacyl-tRNA synthetase complex from murine erythroleukemia cellsJ. Biol. Chem.26415043-150511989Mus musculus PubMed
160Heacock, D.; Forsyth, C.J.; Shiba, K.; Musier-Forsyth, K.Synthesis and aminoacyl-tRNA synthetase inhibitory activity of prolyl adenylate analogsBioorg. Chem.24273-2891996Escherichia coli-
161Kerjan, P.; Triconnet, M.; Waller, J.P.Mammalian prolyl-tRNA synthetase corresponds to the approximately 150 kDa subunit of the high-Mr aminoacyl-tRNA synthetase complexBiochimie74195-2051992Homo sapiens, Mammalia, Ovis aries PubMed
163Ting, S.M.; Bogner, P.; Dignam, J.D.Isolation of prolyl-tRNA synthetase as a free form and as a form associated with glutamyl-tRNA synthetaseJ. Biol. Chem.26717701-177091992Rattus norvegicus PubMed
164Stehlin, C.; Heacock, D.H.; Liu, H.; Musier-Forsyth, K.Chemical modification and site-directed mutagenesis of the single cysteine in motif 3 of class II Escherichia coli prolyl-tRNA synthetaseBiochemistry362932-29381997Escherichia coli PubMed
165Bianchi, C.; Perego R.; Del Monte, U.Polypeptide composition of the 8S form of prolyl-tRNA synthetase from rat liverBiochem. Biophys. Res. Commun.1871071-10761992Rattus norvegicus PubMed
166Rivera, J.A.; Wang, Q.S.; Wong, J.T.F.A highly thermostable proline:tRNA ligase from Thermus aquaticus. Purification and enzyme-tRNA recognition at elevated temperaturesCan. J. Biochem. Cell Biol.62507-5151984Thermus aquaticus PubMed
168Busiello, V.; Di Girolamo, M.; Cini, C.; De Marco, C.beta-Selenaproline as competitive inhibitor of proline activationBiochim. Biophys. Acta606347-3521980Escherichia coli, Rattus norvegicus PubMed
169Arbeeny, C.M.; Briden, K.L.; Stirewalt, W.S.The activity and sedimentation properties of the aminoacyl-tRNA synthetases of rat skeletal muscleBiochim. Biophys. Acta564191-2011979Rattus norvegicus PubMed
170Jeannin, G.; Burkard, G.; Weil, J.H.Aminoacylation of Phaseolus vulgaris cytoplasmic, chloroplastic and mitochondrial tRNAsPro and tRNAsLys by homologous and heterologous enzymesBiochim. Biophys. Acta44224-311976Escherichia coli, Phaseolus vulgaris PubMed
171Norris, R.D.; Fowden, L.Cold-lability of prolyl-tRNA synthetase from higher plantsPhytochemistry131677-16871974Delonix regia, Phaseolus vulgaris-
172Norris, R.D.; Fowden, L.Pro-tRNA synthetase from Phaseolus aureus and Delonix regiaPhytochemistry122829-28411973Delonix regia, Phaseolus vulgaris-
173Norris, R.D.; Fowden, L.A Comparison of the thermal stability and substrate binding constants of prolyl-tRNA synthetase from Phaseolus aureus and Delonix regiaPhytochemistry122109-21211973Delonix regia, Phaseolus vulgaris-
174Norris, R.D.; Fowden, L.Substrate discrimination by prolyl-tRNA synthetase from various higher plantsPhytochemistry112921-29351972Beta vulgaris, Convallaria majalis, Delonix regia, Hemerocallis fulva, Parkinsonia aculeata, Phaseolus vulgaris, Polygonatum multiflorum, Ranunculus bulbosus-
175Papas, T.S.; Mehler, A.H.Kinetic studies of the prolyl transfer ribonucleic acid synthetase of Escherichia coli. Order of addition of substrates and release of productsJ. Biol. Chem.2465924-59281971Escherichia coli PubMed
176Norton, S.J.Purification and properties of the prolyl RNA synthetase of Escherichia coliArch. Biochem. Biophys.106147-1521964Escherichia coli PubMed
177Peterson, P.J.; Fowden, L.Purification, properties and comparative specificities of the enzyme prolyl-transfer ribonucleic acid synthetase from Phaseolus aureus and Polygonatum multiflorumBiochem. J.97112-1241965Asparagus officinalis, Convallaria majalis, Phaseolus vulgaris, Pisum sativum, Polygonatum multiflorum PubMed
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650058Stathopoulos, C.; Jacquin-Becker, C.; Becker, H.D.; Li, T.; Ambrogelly, A.; Longman, R.; Soll, D.Methanococcus jannaschii prolyl-cysteinyl-tRNA synthetase possesses overlapping amino acid binding sitesBiochemistry4046-522001Methanocaldococcus jannaschii PubMed
650167Wong, F.C.; Beuning, P.J.; Nagan, M.; Shiba, K.; Musier-Forsyth, K.Functional role of the prokaryotic proline-tRNA synthetase insertion domain in amino acid editingBiochemistry417108-71152002Escherichia coli PubMed
650558Yu, X.Y.; Hill, J.M.; Yu, G.; Yang, Y.; Kluge, A.F.; Keith, D.; Finn, J.; Gallant, P.; Silverman, J.; Lim, A.A series of quinoline analogues as potent inhibitors of C. albicans prolyl tRNA synthetaseBioorg. Med. Chem. Lett.11541-5442001Candida albicans, Homo sapiens PubMed
650975Yaremchuk, A.; Cusack, S.; Tukalo, M.Crystal structure of a eukaryote/archaeon-like protyl-tRNA synthetase and its complex with tRNAPro(CGG)EMBO J.194745-47582000Thermus thermophilus PubMed
651296Jacquin-Becker, C.; Ahel, I.; Ambrogelly, A.; Ruan, B.; Soll, D.; Stathopoulos, C.Cysteinyl-tRNA formation and prolyl-tRNA synthetaseFEBS Lett.51434-362002Giardia intestinalis, Methanocaldococcus jannaschii, Methanococcus maripaludis, Thermus thermophilus PubMed
651917Norcum, M.T.; Dignam, J.D.Immunoelectron microscopic localization of glutamyl-/prolyl-tRNA synthetase within the eukaryotic multisynthetase complexJ. Biol. Chem.27412205-122081999Oryctolagus cuniculus PubMed
652046Nathanson, L.; Deutscher, M.P.Active aminoacyl-tRNA synthetases are present in nuclei as a high molecular weight multienzyme complexJ. Biol. Chem.27531559-315622000Cricetulus griseus PubMed
652131Burke, B.; Lipman, R.S.A.; Shiba, K.; Musier-Forsyth, K.; Hou, Y.M.Divergent adaptation of tRNA recognition by Methanococcus jannaschii prolyl-tRNA synthetaseJ. Biol. Chem.27620286-202912001Methanocaldococcus jannaschii PubMed
652154Beuning, P.J.; Musier-Forsyth, K.Species-specific differences in amino acid editing by class II prolyl-tRNA synthetaseJ. Biol. Chem.27630779-307852001Escherichia coli, Homo sapiens, Methanocaldococcus jannaschii PubMed
652298Ahel, I.; Stathopoulos, C.; Ambrogelly, A.; Sauerwald, A.; Toogood, H.; Hartsch, T.; Soll, D.Cysteine activation is an inherent in vitro property of prolyl-tRNA synthetasesJ. Biol. Chem.27734743-347482002Aquifex aeolicus, Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Deinococcus radiodurans, Escherichia coli, Magnetospirillum magnetotacticum, Methanocaldococcus jannaschii, Methanothermobacter thermautotrophicus, Novosphingobium aromaticivorans, Rhodopseudomonas palustris, Saccharomyces cerevisiae, Thermus thermophilus PubMed
652299Ambrogelly, A.; Ahel, I.; Polycarpo, C.; Bunjun-Srihari, S.; Krett, B.; Jacquin-Becker, C.; Ruan, B.; Kohrer, C.; Stathopoulos, C.; RajBhandary, U.L.; Soll, D.Methanocaldococcus jannaschii prolyl-tRNA synthetase charges tRNA(Pro) with cysteineJ. Biol. Chem.27734749-347542002Methanocaldococcus jannaschii PubMed
652859Yaremchuk, A.; Tukalo, M.; Grotli, M.; Cusack, S.A succession of substrate induced conformational changes ensures the amino acid specificity of Thermus thermophilus prolyl-tRNA synthetase: comparison with histidyl-tRNA synthetaseJ. Mol. Biol.309989-10022001Thermus thermophilus PubMed
653591Kamtekar, S.; Kennedy, W.D.; Wang, J.; Stathopoulos, C.; Soll, D.; Steitz, T.A.The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetasesProc. Natl. Acad. Sci. USA1001673-16782003Methanocaldococcus jannaschii, Methanothermobacter thermautotrophicus PubMed
653918Cusack, S.; Yaremchuk, A.; Krikliviy, I.; Tukalo, M.tRNAPro anticodon recognition by Thermus thermophilus prolyl-tRNA synthetaseStructure6101-1081998Thermus thermophilus PubMed
660617Murayama, K.; Kato-Murayama, M.; Katsura, K.; Uchikubo-Kamo, T.; Yamaguchi-Hirafuji, M.; Kawazoe, M.; Akasaka, R.; Hanawa-Suetsugu, K.; Hori-Takemoto, C.; Terada, T.; Shirouzu, M.; Yokoyama, S.Structure of a putative trans-editing enzyme for prolyl-tRNA synthetase from Aeropyrum pernix K1 at 1.7 A resolutionActa Crystallogr. Sect. F6126-292005Aeropyrum pernix PubMed
661440Sampath, P.; Mazumder, B.; Seshadri, V.; Gerber, C.A.; Chavatte, L.; Kinter, M.; Ting, S.M.; Dignam, J.D.; Kim, S.; Driscoll, D.M.; Fox, P.L.Noncanonical function of glutamyl-prolyl-tRNA synthetase: Gene-specific silencing of translationCell119195-2082004Homo sapiens PubMed
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662383Praetorius-Ibba, M.; Rogers, T.E.; Samson, R.; Kelman, Z.; Ibba, M.Association between Archaeal prolyl- and leucyl-tRNA synthetases enhances tRNA(Pro) aminoacylationJ. Biol. Chem.28026099-261042005Methanothermobacter thermautotrophicus PubMed
662414An, S.; Musier-Forsyth, K.Cys-tRNA(Pro) editing by Haemophilus influenzae YbaK via a novel synthetase.YbaK.tRNA ternary complexJ. Biol. Chem.28034465-344722005Haemophilus influenzae PubMed
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693908Wei, M.; Yang, Y.; Niu, M.; Desfosse, L.; Kennedy, R.; Musier-Forsyth, K.; Kleiman, L.Inability of HIV-1 produced in murine cells to selectively incorporate primer tRNALys3J. Virol.8212049-120592008Moloney murine leukemia virus PubMed
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LINKS TO OTHER DATABASES (specific for EC-Number 6.1.1.15)
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Protein Mutant Database
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