6.1.1.21: histidine-tRNA ligase
This is an abbreviated version!
For detailed information about histidine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.21
-
6.1.1.21
-
synthetases
-
aminoacylation
-
aminoacyl-trna
-
autoantibody
-
histidylation
-
myositis
-
anti-jo-1
-
polymyositis
-
anticodon
-
dermatomyositis
-
aarss
-
perrault
-
hiss
-
histidinol
-
anti-synthetase
-
guanylyltransferase
-
hsd17b4
-
myositis-specific
-
c10orf2
-
thrrs
-
threonyl-trna
-
trna-like
-
acid-starved
-
seryl-trna
-
analysis
-
medicine
- 6.1.1.21
- synthetases
- aminoacylation
- aminoacyl-trna
- autoantibody
-
histidylation
- myositis
-
anti-jo-1
- polymyositis
-
anticodon
- dermatomyositis
-
aarss
-
perrault
- hiss
- histidinol
-
anti-synthetase
-
guanylyltransferase
- hsd17b4
-
myositis-specific
- c10orf2
- thrrs
- threonyl-trna
-
trna-like
-
acid-starved
- seryl-trna
- analysis
- medicine
Reaction
Synonyms
antihistidyl-tRNA synthetase, class II histidyl-tRNA synthetase, HARS, HARS1, HARS2, HisRS, HisRS-1, HisRS-2, Histidine translase, Histidine--tRNA ligase, Histidine--tRNA ligase homolog, histidine-tRNA ligase, histidine-tRNA ligase homolog, histidyl tRNA synthetase, Histidyl-transfer ribonucleate synthetase, histidyl-transfer RNA synthetase, Histidyl-tRNA synthetase, HRS, HTS1, Jo-1, Jo-1 antigen, mitochondrial histidyl tRNA synthetase, Synthetase, histidyl-transfer ribonucleate
ECTree
6.1.1.21 histidine-tRNA ligaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 6.1.1.21 - histidine-tRNA ligase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 1-methyl-L-histidine + tRNAHis
AMP + diphosphate + 1-methyl-L-histidyl-tRNAHis
-
-
-
-
?
ATP + 2-thio-L-histidine + tRNAHis
AMP + diphosphate + 2-thio-L-histidyl-tRNAHis
-
low activity
-
-
?
ATP + 3-methyl-L-histidine + tRNAHis
AMP + diphosphate + 3-methyl-L-histidyl-tRNAHis
-
-
-
-
?
ATP + D-histidine + tRNAHis
AMP + diphosphate + D-histidyl-tRNAHis
-
-
-
-
?
ATP + L-histidine + minimalist RNA structures in a resected pseudoknot fold
AMP + diphosphate + L-histidyl-tRNAHis
-
specifically recognized substrate, derived from tyrosine-accepting tRNA-like domain of brome mosaic virus RNA
-
?
ATP + L-histidine + synthetic tRNAHis A-1
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + synthetic tRNAHis G-1
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHisCUA
AMP + diphosphate + L-histidyl-tRNAHisCUA
-
-
-
-
?
ATP + L-histidine + tyrosine-accepting tRNA-like domain of brome mosaic virus RNA
AMP + diphosphate + L-histidyl-tyrosine-accepting tRNA-like domain of brome mosaic virus RNA
-
specifically recognized substrate
-
?
ATP + L-histidine + U73tRNAHisGUG
AMP + diphosphate + L-histidyl-U73tRNAHisGUG
-
-
-
-
?
ATP + L-histidine + wild type tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
-
?
ATP + L-histidine + wild-type full length tRNAHis G-1
AMP + diphosphate + L-histidyl-tRNAHis
-
activity is highly dependent upon the recognition of the unique G-1:C73 base pair and the 5'-monophosphate
-
?
dATP + L-histidine + tRNAHis
dAMP + diphosphate + L-histidyl-tRNAHis
-
very poor substrate
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidinyl-tRNAHis
-
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidinyl-tRNAHis
-
all histidine tRNA molecules have an extra nucleotide, G-1, at the 59 end of the acceptor stem, importance of the G-1:C73 base pair to tRNAHisc, identity, specifically the 59-monophosphate of G-1 and the major groove amine of C73 are recognized by the enzyme of Escherichia coli stabilizing the reaction transition state
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidinyl-tRNAHis
-
strong association of autoantibodies, specificity recognizing the enzyme's granzyme B binding site of the lung enzyme, to HisRS with interstitial lung disease in patients with myositis
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidinyl-tRNAHis
-
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidinyl-tRNAHis
-
all histidine tRNA molecules have an extra nucleotide, G-1, at the 59 end of the acceptor stem, G-1:C73 base pair binding analysis of the yeast enzyme
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
the anticodon is not recognized by the histidyl-tRNA synthetase similar to that of Escherichia coli histidine tRNA recognition system. Discriminator base C73 is weekly recognized and an additional G residue is specifically recognized by the enzyme
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
the anticodon is not recognized by the histidyl-tRNA synthetase similar to that of Escherichia coli histidine tRNA recognition system. Discriminator base C73 is weekly recognized and an additional G residue is specifically recognized by the enzyme
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
best substrate
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
also active with tRNAHisCUA, very weak activity with U73tRNAHisGUG
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
the enzyme is involved in several regulatory mechanisms of the cell metabolism
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
phylogenetic and evolutionary development
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
strategy for RNA recognition by the enzyme
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
the cytoplasmic enzyme efficiently charges bulk E. coli tRNA, the mitochondrial enzyme does not charge it
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
active with wild-type and mutant C73A and A37 insertion tRNAHis
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
histidine A motif, Arg257-Tyr262, is essential for substrate recognition, a loop, Gly52-Lys62, controls the communication between histidine and ATP binding sites, the motif loop, Glu114-Arg120, binds ATP, an insertion domain binds tRNA
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
the enzyme is involved in several regulatory mechanisms of the cell metabolism
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
Trypanosoma brucei CL Brener
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
-
?
additional information
?
-
-
the enzyme recognizes only tRNAHis with cytosine73 but not with adenine73
-
-
?
additional information
?
-
-
Caulobacter crescentus HisRS shows very low activity with Escherichia coli tRNAHis
-
-
?
additional information
?
-
-
no activity with DL-alpha-methyl-histidine, benzyl-L-histidine, 3-[4-thiazolyl]-L-alanine, 2-[thiazolyl]-L-alanine, 1,2,4-triazole-alanine, 2-furyl-L-alanine, 3-cyclopentane-L-alanine, and [3-thienyl]-DL-alanine
-
-
?
additional information
?
-
-
substrate specificity for the N-1 base of wild-type enzyme and mutants, overview
-
?
additional information
?
-
the enzyme can act as an important antigen in autoimmune diseases such as rheumatic arthritis or myositis
-
?
additional information
?
-
-
the enzyme can act as an important antigen in autoimmune diseases such as rheumatic arthritis or myositis
-
?
additional information
?
-
-
binding of a chemically synthesized 24-nucleotide RNA microhelix, which recapitulates the acceptor stem of Escherichia coli tRNAHis, functional group analysis, overview
-
-
?
additional information
?
-
-
determination of enzyme-induced chemotactic activity of human cells, e.g. leukocytes and primary neutrophils, to the enzyme
-
?
additional information
?
-
-
the enzyme recognizes tRNAHis with cytosine73 or adenine73
-
-
?
additional information
?
-
-
1. plays an important role in the regulation of protein degradation as well as in protein biosynthesis. 2. involvement of tRNAHis and possibly histidyl-tRNA synthetase in a nonlysosomal ubiquitin-dependent and ATP-dependent protein degradation pathway. 3. involvement in autoimmune diseases
-
-
?
additional information
?
-
TFAM, an automated, statistical method to classify the identity of tRNAs. TFAM is an effective tool for the bioinformatics, comparative genomics and evolutionary study of tRNA identity
-
-
?
additional information
?
-
-
TFAM, an automated, statistical method to classify the identity of tRNAs. TFAM is an effective tool for the bioinformatics, comparative genomics and evolutionary study of tRNA identity
-
-
?
additional information
?
-
-
substrate specificty, overview
-
?
additional information
?
-
-
binding of a chemically synthesized 24-nucleotide RNA microhelix, which recapitulates the acceptor stem of Saccharomyces cervisiae tRNAHis, functional group analysis, overview
-
-
?
additional information
?
-
-
addition of a first nucleotide to tRNAThr1 allows efficient histidylation by histidyl-tRNA synthetase. Loss of the first nucleotide of wild-type tRNAHis converts it to a substrate for threonyl-tRNA sythetase, EC 6.1.1.3
-
-
?
additional information
?
-
-
the enzyme recognizes tRNAHis with cytosine73 or adenine73 and a slight preference for adenine7
-
-
?
additional information
?
-
-
ATP-diphosphate exchange
-
-
?
additional information
?
-
the enzyme can act as an important antigen in autoimmune diseases such as rheumatic arthritis or myositis
-
?
additional information
?
-
-
the enzyme can act as an important antigen in autoimmune diseases such as rheumatic arthritis or myositis
-
?
