Any feedback?
No. of entries
Information on EC 6.1.1.9 - valine-tRNA ligase
for references in articles please use BRENDA:EC6.1.1.9
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 6 Ligases
6.1 Forming carbon-oxygen bonds
6.1.1 Ligases forming aminoacyl-tRNA and related compounds
6.1.1.9 valine-tRNA ligase
The enzyme appears in viruses and cellular organisms
- 6.1.1.9
- synthetases
- aminoacylation
- aminoacyl-trna
-
valylation
-
isoleucyl-trna
-
anticodon
- ilers
-
turnip
-
noncognate
- leucyl-trna
-
mischarged
-
trna-like
-
isoleucyl
-
misacylated
-
misactivated
-
post-transfer
-
l-shaped
-
aarss
- phenylalanyl-trna
-
threonylation
- trnaile
- cysrs
-
atp-ppi
- medicine
showSynonyms
valyl-trna synthetase, valrs, glp-4, val-trna synthetase, valyl-transfer rna synthetase, osvalrs2, valine-trna ligase, valyl-trna ligase, valyl transfer ribonucleic acid synthetase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G7a
Synthetase, valyl-transfer ribonucleate
Val-tRNA synthetase
Valine transfer ribonucleate ligase
Valine translase
Valine--tRNA ligase
ValRS
valS
Valyl transfer ribonucleic acid synthetase
Valyl-transfer ribonucleate synthetase
Valyl-transfer RNA synthetase
Valyl-tRNA ligase
Valyl-tRNA synthetase
VARS
G7a
-
-
-
-
Synthetase, valyl-transfer ribonucleate
-
-
-
-
Valine transfer ribonucleate ligase
-
-
-
-
Valine translase
-
-
-
-
Valine--tRNA ligase
-
-
-
-
ValRS
-
-
-
-
Valyl transfer ribonucleic acid synthetase
-
-
-
-
Valyl-transfer ribonucleate synthetase
-
-
-
-
Valyl-transfer RNA synthetase
-
-
-
-
Valyl-tRNA ligase
-
-
-
-
Valyl-tRNA synthetase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal
-
-
-
-
ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal
pre- and post-transfer editing mechanism, mechanism, active site/editing site
-
ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal
tRNAVal 3'-end, and a purine at position 76, is crucial for substrate editing mechanism
-
ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal
substrate binding mechanism, bases A73 and C75 are involved in the tRNA substrate recognition and editing reaction
-
ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal
Lys593 and Lys554 are in the active site binding valine or threonine, part of the 554KMSKS558 consensus sequence, mechanism, determination of diverse amino acid residues of the enzyme molecule involved in substrate binding, Lys277 plays a crucial role in the fidelity of tRNA aminoacylation by the enzyme, nucleophilic attack of misacylated tRNA in the diting site of the enzyme
-
ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal
mechanism and structural basis of molecular interactions of the enzyme with the C34A35C36 anticodon for tRNAVal recognition by the enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Aminoacylation
esterification
Aminoacylation
-
-
-
-
esterification
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
tRNA charging
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-valine:tRNAVal ligase (AMP-forming)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9023-47-6
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-chloroadenosine 5'-triphosphate + L-valine + tRNAVal
2-chloroadenosine 5'-monophosphate + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + DL-2-amino-3-chlorobutyrate + tRNAVal
AMP + diphosphate + DL-2-amino-3-chlorobutyryl-tRNAVal
-
Substrates: as effective as valine
Products: -
Products: -
?
ATP + DL-2-aminobutyrate + tRNAVal
AMP + diphosphate + DL-2-aminobutyryl-tRNAVal
-
Substrates: 30% of the activity with valine
Products: -
Products: -
?
ATP + DL-allo-2-amino-3-chlorobutyrate + tRNAVal
AMP + diphosphate + DL-allo-2-amino-3-chlorobutyryl-tRNAVal
-
Substrates: 15% of the activity with valine
Products: -
Products: -
?
ATP + DL-threonine + tRNAVal
AMP + diphosphate + DL-threonyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-isoleucine + tRNAVal
AMP + diphosphate + L-isoleucyl-tRNAVal
-
Substrates: very low activity
Products: -
Products: -
?
ATP + L-norvaline + tRNANva
AMP + diphosphate + L-norvalyl-tRNANva
-
Substrates: -
Products: -
Products: -
?
ATP + L-threonine + tRNAVal
?
-
Substrates: 1 step performance of an originally two-step reaction, the enzyme can hardly differentiate between the cognate amino acid valine and others, especially threonine, to minimize misaminoacetylation the enzyme performs a proofreading, socalled editing reaction at a second active site, which is dependent on the presence of cognate tRNAVal whose 3'-end is involved in the editing reaction, a majority of editing by the enzyme entails prior charging of the tRNA, misacylated tRNA is a transient intermediate in the editing reaction
Products: -
Products: -
?
ATP + L-valine + tRNAVal,3' 2-aminopurine
AMP + diphosphate + L-valyl-tRNAVal, 3' 2-aminopurine
-
Substrates: mutant tRNAVal with 3'-terminal 2-aminopurine base analogue substitution
Products: -
Products: -
?
ATP + L-valine + tRNAVal,3' inosine
AMP + diphosphate + L-valyl-tRNAVal, 3' inosine
-
Substrates: mutant tRNAVal with 3'-terminal inosine base analogue substitution
Products: -
Products: -
?
ATP + L-valine + tRNAVal,3' isoguanosine
AMP + diphosphate + L-valyl-tRNAVal, 3' isoguanosine
-
Substrates: mutant tRNAVal with 3'-terminal isoguanosine base analogue substitution
Products: -
Products: -
?
ATP + L-valine + tRNAVal,3' purine riboside
AMP + diphosphate + L-valyl-tRNAVal, 3' purine riboside
-
Substrates: mutant tRNAVal with 3'-terminal purine riboside base analogue substitution
Products: -
Products: -
?
formycin 5'-triphosphate + L-valine + tRNAVal
formycin 5'-monophosphate + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
L-threonyl-tRNAVal
L-threonine + tRNAVal
-
Substrates: substrate bound to the enzyme, intermediate in the posttransfer editing reaction
Products: -
Products: -
ir
L-threonyl-tRNAVal-AMP
L-threonine + tRNAVal + AMP
-
Substrates: substrate bound to the enzyme, intermediate in the pretransfer editing reaction
Products: -
Products: -
ir
tubercidin 5'-triphosphate + L-valine + tRNAVal
tubercidin 5'-monophosphate + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-threonine + tRNAVal
AMP + diphosphate + L-threonyl-tRNAVal
-
Substrates: noncognate isosteric substrate, low activity, posttransfer editing occurs
Products: -
Products: -
ir
ATP + L-threonine + tRNAVal
AMP + diphosphate + L-threonyl-tRNAVal
-
Substrates: 28% of the activity with valine
Products: -
Products: -
?
ATP + L-valine + tRNAiMet,GAC mutant
AMP + diphosphate + L-valyl-tRNAiMet,GAC mutant
-
Substrates: anticodon CAU to GAC initiator tRNA mutant, i.e. G34C36 mutant, is aminoacylated in vitro and in vivo, its anticodon sequence corresponds to the one of tRNAVal
Products: -
Products: -
?
ATP + L-valine + tRNAiMet,GAC mutant
AMP + diphosphate + L-valyl-tRNAiMet,GAC mutant
-
Substrates: anticodon CAU to GAC initiator tRNA mutant, i.e. G34C36 mutant, is aminoacylated in vitro and in vivo, its anticodon sequence corresponds to the one of tRNAVal
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: enzyme contains 2 tRNA binding sites involved in aminoacetylation and editing reactions, misacetylated tRNAVal is edited by the enzyme to avoid accumulation, the 3'-end of the tRNA is involved
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: two-step reaction, covalent valylation of the enzyme
Products: -
Products: -
ir
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: two-step reaction, the enzyme can hardly differentiate between the cognate amino acid valine and others, especially threonine, to minimize misaminoacetylation the enzyme performs a proofreading, socalled editing reaction at a second active site, which is dependent on the presence of cognate tRNAVal whose 3'-end is involved in the editing reaction, a majority of editing by the enzyme entails prior charging of the tRNA, misacylated tRNA is a transient intermediate in the editing reaction
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
ir
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
Substrates: charging of tRNAVal by ValS occurs in two steps: firstly, valine is activated with ATP to form Val-AMP leading to the release of pyrophosphate, and secondly, the valine is then transferred to the tRNAVal to form Val-tRNAVal, with a concomitant release of AMP
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: chloroplastic enzyme charges E. coli tRNA and not yeast tRNA, cytoplasmic enzyme is able to aminoacylate yeast tRNA but not E. coli tRNA
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: tRNA recognition mechanism, the anticodon sequence is important for the aminoacylation
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: tRNA recognition mechanism, the anticodon sequence is important for the aminoacylation
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: tRNA from E. coli or Mycobacterium smegmatis
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: the enzyme is strictly specific for the cognate L-valine and discriminates from the larger L-isoleucine and L-threonine by the tRNA-dependent double sieve mechanism
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: wild-type tRNAVal substrate and mutant forms, the anticodon loop structure of the tRNA is important for substrate recognition
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal(GAC)
AMP + diphosphate + L-valyl-tRNAVal(GAC)
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal(GAC)
AMP + diphosphate + L-valyl-tRNAVal(GAC)
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal(UAC)
AMP + diphosphate + L-valyl-tRNAVal(UAC)
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal(UAC)
AMP + diphosphate + L-valyl-tRNAVal(UAC)
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal(UAC-2)
AMP + diphosphate + L-valyl-tRNAVal(UAC-2)
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal(UAC-2)
AMP + diphosphate + L-valyl-tRNAVal(UAC-2)
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalytic activity with L-valine and diverse tRNA analogues with functional group substitutions at the terminal nucleoside of the 3'-end, some of which stimulate the editing reaction, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity with diverse Escherichia coli tRNAs and tRNA mutants in editing and aminoacylation reaction, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also performs the ATP-diphosphate exchange reaction, labeling of the enzyme by methionyladenylate, determination of lysine residues involved in binding
Products: -
Products: -
?
additional information
?
-
-
Substrates: tRNAVal variants in position 76, i.e. U76, C76, G76 activate the editing activity, misactivation of threonine, alanine, serine, cysteine, alpha-aminobutyrate, and to a low extent of norvaline activates the editing reaction at different rates, overview, the enzyme is unable to deacylate misacylated tRNAVal terminating in 3'-pyrimidines but does deacylate mischarged tRNAVal terminating in adenosine or guanosine, no misactivation of methionine, leucine, glycine, glutamic acid, lysine, tyrosine, and phenylalanine
Products: -
Products: -
?
additional information
?
-
-
Substrates: valine-dependent ATP-diphosphate exchange: valine + ATP + enzyme /Val-AMP-enzyme + diphosphate
Products: -
Products: -
?
additional information
?
-
Substrates: functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: valine-dependent ATP-diphosphate exchange: valine + ATP + enzyme /Val-AMP-enzyme + diphosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with dATP
Products: -
Products: -
?
additional information
?
-
Substrates: interaction of membrane-anchored ValRS with ATP synthase, analysis of the impact of the interaction on the activity of ValRS by measuring aminoacylation activity in whole cell extracts of the wild-type strain and the Anabaena 1C mutant, where the interaction between ValRS and ATP synthase is not expected to occur, analysis of aminoacyl-tRNA synthetases protein interactions, overview
Products: -
Products: -
?
additional information
?
-
Substrates: functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: redundancy of non-AUG initiators is a mechanism to enhance the efficiency of translation in yeast
Products: -
Products: -
?
additional information
?
-
Substrates: functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: loss of the electrostatically interactions between the coiled-coil domain of the enzyme and base A20 and tertiary bas pair G19.C56 increases the Km for the tRNA by 28fold and the kcat for aminoacylation by 19fold
Products: -
Products: -
?
additional information
?
-
-
Substrates: substitutions in the anticodon loop of turnip yellow mosaic virus RNA diminish the viral RNA's ability to be valylated by wheat germ ValRS
Products: -
Products: -
?
additional information
?
-
-
Substrates: valine-dependent ATP-diphosphate exchange: valine + ATP + enzyme /Val-AMP-enzyme + diphosphate
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
ir
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
Products: -
Products: -
?
additional information
?
-
Substrates: functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
Products: -
Products: -
?
additional information
?
-
Substrates: interaction of membrane-anchored ValRS with ATP synthase, analysis of the impact of the interaction on the activity of ValRS by measuring aminoacylation activity in whole cell extracts of the wild-type strain and the Anabaena 1C mutant, where the interaction between ValRS and ATP synthase is not expected to occur, analysis of aminoacyl-tRNA synthetases protein interactions, overview
Products: -
Products: -
?
additional information
?
-
Substrates: functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
Products: -
Products: -
?
additional information
?
-
Substrates: functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
KCl
Mg2+
Mn2+
KCl
-
30 mM: enhances activity of the cytoplasmic enzyme, has no effect on the chloroplastic enzyme, above 30 mM: inhibits activity of cytoplasmic enzyme more strongly than that of chloroplastic enzyme
Mg2+
-
optimal Mg2+/ATP ratio is 2.5 for the chloroplastic and 1 for the cytoplasmic enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-triphospho-5'-adenosine
-
aminoacylation and ATP-diphosphate exchange abolished
S-adenosylhomocysteine
-
competitive with respect to ATP and valine in the ATP-diphosphate exchange reaction, noncompetitive with respect to ATP and valine and uncompetitive with respect ro tRNA in the tRNA aminoacylation
KCl
-
above 30 mM: inhibits activity of cytoplasmic enzyme more strongly than that of chloroplastic enzyme, 30 mM: enhances activity of the cytoplasmic enzyme, has no effect on the chloroplastic enzyme
additional information
-
incorporation of 2.1 mol L-valine per mol of enzyme leads to inactivation
-
additional information
-
reductive activation of the enzyme is strongly inhibited by 0.001-0.30 mM unsaturated fatty acids, or by diethylstilbestrol
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
spermine
-
chloroplastic enzyme: unable to promote aminoacylation in absence of Mg2+. In presence of suboptimal concentrations of Mg2+, spermine can restore maximal activity (not in cytoplasmic enzyme)
additional information
-
stimulatory effects of diverse tRNA variants on the editing activity, overview
-
additional information
-
loss of the electrostatically interactions between the coiled-coil domain of the enzyme and base A20 and tertiary bas pair G19.C56 increases the Km for the tRNA by 28fold and the kcat for aminoacylation by 19fold
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Brain Diseases
Biallelic mutations in valyl-tRNA synthetase gene VARS are associated with a progressive neurodevelopmental epileptic encephalopathy.
Brain Diseases
Biallelic VARS variants cause developmental encephalopathy with microcephaly that is recapitulated in vars knockout zebrafish.
Cardiomyopathy, Hypertrophic
Case Report and Review of the Literature: A New and a Recurrent Variant in the VARS2 Gene Are Associated With Isolated Lethal Hypertrophic Cardiomyopathy, Hyperlactatemia, and Pulmonary Hypertension in Early Infancy.
Epilepsy
Biallelic VARS variants cause developmental encephalopathy with microcephaly that is recapitulated in vars knockout zebrafish.
Epilepsy
Case Report and Review of the Literature: A New and a Recurrent Variant in the VARS2 Gene Are Associated With Isolated Lethal Hypertrophic Cardiomyopathy, Hyperlactatemia, and Pulmonary Hypertension in Early Infancy.
Infections
Analysis of the structure of T4 bacteriophage-modified valyl-tRNA synthetase by limited proteolysis and isoelectric focusing.
Infections
C. elegans germline-deficient mutants respond to pathogen infection using shared and distinct mechanisms.
Infections
Response of a phage modification factor to enhanced production of its target molecule.
Liver Neoplasms, Experimental
[Effects of ionizing radiations on the activity of valyl-tRNA synthetase isolated from rat liver and Morris hepatoma 7777 (author's transl)]
Microcephaly
Biallelic VARS variants cause developmental encephalopathy with microcephaly that is recapitulated in vars knockout zebrafish.
Microcephaly
Loss of function mutations in VARS encoding cytoplasmic valyl-tRNA synthetase cause microcephaly, seizures, and progressive cerebral atrophy.
Muscle Hypotonia
Case Report and Review of the Literature: A New and a Recurrent Variant in the VARS2 Gene Are Associated With Isolated Lethal Hypertrophic Cardiomyopathy, Hyperlactatemia, and Pulmonary Hypertension in Early Infancy.
Neoplasms
Identification of a Specific Translational Machinery via TCTP-EF1A2 Interaction Regulating NF1-associated Tumor Growth by Affinity Purification and Data-independent Mass Spectrometry Acquisition (AP-DIA).
Seizures
Loss of function mutations in VARS encoding cytoplasmic valyl-tRNA synthetase cause microcephaly, seizures, and progressive cerebral atrophy.
Sjogren's Syndrome
Short-range linkage relationships of the valyl-tRNA synthetase gene in Fugu rubripes.
Tuberculosis
Purification & properties of valyl-tRNA synthetase from Mycobacterium tuberculosis H37Rv.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
L-threonine
-
ATP-diphosphate exchange reaction, native wild-type enzyme, pH 7.5, 25°C
0.00061
tRNAVal(GAC)
-
in 100 mM HEPES (pH 7.2), 20 mM KCl, 30 mM MgCl2, at 30°C
-
0.00208
tRNAVal(UAC)
-
in 100 mM HEPES (pH 7.2), 20 mM KCl, 30 mM MgCl2, at 30°C
-
0.00108
tRNAVal(UAC-2)
-
in 100 mM HEPES (pH 7.2), 20 mM KCl, 30 mM MgCl2, at 30°C
-
0.11
ATP
-
ATP-diphosphate exchange reaction, His-tagged wild-type and mutant enzymes, pH 7.5, 25°C
0.0019
L-valine
-
aminoacylation reaction, His-tagged K277A mutant enzyme, pH 7.5, 25°C
0.002
L-valine
-
with mutant tRNAVal with 3'-terminal isoguanosine base analogue, pH 7.5, 37°C
0.0048
L-valine
-
with mutant tRNAVal with 3'-terminal inosine base analogue, pH 7.5, 37°C
0.005
L-valine
-
with mutant tRNAVal with 3'-terminal 2-aminopurine base analogue, pH 7.5, 37°C
0.0088
L-valine
-
with mutant tRNAVal with 3'-terminal purine riboside base analogue, pH 7.5, 37°C
0.047
L-valine
-
aminoacylation reaction, His-tagged wild-type enzyme, pH 7.5, 25°C
0.062
L-valine
-
ATP-diphosphate exchange reaction, native wild-type enzyme, pH 7.5, 25°C
0.07
L-valine
-
ATP-diphosphate exchange reaction, His-tagged wild-type enzyme, pH 7.5, 25°C
0.072
L-valine
-
ATP-diphosphate exchange reaction, His-tagged K277A mutant enzyme, pH 7.5, 25°C
0.00008
tRNAVal
-
aminoacylation reaction with L-valine, wild-type enzyme, pH 7.5, 25°C
0.0001
tRNAVal
-
aminoacylation reaction with L-valine, K277A mutant enzyme, pH 7.5, 25°C
0.0001
tRNAVal
-
aminoacylation reaction with L-valine, His-tagged wild-type enzyme, pH 7.5, 25°C
0.00026
tRNAVal
-
aminoacylation reaction with L-valine, His-tagged K277A mutant enzyme, pH 7.5, 25°C
0.00165
tRNAVal
-
substrate from mitochondria, , mitochondrial and cytoplasmic enzyme
additional information
additional information
-
Km-values of ATP analogs
-
additional information
additional information
-
Km of anticodon loop mutants of turnip yellow mosaic virus RNA
-
additional information
additional information
-
Km for tRNAVal mutants, loss of the electrostatically interactions between the coiled-coil domain of the enzyme and base A20 and tertiary bas pair G19.C56 increases the Km for the tRNA by 28fold
-
additional information
additional information
-
steady-state parameters for tRNA-independent pre-transfer editing by ValRS and its mutants determined by varying concentrations of noncognate threonine, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
50
ATP
-
ATP-diphosphate exchange reaction, His-tagged wild-type enzyme, pH 7.5, 25°C
57
ATP
-
ATP-diphosphate exchange reaction, His-tagged K277A mutant enzyme, pH 7.5, 25°C
0.064
L-valine
-
aminoacylation reaction, His-tagged K277A mutant enzyme, pH 7.5, 25°C
0.68
L-valine
-
with mutant tRNAVal with 3'-terminal 2-aminopurine base analogue, pH 7.5, 37°C
0.99
L-valine
-
with mutant tRNAVal with 3'-terminal isoguanosine base analogue, pH 7.5, 37°C
1.06
L-valine
-
with mutant tRNAVal with 3'-terminal inosine base analogue, pH 7.5, 37°C
1.5
L-valine
-
aminoacylation reaction, His-tagged wild-type enzyme, pH 7.5, 25°C
6.08
L-valine
-
with mutant tRNAVal with 3'-terminal inosine base analogue, pH 7.5, 37°C
6.08
L-valine
-
with mutant tRNAVal with 3'-terminal isoguanosine base analogue, pH 7.5, 37°C
6.08
L-valine
-
with mutant tRNAVal with 3'-terminal 2-aminopurine base analogue, pH 7.5, 37°C
14.4
L-valine
-
with mutant tRNAVal with 3'-terminal purine riboside base analogue, pH 7.5, 37°C
1.5
tRNAVal
-
aminoacylation reaction with L-valine, K277A mutant enzyme, pH 7.5, 25°C
1.7
tRNAVal
-
aminoacylation reaction with L-valine, wild-type enzyme, pH 7.5, 25°C
50
tRNAVal
-
ATP-diphosphate exchange reaction, K277A mutant enzyme, pH 7.5, 25°C
51
tRNAVal
-
ATP-diphosphate exchange reaction, wild-type enzyme, pH 7.5, 25°C
additional information
additional information
-
rate of hydrolysis of Thr-tRNAVal and Val-tRNAVal by wild-type and mutant enzyme, incorporation of amino acids valine and threonine into the enzyme
-
additional information
additional information
-
kcat for tRNAVal mutants, loss of the electrostatically interactions between the coiled-coil domain of the enzyme and base A20 and tertiary bas pair G19.C56 increases the kcat for aminoacylation by 19fold
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
catalytic activity with L-valine and diverse tRNA analogues with functional group substitutions at the terminal nucleoside of the 3'-end, overview
additional information
-
in ValRS transfer to tRNA is 200fold faster than hydrolysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.9
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 10
-
6.5: 30-40% of maximal activity, 10: 10% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Anabaena sp. {PCC 7120}, or SAG 25.82, or UTEX 2576
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
in situ hybridization demonstrates expression of gene glp-4, VARS-2, in the germline and soma, overview. Very strong germline expression is observed in the two U-shaped gonad arms
brenda
additional information
-
in situ hybridization demonstrates expression of gene glp-4, VARS-2, in the germline and soma, overview. Very strong germline expression is observed in the two U-shaped gonad arms
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Schizosaccharomyces pombe contains two distinct nuclear ValRS genes, one encoding the mitochondrial form and the other its cytosolic counterpart. The cytosolic form closely resembles other yeast ValRS sequences. Gene is active and essential for the survival of the yeast
brenda
ValRS is anchored to thylakoid membranes by means of the CAAD domain
brenda
additional information
Schizosaccharomyces pombe contains two distinct nuclear ValRS genes, one encoding the mitochondrial form and the other its cytosolic counterpart. The mitochondrial form exhibits significant divergence from other yeast ValRS sequences. Gene is active and essential for the survival of the yeast. The mitochondrial form lacks the characteristic appended domain
brenda
additional information
out of the 20 aaRSs, only ValRS is found to localize in thylakoid membranes whereas the other enzymes occupy the soluble portion of the cytoplasm, analysis of aminoacyl-tRNA synthetases protein interactions, overview
-
brenda
additional information
the white panicle1 mutant WP1 form of a Val-tRNA synthetase (OsValRS2) from Oryza sativa is targeted to both chloroplasts and mitochondria
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
a single base change in OsValRS2 causes virescent to albino mutant phenotypes in seedlings and white panicles at heading, termed the white panicle 1 (wp1) mutant. The white panicle1 mutant form of a Val-tRNA synthetase from Oryza sativa is targeted to both chloroplasts and mitochondria. The wp1 mutants are defective in early chloroplast development, and wp1 is impaired in chloroplast ribosome biogenesis. Expression of nuclear-encoded photosynthetic genes is significantly repressed, while expression of many chloroplast-encoded genes also changed significantly in wp1 mutants, although mRNA levels of some genes are higher in wp1 than in wild-type. Phenotype, overview
physiological function
additional information
evolution
the enzyme belongs to the class I aminoacyl-tRNA synthetases
evolution
the proline triplet in ValS, the tRNA synthetase that charges tRNAVal with valine, is the only single polyproline stretch that is invariant across all domains of life. The critical role of the proline triplet for ValS activity may explain why bacterial cells co-evolved the EF-P rescue system. Nature has evolved not only specialized translation factors to overcome stalling at polyproline stretches, but also evolved independent sets of modification enzymes to activate these factors. This in itself implies that the benefits of retaining polyproline stretches significantly outweigh the cost of implementing and maintaining the EF-P and a/eIF5A rescue systems
evolution
glp-4 VARS-2 is a cytoplasmic class I valyl aminoacyl tRNA synthetase
physiological function
gene is active and essential for the survival of the yeast
physiological function
-
hydrolytic editing activities are present in aminoacyl-tRNA synthetases possessing reduced amino acid discrimination in the synthetic reactions. Post-transfer hydrolysis of misacylated tRNA in class I editing enzymes, e.g. ValRS, occurs in a spatially separate domain inserted into the catalytic Rossmann fold, location and mechanisms of pre-transfer hydrolysis of misactivated amino acids, overview. The rates of amino acid transfer to tRNA are similar for cognate and noncognate aminoacyl-adenylates. Editing by ValRS occurs nearly exclusively by post-transfer hydrolysis in the editing domain
physiological function
in Anabaena sp. PCC 7120, ValRS acts as a hub for the nucleation of a translational complex by attracting other aaRSs to the membranes
physiological function
the proline triplet located in the active site of ValS is important for efficient charging of tRNAVal with valine preventing formation of mischarged Thr-tRNAVal, as well as for efficient growth of Escherichia coli in vivo. The critical role of the proline triplet for ValS activity may explain why bacterial cells co-evolved the EF-P rescue system
physiological function
the Val-tRNA synthetase OsValRS2 regulates chloroplast ribosome biogenesis in rice and is essential for early chloroplast development
physiological function
glp-4 VARS-2 is a cytoplasmic class I valyl aminoacyl tRNA synthetase that catalyzes the transfer of valine to its cognate tRNA for protein synthesis
physiological function
-
the evolutionary related IleRS, leucyl- and valyl-tRNA synthetases, all efficiently hydrolyze Nva-tRNAs even when editing of Nva seems redundant
additional information
-
human valyl-tRNA synthetase and mitochondrial protein elongation factor EF-Tu show suppressing cross-activity on different tRNA mutants in humans and Saccharomyces cerevisiae, mechanism and specificity of suppression, overview. Suppressive activities of wild-type and mutant enzymes, overview
additional information
molecular trigger for pre-transfer editing pathway in valyl-tRNA synthetase, molecular dynamics simulations using ValRS structure, PDB ID 1GAX, overview. Structural models of the complexes ValRS-tRNAval-Val-AMP and ValRS-tRNAval-Thr-AMP
additional information
analysis of aminoacyl-tRNA synthetases protein interactions, overview. The Anabaena sp. ValRs is a CAAD-containing aaRSs, the CAAD domain possesses an inherent membrane targeting ability
additional information
expression of ValS is strictly dependent on the presence of active elongation factor P (EF-P) in vivo and in vitro
additional information
structure homology modeling using the valine tRNA-synthetase (valRS) from Thermus thermophilius, PDB ID 1IVS, as a template, also with bound valyl-adenylate substrate
additional information
-
structure homology modeling using the valine tRNA-synthetase (valRS) from Thermus thermophilius, PDB ID 1IVS, as a template, also with bound valyl-adenylate substrate
Show AA Sequence and Transmembrane Helices (33784 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
125000
126000
140000
additional information
140000
-
x * 140000, SDS-PAGE, valyl-tRNA synthetase component purified from the heterotypic complex
140000
-
4 * 140000, SDS-PAGE, the high molecular weight valyl-tRNA synthetase is a homotypic tetramer which converts to the monomeric valyl-tRNA synthetase after cleavage of a small peptide
additional information
-
nucleotide sequence of the Escherichia coli valyl-tRNA synthetase gene
additional information
-
heterotypic complex of valyl-tRNA synthetase with elongation factor I has a MW of 700000, gel filtration
additional information
-
three-dimensional structure of the valyl-tRNA synthetase/elongation factor-1H complex
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
tetramer
additional information
?
-
x * 140000, SDS-PAGE, valyl-tRNA synthetase component purified from the heterotypic complex
monomer
-
the high molecular weight valyl-tRNA synthetase is a homotypic tetramer which converts to the monomeric valyl-tRNA synthetase after cleavage of a small peptide
tetramer
-
4 * 140000, SDS-PAGE, the high molecular weight valyl-tRNA synthetase is a homotypic tetramer which converts to the monomeric valyl-tRNA synthetase after cleavage of a small peptide
additional information
the enzyme possesses N terminal alpha-helices with basic residues distributed asymmetrically, on a single face of the helix, termed basic faced alpha helices, BFAHs, which are unique to the aminoacyl-tRNA synthetases, structural analysis, determination of distribution of basic residues within protein secondary structure by Fourier analysis, functional and evolutionary aspects of these structural features, overview
additional information
glp-4 VARS-2 has two tRNA recognition domains (1 and 2), a split class 1 Rossmann-fold, which functions in catalyzing the synthesis of aminoacyl-adenylate and aminoacyl-tRNAval, an editing domain, and the connective polypeptide (CP1) domain, which also functions in post-transfer editing. Structural analysis of glp-4 VARS-2, homology modeling, overview
additional information
-
glp-4 VARS-2 has two tRNA recognition domains (1 and 2), a split class 1 Rossmann-fold, which functions in catalyzing the synthesis of aminoacyl-adenylate and aminoacyl-tRNAval, an editing domain, and the connective polypeptide (CP1) domain, which also functions in post-transfer editing. Structural analysis of glp-4 VARS-2, homology modeling, overview
additional information
the enzyme possesses N terminal alpha-helices with basic residues distributed asymmetrically, on a single face of the helix, termed basic faced alpha helices, BFAHs, which are unique to the aminoacyl-tRNA synthetases, structural analysis, determination of distribution of basic residues within protein secondary structure by Fourier analysis, functional and evolutionary aspects of these structural features, overview
additional information
the enzyme possesses N terminal alpha-helices with basic residues distributed asymmetrically, on a single face of the helix, termed basic faced alpha helices, BFAHs, which are unique to the aminoacyl-tRNA synthetases, structural analysis, determination of distribution of basic residues within protein secondary structure by Fourier analysis, functional and evolutionary aspects of these structural features, overview
additional information
-
the enzyme possesses N terminal alpha-helices with basic residues distributed asymmetrically, on a single face of the helix, termed basic faced alpha helices, BFAHs, which are unique to the aminoacyl-tRNA synthetases, structural analysis, determination of distribution of basic residues within protein secondary structure by Fourier analysis, functional and evolutionary aspects of these structural features, overview
additional information
the enzyme possesses N terminal alpha-helices with basic residues distributed asymmetrically, on a single face of the helix, termed basic faced alpha helices, BFAHs, which are unique to the aminoacyl-tRNA synthetases, structural analysis, determination of distribution of basic residues within protein secondary structure by Fourier analysis, functional and evolutionary aspects of these structural features, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.7 A resolution crystal structure of the ValRS editing domain and 1.7 A resolution crystal structure of the editing domain bound with [N-(L-threonyl)-sulfamoyl]adenosine, hanging drop vapor diffusion method
enzyme complexed with tRNAVal and valyl-adenylate, hanging-drop vapour diffusion method, 20°C, 1 month, equal volumes of protein and crystallization solution: 50 mM N-(2-acetoamide)iminodiacetic acid sodium salt buffer, pH 6.5, 2% 2-propanol, 0.1 M lithium sulfate, 12% PEG4000, equilibration against reservoir solution: 50 mM N-(2-acetoamide)iminodiacetic acid sodium salt buffer, pH 6.5, 2% propanol, 0.1 M lithium sulfate, and 14% PEG 4000, ligand-free crystals by macro-seeding, X-ray diffraction structure determination at 2.9 A resolution, and analysis
-
enzyme in complex with tRNAValCAC isoacceptor and an analogue of the Val-adenylate intermediate, hanging-drop vapour diffusion method, 2 months, 4°C, 7-10 mg/ml protein/tRNA/Val-AMS solution in a molar ration of 1:1.1:2, plus equal volume of crystallization solution containing 50 mM sodium cacodylate, pH 6.5, 1.0 ammonium sulfate, 10 mM MgSO4, 6% 1,8-diaminooctane, equilibration against a reservoir solution of 50 mM sodium cacodylate, pH 6.5, 2.8 M ammonium sulfate, 10 mM MgSO4, X-ray structure determination at 2.9 A resolution and analysis
-
molecular dynamics simulation studies based on PDB structure ID 1wk9. Noncognate substrates Thr-AMP and Thr-A76, bind more strongly than the cognate substrates Val-AMP and Val-A76 in both pre- and post-transfer editing, respectivel
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G296D
naturally occuring mutation bn2, the mutant glp-4(bn2ts) shows partial loss of function. Aspartate 296 in the editing pocket induces inappropriate deacylation of correctly charged Val-tRNAval. Intragenic suppressor mutations are predicted to displace aspartate 296 so that it is less able to catalyze inappropriate deacylation. Thus glp-4(bn2ts) likely causes reduced protein translation due to decreased levels of Val-tRNAval. glp-4(bn2ts) mutants are widely used to generate germline deficient mutants for organismal studies, under the assumption that the soma is unaffected. As reduced translation has also been demonstrated to alter organismal properties, it is unclear whether changes in aging, stress resistance etc. observed in glp-4(bn2ts) mutants are the result of germline deficiency or reduced translation. The G296D mutation lies just inside a region of the valyl-tRNA synthetase called the CP1 domain
D286A
-
site-directed mutagenesis, the ValRS CP1 domain mutant is unable to deacylate misacylated tRNA even at high enzyme concentrations
K277A
-
site-directed mutagenesis, mutant exhibits a reduced posttransfer editing activity compared to the wild-type, also the specificiy of the editing reaction is modulated, the mutant hydrolyzes the correctly formed Val-tRNAVal, increased sensitivity to Mg2+, high concentrations inactivate
K277P
-
site-directed mutagenesis, the ValRS CP1 domain mutant is unable to deacylate misacylated tRNA even at high enzyme concentrations
K277P/D286A
-
site-directed mutagenesis, the ValRS CP1 domain mutant is unable to deacylate misacylated tRNA even at high enzyme concentrations
DELTA1-97
-
an N-domain-deleted yeast valyltRNA synthetase mutant (DELTA1-97) form Saccharomyces cerevisiae can be rescued by fusion of the equivalent domain from its human homologue
P661T
i.e. NM_006295.2:c.1981C>A p.(Pro661Thr), biallelic missense variant identified in patients with a range of global developmental delay, epileptic encephalopathy and primary or progressive microcephaly. Primary cells show intact VARS protein but reduced enzymatic activity
R119C
i.e. NM_006295.2:c.3355C>T p.(Arg1119Cys), biallelic missense variant identified in patients with a range of global developmental delay, epileptic encephalopathy and primary or progressive microcephaly. Primary cells show intact VARS protein but reduced enzymatic activity
R94H
i.e. NM_006295.2:c.2840G>A p.(Arg947His), biallelic missense variant identified in patients with a range of global developmental delay, epileptic encephalopathy and primary or progressive microcephaly. Primary cells show intact VARS protein but reduced enzymatic activity
D750G
-
the mutation is associated with a temperature-sensitive phenotype. Although depicting slower growth at 26°C, the mutant strain is unable to grow at 37°C
DELTA1-97
-
deletion of N-terminal polypeptide extension of 97 residues, which is absent in bacteria, severely impairs tRNA binding, aminoacylation, and complementation activities of the enzyme. This N-domain-deleted yeast valyl-tRNA synthetase mutant can be rescued by fusion of the equivalent domain from its human homologue
DELTA32-71
-
deletion of a lysine rich insert impairs aminoacylation activity of the enzyme in vitro but aminoacylation activity is still significantly higher than in DELTA1-97 mutant. Km: 0.001 mM (L-valyl-tRNAVal), kcast: 0.06/sec (L-valyl-tRNAVal)
D279A
F264A
valylation activity is similar to that of wild-type enzyme, about 15% decrease in ATP consumption rate compared to wild-type enzyme, somewhat reduced deacylation activityith Thr-tRNAVal, mutation impairs editing activity of ValRS
K270A
R216A
valylation activity is similar to that of wild-type enzyme, about 15% decrease in ATP consumption rate compared to wild-type enzyme, somewhat reduced deacylation activity with Thr-tRNAVal
R818A/R843A
-
slightly reduced activity compared to the wild-type enzyme with tRNAValCAC mutant substrate
T272A
valylation activity is similar to that of wild-type enzyme, about 15% decrease in ATP consumption rate compared to wild-type enzyme, somewhat reduced deacylation activity with Thr-tRNAVal
additional information
D279A
valylation activity is similar to that of wild-type enzyme, efficiently produces Thr-tRNAVal, drastic decrease in ATP consumption rate, severe deficiency in deacylation activity with Thr-tRNAVal compared to wild-type enzyme
D279A
editing site mutation, severely affects the binding ability of pre-transfer substrate Thr-AMP
K270A
slight reduction of valylation activity, efficiently produces Thr-tRNAVal, drastic decrease in ATP consumption rate, severe deficiency in deacylation activity with Thr-tRNAVal compared to wild-type enzyme
K270A
editing site mutation, severely affects the binding ability of pre-transfer substrate Thr-AMP
additional information
a knockout mutation causes early larval lethality
additional information
-
a knockout mutation causes early larval lethality
additional information
-
substitution of base 75 of C by U or A leads to effective stimulation of the editing activity at lower rates, substitution with G leads to reduction of the editing activity by 95%, mutational exchange of the discriminator base A73 to U73 or C73 does not alter enzyme activity but exchange to G73 stimulates editing activity of the catalytically inactive mutant
additional information
generation of three single ValS Pro-to-Gly mutants, ValS-GPP, ValS-PGP, and ValS-PPG, as well as a triple PPP-to-GGG mutant (ValS-GGG). The ability of the ValS mutants to charge tRNAVal with [14C]valine is assessed and compared to wild-type ValS. All ValS mutants are less efficient than the wild-type, the ValS-PPG and ValS-GGG mutants are completely devoid of activity, whereas the ValS-PGP and ValS-GPP mutants retain some activity but at lower levels than the wild-type enzyme
additional information
-
fusion of the N-terminal 97 residue domain of human ValRS to Escherichia coli glutaminyl-tRNA synthetase enables the otherwise inactive prokaryotic enzyme to function as a yeast enzyme in vivo. Different from the native yeast enzyme, which shows different affinities toward mixed tRNA populations, the fusion enzyme exhibites similar binding affinities for all yeast tRNAs
additional information
missense mutation c.3192G>A, p.Met1064Ile and a splice site mutation c.1577-2A>G are found in siblings from a non-consanguineous family with severe early onset of neurological manifestations. The splice site acceptor variant allele leads to nonsense mediated decay, the missense mutation lies in a highly conserved region and could alter side chain packing. Levels of mRNA and protein in skin derived fibroblasts are remarkably reduced
additional information
i.e. NM_006295.2:c.(2074G>C;1324C>T) p.(Ala692Pro;Arg442*), biallelic missense variant identified in patients with a range of global developmental delay, epileptic encephalopathy and primary or progressive microcephaly. Primary cells show intact VARS protein but reduced enzymatic activity
additional information
a single base change in OsValRS2, changing a Trp into a Cys, causes virescent to albino mutant phenotypes in seedlings and white panicles at heading, the mutant is termed the white panicle 1 (wp1) mutant. The white panicle1 mutant form of a Val-tRNA synthetase (OsValRS2) from Oryza sativa is targeted to both chloroplasts and mitochondria. The wp1 mutants are defective in early chloroplast development, and wp1 is impaired in chloroplast ribosome biogenesis. Expression of nuclear-encoded photosynthetic genes is significantly repressed, while expression of many chloroplast-encoded genes also changed significantly in wp1 mutants, although mRNA levels of some genes are higher in wp1 than in wild-type. Phenotype, overview
additional information
-
substitution of the AUG initiator of the mitochondrial ValRS isozyme, ATG1 of VAS1, with redundant ACG triplets, mutation of ATG1 to GCG deprived the construct of its mitochondrial activity, redundant ACG triplets could effectively substitute for ATG1 in initiation of the mitochondrial enzyme, while a single ACG triplet could hardly do so
additional information
-
fusion of the N-terminal 97 residue domain of the yeast enzyme or its human counterpart to Escherichia coli glutaminyl-tRNA synthetase enables the otherwise inactive prokaryotic enzyme to function as a yeast enzyme in vivo. Different from the native yeast enzyme, which shows different affinities toward mixed tRNA populations, the fusion enzyme exhibites similar binding affinities for all yeast tRNAs
additional information
-
a C-treminally truncated mutant enzyme shows highly reduced activity compared to the wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
-
half-life: 30 min, when enzyme is stabilized by 1 mg/ml bovine serum albumin and 50% glycerol
40
-
5 min, chloroplastic enzyme loses 30% of its activity, mitochondrial enzyme 75%
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-180°C, purified enzyme highly unstable, stored immediately after purification at -180°C
-
-20°C, without addition of tRNA about 80% loss of activity during 1 week
-
4°C, 50 mM potassium phosphate buffer, pH 7.0, 1 mM MgCl2, 0.002 mM L-valine, 100 mM NaCl, 15% v/v 1,2-propanediol, stable for several weeks
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from chloroplast membranes by ultracentrifugation, solubilization with 1%n-dodecyl-beta-D-maltoside, and again ultracentrifugation, recombinant enzyme from Escherichia coli strain C41(DE3), recombinant GFP-tagged enzyme from Anabaena sp. membranes
recombinant His-tagged ValRS from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
-
using Ni-NTA chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae as a His-tagged fusion protein
expression in Escherichia coli
gene glp-4, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of wild-type and mutant ValRS enzymes in Escherichia coli strain Rosetta (DE3)
gene Os03g0694900 encodes wild-type OsValRS, and gene LOC_Os07g06940 encodes enzyme mutant WP1, map-based cloning of the WP1 gene to the short arm of chromosome 7 between two simple sequence repeat markers, Bs8 and Bs1, DNA and amino acid sequence determination and analysis
gene valS, expression of His-tagged wild-type and mutant enzymes in strain JM101Tr
-
gene valS, phylogenetic analysis, recombinant expression of the enzyme in Escherichia coli strain C41(DE3), recombinant expression of GFP-tagged enzyme in Anabaena sp. in membranes
gene VAS1, codes for both cytoplasmic and mitochondrial isozymes of ValRS through alternative transcription and translation, expression of wild-type and mutant enzymes in yeast
-
overexpression of wild-type and mutant emnzymes in Escherichia coli strain JM109(DE3)
-
expressed in Saccharomyces cerevisiae as a His-tagged fusion protein
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of ValS in vivo and in vitro requires the elongation factor P (EF-P), the downregulation of ValS in the absence of active EF-P is specific, the lack of EF-P leads to a strong downregulation of ValS. The lack of YfcM (DELTAyfcM), which hydroxylates the lysinylated EF-P, does not lead to downregulation of ValS. ValS expression is also dependent on EF-P in vitro
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
a C25U point mutation in the MTTV gene, gene encoding tRNAVal, is associated with a metabolic disorder resulting in the neonatal deaths of numerous siblings. In primary myoblasts and transmitochondrial cybrids established from the proband and offspring, the steady-state levels of the mutated mt-tRNAVal are greater than in the biopsy material, but are still lower than in control myoblasts. Decrease in steady-state mt-tRNAVal observed cell lines is caused by a rapid degradation of the deacylated form of the abnormal mt-tRNAVal. By both establishing the identity of the human mitochondrial valyltRNA synthetase then inducing its overexpression in transmitochondrial cell lines, steady-state levels of the mutated mt-tRNAVal can be partially restored
medicine
missense mutation c.3192G>A, p.Met1064Ile and a splice site mutation c.1577-2A>G are found in siblings from a non-consanguineous family with severe early onset of neurological manifestations. The splice site acceptor variant allele leads to nonsense mediated decay, the missense mutation lies in a highly conserved region and could alter side chain packing. Levels of mRNA and protein in skin derived fibroblasts are remarkably reduced
medicine
biallelic missense variants . NM_006295.2:c.3355C>T p.(Arg1119Cys), NM_006295.2:c.2840G>A p.(Arg947His), NM_006295.2:c.1981C>A p.(Pro661Thr), NM_006295.2:c.(2074G>C;1324C>T) p.(Ala692Pro;Arg442*), have been identified in patients with a range of global developmental delay, epileptic encephalopathy and primary or progressive microcephaly. Primary cells show intact VARS protein but reduced enzymatic activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bhanot, O.S.; Kucan, Z.; Aoyagi, S.; Lee, F.C.; Chambers, R.W.
Purification of tyrosine:tRNA ligase, valine:tRNA ligase, alanine:tRNA ligase, and isoleucine:tRNA ligase from Saccharomyces cerevisiae alphaS288C
Methods Enzymol.
29E
547-576
1974
Saccharomyces cerevisiae, Saccharomyces cerevisiae alphaS288C
-
brenda
Kohda, D.; Yokoyama, S; Miyazawa, T.
Thermostable valyl-tRNA, isoleucyl-tRNA and methionyl-tRNA synthetases from an extreme thermophile Thermus thermophilus HB8. Protein structure and Zn2+ binding
FEBS Lett.
174
20-23
1984
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Colas, B.; Imbault, P.; Sarantoglou, V.; Boulanger, Y.; Weil, J.H.
Chloroplastic and cytoplasmic valyl- and leucyl-tRNA synthetases from Euglena gracilis. Comparative study of their structural properties
Biochim. Biophys. Acta
697
71-77
1982
Euglena gracilis
brenda
Imbault, P.; Sarantoglou, V.; Weil, J.H.
Properties of purified chloroplastic and cytoplasmic valyl- and leucyl-tRNA synthetases from Euglena gracilis
Phytochemistry
21
1189-1193
1982
Euglena gracilis
-
brenda
Freist, W.; von der Haar, F.; Faulhammer, H.; Cramer, F.
Valyl-tRNA, isoleucyl-tRNA and tyrosyl-tRNA synthetase from baker's yeast. Substrate specificity with regard to ATP analogs and mechanism of the aminoacylation reaction
Eur. J. Biochem.
66
493-497
1976
Saccharomyces cerevisiae
brenda
Dreher, T.W.; Tsai, C.H.; Florentz, C.; Giege, R.
Specific valylation of turnip yellow mosaic virus RNA by wheat germ valyl-tRNA synthetase determined by three anticodon loop nucleotides
Biochemistry
31
9183-9189
1992
Triticum aestivum
brenda
Hountondji, C.; Schmitter, J.M.; Fukui, T.; Tagaya, M.; Blanquet, S.
Affinity labeling of aminoacyl-tRNA synthetases with adenosine triphosphopyridoxal. Probing the Lys-Met-Ser-Lys-Ser signature sequence as the ATP-binding site in Escherichia coli methionyl- and valyl-tRNA synthetases
Biochemistry
29
11266-11273
1990
Escherichia coli
brenda
Bee, G.; Kerjan, P.; Zha, X.D.; Waller, J.P.
Valyl-tRNA synthetase from rabbit liver. Purification as a heterotypic complex in association with elongation factor 1
J. Biol. Chem.
264
21131-21137
1989
Oryctolagus cuniculus
brenda
Bee, G.; Waller, J.P.
Valyl-tRNA synthetase from rabbit liver. II. The enzyme derived from the high-Mr complex displays hydrophobic as well as polyanion-binding properties
J. Biol. Chem.
264
21138-21143
1989
Oryctolagus cuniculus, Saccharomyces cerevisiae, Saccharomyces cerevisiae D273
brenda
Godar, D.E.; Yang, D.C.H.
Mammalian high molecular weight and monomeric forms of valyl-tRNA synthetase
Biochemistry
27
2181-2186
1988
Rattus norvegicus
brenda
Bergmann, F.H.; Berg, P.; Dieckmann, M.
The Enzymic synthesis of amino acyl derivatives of ribonucleic acid. II. The preparation of leucyl-, valyl-, isoleucyl-, and methionyl ribonucleic acid synthetases from Escherichia coli
J. Biol. Chem.
236
1735-1740
1961
Escherichia coli
-
brenda
Paradies, H.H.
Isolation and crystallization of valyl-tRNA synthetase from E. coli MRE 600
J. Biochem.
76
655-659
1974
Escherichia coli, Escherichia coli MRE 600
brenda
Suyama, Y.; Hamada, J.
The mitochondrial and cytoplasmic valyl tRNA synthetases in Tetrahymena are indistinguishable
Arch. Biochem. Biophys.
191
437-443
1978
Tetrahymena pyriformis
brenda
Natarajan, V.; Gopinathan, K.P.
Purification and properties of valyl-tRNA synthetase from Mycobacterium smegmatis
Biochim. Biophys. Acta
568
253-263
1979
Mycolicibacterium smegmatis
brenda
Sarantoglou, V.; Imbault, P.; Weil, J.H.
The use of affinity elution from blue dextran Sepharose by yeast tRNA2Val in the complete purification of the cytoplasmic valyl-tRNA synthetase from Euglena gracilis
Biochem. Biophys. Res. Commun.
93
134-140
1980
Euglena gracilis
brenda
Felter, S.; Diatewa, M.; Schneider, C.; Stahl, A.J.C.
Yeast mitochondrial and cytoplasmic valyl-tRNA synthetases
Biochem. Biophys. Res. Commun.
98
727-734
1981
Saccharomyces cerevisiae
brenda
Jakubowski, H.
The mechanism of inhibition of valyl-tRNA synthetase by S-adenosylhomocysteine
Biochim. Biophys. Acta
709
325-331
1982
Lupinus luteus
brenda
Black, S.
A novel thiol-dependent arsenite-sensitive valyl-tRNA synthetase activity from yeast
J. Biol. Chem.
258
2112-2114
1983
Saccharomyces cerevisiae
brenda
Black, S.
Inhibition of the reductive activation of a valyl-tRNA synthetase from yeast by unsaturated fatty acids and associated observations on newly found lipophilic substances from yeast
J. Biol. Chem.
260
433-440
1985
Saccharomyces cerevisiae
brenda
Brand, N.J.; Fersht, A.R.
Molecular cloning of the gene encoding the valyl-tRNA synthetase from Bacillus stearothermophilus
Gene
44
139-142
1986
Geobacillus stearothermophilus
brenda
Kakitani, M.; Tonomura, B.; Hiromi, K.
Valyl-tRNA synthetase from Bacillus stearothermophilus. Purification and binding with the substrates L-valine and ATP
Agric. Biol. Chem.
50
2437-2444
1986
Geobacillus stearothermophilus, Geobacillus stearothermophilus NCA 1503
-
brenda
Motorin, Y.A.; Wolfson, A.D.; Orlowsky, A.F.; Gladilin, K.L.
Purification of valyl-tRNA synthetase high-molecular-mass complex from rabbit liver
FEBS Lett.
220
363-365
1987
Oryctolagus cuniculus
brenda
Hrtlein, M.; Frank, R.; Madern, D.
Nucleotide sequence of Escherichia coli valyl-tRNA synthetase gene valS
Nucleic Acids Res.
15
9081-9082
1987
Escherichia coli
brenda
Heck, J.D.; Hatfield, G.W.
Valyl-tRNA synthetase gene of Escherichia coli K12. Primary structure and homology within a family of aminoacyl-tRNA synthetases
J. Biol. Chem.
263
868-877
1988
Escherichia coli
brenda
Tardif, K.D.; Liu, M.; Vitseva, O.; Hou, Y.M.; Horowitz, J.
Misacylation and editing by Escherichia coli valyl-tRNA synthetase: evidence for two tRNA binding sites
Biochemistry
40
8118-8125
2001
Escherichia coli
brenda
Hountondji, C.; Lazennec, C.; Beauvallet, C.; Dessen, P.; Pernollet, J.C.; Plateau, P.; Blanquet, S.
Crucial role of conserved lysine 277 in the fidelity of tRNA aminoacylation by Escherichia coli valyl-tRNA synthetase
Biochemistry
41
14856-14865
2002
Escherichia coli
brenda
Fukai, S.; Nureki, O.; Sekine, S.; Shimada, A.; Tao, J.; Vassylyev, D.G.; Yokoyama, S.
Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNA(Val) and valyl-tRNA synthetase
Cell
103
793-803
2000
Thermus thermophilus
brenda
Ramesh, V.; RajBhandary, U.L.
Importance of the anticodon sequence in the aminoacylation of tRNAs by methionyl-tRNA synthetase and by valyl-tRNA synthetase in an archaebacterium
J. Biol. Chem.
276
3660-3665
2001
Haloferax volcanii, Haloferax volcanii WFD11
brenda
Tardif, K.D.; Horowitz, J.
Transfer RNA determinants for translational editing by Escherichia coli valyl-tRNA synthetase
Nucleic Acids Res.
30
2538-2545
2002
Escherichia coli
brenda
Tardif, K.D.; Horowitz, J.
Functional group recognition at the aminoacylation and editing sites of E. coli valyl-tRNA synthetase
RNA
10
493-503
2004
Escherichia coli
brenda
Fukai, S.; Nureki, O.; Sekine, S.; Shimada, A.; Vassylyev, D.G.; Yokoyama, S.
Mechanism of molecular interactions for tRNA(Val) recognition by valyl-tRNA synthetase
RNA
9
100-111
2003
Thermus thermophilus
brenda
Jiang, S.; Wolfe, C.L.; Warrington, J.A.; Norcum, M.T.
Three-dimensional reconstruction of the valyl-tRNA synthetase/elongation factor-1H complex and localization of the delta subunit
FEBS Lett.
579
6049-6054
2005
Homo sapiens
brenda
Fukunaga, R.; Yokoyama, S.
Structural basis for non-cognate amino acid discrimination by the valyl-tRNA synthetase editing domain
J. Biol. Chem.
280
29937-29945
2005
Thermus thermophilus (P96142), Thermus thermophilus
brenda
Massey, S.E.
Basic faced alpha-helices are widespread in the peptide extensions of the eukaryotic aminoacyl-tRNA synthetases
In Silico Biol.
6
259-273
2006
Saccharomyces cerevisiae, Arabidopsis thaliana (P93736), Takifugu rubripes (P49696), Homo sapiens (P26640), Oryza sativa (Q851K9)
brenda
Chang, K.J.; Lin, G.; Men, L.C.; Wang, C.C.
Redundancy of non-AUG initiators. A clever mechanism to enhance the efficiency of translation in yeast
J. Biol. Chem.
281
7775-7783
2006
Saccharomyces cerevisiae
brenda
Chang, C.P.; Lin, G.; Chen, S.J.; Chiu, W.C.; Chen, W.H.; Wang, C.C.
Promoting the formation of an active synthetase/tRNA complex by a nonspecific tRNA-binding domain
J. Biol. Chem.
283
30699-30706
2008
Saccharomyces cerevisiae, Homo sapiens
brenda
Rorbach, J.; Yusoff, A.A.; Tuppen, H.; Abg-Kamaludin, D.P.; Chrzanowska-Lightowlers, Z.M.; Taylor, R.W.; Turnbull, D.M.; McFarland, R.; Lightowlers, R.N.
Overexpression of human mitochondrial valyl tRNA synthetase can partially restore levels of cognate mt-tRNAVal carrying the pathogenic C25U mutation
Nucleic Acids Res.
36
3065-3074
2008
Homo sapiens
brenda
Bharatham, N.; Bharatham, K.; Lee, Y.; Woo Lee, K.
Molecular dynamics simulation study of valyl-tRNA synthetase with its pre- and post-transfer editing substrates
Biophys. Chem.
143
34-43
2009
Thermus thermophilus (P96142)
brenda
Chiu, W.C.; Chang, C.P.; Wen, W.L.; Wang, S.W.; Wang, C.C.
Schizosaccharomyces pombe possesses two paralogous valyl-tRNA synthetase genes of mitochondrial origin
Mol. Biol. Evol.
27
1415-1424
2010
Schizosaccharomyces pombe (O75005), Schizosaccharomyces pombe (O14160), Schizosaccharomyces pombe
brenda
Montanari, A.; De Luca, C.; Frontali, L.; Francisci, S.
Aminoacyl-tRNA synthetases are multivalent suppressors of defects due to human equivalent mutations in yeast mt tRNA genes
Biochim. Biophys. Acta
1803
1050-1057
2010
Homo sapiens
brenda
Dulic, M.; Cvetesic, N.; Perona, J.J.; Gruic-Sovulj, I.
Partitioning of tRNA-dependent editing between pre- and post-transfer pathways in class I aminoacyl-tRNA synthetases
J. Biol. Chem.
285
23799-23809
2010
Escherichia coli
brenda
Li, L.; Yu, L.; Huang, Q.
Molecular trigger for pre-transfer editing pathway in valyl-tRNA synthetase: a molecular dynamics simulation study
J. Mol. Model.
17
555-564
2011
Thermus thermophilus (P96142)
brenda
Duarte, M.; Videira, A.
Defective valyl-tRNA synthetase hampers the mitochondrial respiratory chain in Neurospora crassa
Biochem. J.
448
297-306
2012
Neurospora crassa
brenda
Olmedo-Verd, E.; Santamaria-Gomez, J.; Ochoa de Alda, J.A.; Ribas de Pouplana, L.; Luque, I.
Membrane anchoring of aminoacyl-tRNA synthetases by convergent acquisition of a novel protein domain
J. Biol. Chem.
286
41057-41068
2011
Anabaena sp., Anabaena sp. PCC 7120
brenda
Cvetesic, N.; Perona, J.J.; Gruic-Sovulj, I.
Kinetic partitioning between synthetic and editing pathways in class I aminoacyl-tRNA synthetases occurs at both pre-transfer and post-transfer hydrolytic steps
J. Biol. Chem.
287
25381-25394
2012
Escherichia coli
brenda
Starosta, A.L.; Lassak, J.; Peil, L.; Atkinson, G.C.; Woolstenhulme, C.J.; Virumaee, K.; Buskirk, A.; Tenson, T.; Remme, J.; Jung, K.; Wilson, D.N.
A conserved proline triplet in Val-tRNA synthetase and the origin of elongation factor P
Cell Rep.
9
476-483
2014
Escherichia coli (P07118)
brenda
Santamaria-Gomez, J.; Ochoa de Alda, J.A.; Olmedo-Verd, E.; Bru-Martinez, R.; Luque, I.
Sub-cellular localization and complex formation by aminoacyl-tRNA synthetases in cyanobacteria evidence for interaction of membrane-anchored ValRS with ATP synthase
Front. Microbiol.
7
857
2016
Nostoc sp. PCC 7120 = FACHB-418 (Q8YX97)
brenda
Rastogi, S.; Borgo, B.; Pazdernik, N.; Fox, P.; Mardis, E.; Kohara, Y.; Havranek, J.; Schedl, T.
Caenorhabditis elegans glp-4 encodes a valyl aminoacyl tRNA synthetase
G3 (Bethesda)
5
2719-2728
2015
Caenorhabditis elegans (Q9U1Q4), Caenorhabditis elegans
brenda
Wang, Y.; Wang, C.; Zheng, M.; Lyu, J.; Xu, Y.; Li, X.; Niu, M.; Long, W.; Wang, D.; Wang, H.; Terzaghi, W.; Wang, Y.; Wan, J.
White panicle1, a Val-tRNA synthetase regulating chloroplast ribosome biogenesis in rice, is essential for early chloroplast development
Plant Physiol.
170
2110-2123
2016
Oryza sativa Japonica Group (Q851K9)
brenda
Stephen, J.; Nampoothiri, S.; Banerjee, A.; Tolman, N.J.; Penninger, J.M.; Elling, U.; Agu, C.A.; Burke, J.D.; Devadathan, K.; Kannan, R.; Huang, Y.; Steinbach, P.J.; Martinis, S.A.; Gahl, W.A.; Malicdan, M.C.V.
Loss of function mutations in VARS encoding cytoplasmic valyl-tRNA synthetase cause microcephaly, seizures, and progressive cerebral atrophy
Hum. Genet.
137
293-303
2018
Homo sapiens (P26640)
brenda
Bilus, M.; Semanjski, M.; Mocibob, M.; Zivkovic, I.; Cvetesic, N.; Tawfik, D.S.; Toth-Petroczy, A.; Macek, B.; Gruic-Sovulj, I.
On the mechanism and origin of isoleucyl-tRNA synthetase editing against norvaline
J. Mol. Biol.
431
1284-1297
2019
Escherichia coli
brenda
Friedman, J.; Smith, D.E.; Issa, M.Y.; Stanley, V.; Wang, R.; Mendes, M.I.; Wright, M.S.; Wigby, K.; Hildreth, A.; Crawford, J.R.; Koehler, A.E.; Chowdhury, S.; Nahas, S.; Zhai, L.; Xu, Z.; Lo, W.S.; James, K.N.; Musaev, D.; Accogli, A.; Guerrero, K.; Tran, L.T.; Omar, T.E.I.; Ben-Omran, T.; Dimmock, D.
Biallelic mutations in valyl-tRNA synthetase gene VARS are associated with a progressive neurodevelopmental epileptic encephalopathy
Nat. Commun.
10
707
2019
Homo sapiens (P26640)
brenda
EXTERNAL LINKS (specific for EC-Number 6.1.1.9)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
