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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + RNA microhelix
?
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 + tRNAHis
AMP + diphosphate + L-histidinyl-tRNAHis
ATP + L-histidine + tRNAHis
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
-
-
?
additional information
?
-
ATP + L-histidine + RNA microhelix
?
-
-
-
-
?
ATP + L-histidine + RNA microhelix
?
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
?
-
-
ATP-diphosphate exchange
-
-
?
additional information
?
-
-
ATP-diphosphate exchange
-
-
?
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidinyl-tRNAHis
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
additional information
?
-
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidinyl-tRNAHis
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
the enzyme is involved in several regulatory mechanisms of the cell metabolism
-
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
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
-
-
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
-
-
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
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
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
-
-
-
-
?
additional information
?
-
-
Caulobacter crescentus HisRS shows very low activity with Escherichia coli tRNAHis
-
-
?
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
?
-
-
determination of enzyme-induced chemotactic activity of human cells, e.g. leukocytes and primary neutrophils, to the enzyme
-
?
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
?
-
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
-
?
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0.008 - 0.6872
L-histidine
0.0038 - 0.124
RNA microhelix
-
0.00096 - 0.0063
synthetic tRNAHis A-1
-
0.0012 - 0.0178
synthetic tRNAHis G-1
-
0.0055 - 0.013
tRNAHisCUA
-
0.000004
tRNAHisII
-
substrate from rabbit reticuloytes
0.00031 - 0.0016
U73tRNAHisGUG
-
0.00034 - 0.015
wild-type full length tRNAHis G-1
-
additional information
additional information
-
0.0442
ATP
-
wild type enzyme, at pH 7.5 and 25°C
0.14
ATP
-
ATP, , wild-type cytoplasmic enzyme
0.22
ATP
-
mutant enzyme form des(A2-Q6), ATP-diphosphate exchange
0.3
ATP
-
mutant enzyme form V-HisRS-R259K, ATP-diphosphate exchange
0.33
ATP
-
mutant enzyme form V-HisRS-R259Q, ATP-diphosphate exchange
0.35
ATP
-
mutant enzyme form V-HisRS, ATP-diphosphate exchange
0.39
ATP
-
mutant enzyme form M-HisRS, ATP-diphosphate exchange
0.5
ATP
-
pH 8.0, 37°C, diphosphate exchange
0.56
ATP
-
HisRS, ATP-diphosphate exchange
0.59
ATP
-
aminoacylation
0.655
ATP
-
mutant enzyme form des(A2-G10)HisRS, ATP-diphosphate exchange
0.74
ATP
-
truncated enzyme form NcatHisRS, ATP-diphosphate exchange
0.89
ATP
-
wild-type HisRS, ATP-diphosphate exchange
0.89
ATP
-
pH 8.0, 37°C, diphosphate exchange
1.763
ATP
-
mutant enzyme Y330C, at pH 7.5 and 25°C
0.0006
His
-
peptite mutant EB2 mitochondrial enzyme
0.0009
His
-
wild-type mitochondrial enzyme
0.001
His
-
petite mutant EB2 cytoplasmic enzyme
0.0018
His
-
wild-type cytoplasmic enzyme
0.0058
His
-
aminoacylation
0.008
His
-
HisRS, aminoacylation
0.011
His
-
mutant enzyme form M-HisRS, aminoacylation
0.017
His
-
mutant enzyme form V-HisRS, mutant enzyme form V-His-RS-R259K, aminoacylation
0.02
His
-
mutant enzyme form des(A2-Q6)-HisRS, aminoacylation
0.025
His
-
aminoacylation
0.03
His
-
wild-type HisRS, ATP-diphosphate exchange
0.046
His
-
tuncated enzyme form NcatHisRS, ATP-diphosphate exchange
0.06
His
-
mutant enzyme form des(A2-G10)-HisRS, aminoacylation
0.08
His
-
wild-type mitochondrial enzyme
0.008
L-histidine
-
wild type enzyme, at pH 7.5 and 25°C
0.009
L-histidine
-
pH 8.0, 37°C, diphosphate exchange
0.0108
L-histidine
-
mutant enzyme S365N, at pH 7.5 and 25°C
0.03
L-histidine
-
pH 8.0, 37°C, diphosphate exchange
0.2029
L-histidine
-
mutant enzyme Y330C, at pH 7.5 and 25°C
0.6872
L-histidine
-
mutant enzyme V155G, at pH 7.5 and 25°C
0.0038
RNA microhelix
-
pH 8.0, 37°C, aminoacylation
-
0.124
RNA microhelix
-
pH 8.0, 37°C, aminoacylation
-
0.00096
synthetic tRNAHis A-1
-
7.5, 37°C, wild-type enzyme
-
0.0026
synthetic tRNAHis A-1
-
7.5, 37°C, enzyme mutant R123A
-
0.0055
synthetic tRNAHis A-1
-
7.5, 37°C, enzyme mutant R9H
-
0.0063
synthetic tRNAHis A-1
-
7.5, 37°C, enzyme mutant R116A
-
0.0012
synthetic tRNAHis G-1
-
7.5, 37°C, wild-type enzyme
-
0.0025
synthetic tRNAHis G-1
-
7.5, 37°C, enzyme mutant R123A
-
0.0081
synthetic tRNAHis G-1
-
7.5, 37°C, enzyme mutant R116A
-
0.0178
synthetic tRNAHis G-1
-
7.5, 37°C, enzyme mutant R9H
-
0.000006
tRNAHis
-
unfractionated substrate from rabbit liver or rabbit reticulocyte tRNAHisI
0.00012
tRNAHis
-
aminoacylation
0.00014
tRNAHis
-
pH 8.0, 37°C, aminoacylation
0.00017
tRNAHis
mutant E83Q, pH 7.5, 37°C
0.000199
tRNAHis
-
mutant enzyme S365N, at pH 7.5 and 25°C
0.00033
tRNAHis
-
mutant enzyme Y330C, at pH 7.5 and 25°C
0.00034
tRNAHis
wild-type, pH 7.5, 37°C
0.00043
tRNAHis
-
pH 7.2, 37°C, wild-type substrate
0.00048
tRNAHis
mutant Q127A, pH 7.5, 37°C
0.00056
tRNAHis
-
truncated enzyme form NcatHisRS, aminoacylation
0.000782
tRNAHis
-
wild type enzyme, at pH 7.5 and 25°C
0.000979
tRNAHis
-
mutant enzyme V155G, at pH 7.5 and 25°C
0.0014
tRNAHis
-
full-length HisRS, aminoacylation
0.00325
tRNAHis
-
wild-type Caulobacter crescentus tRNAHis, pH 7.5, 30°C
0.0033
tRNAHis
mutant R159H, pH 7.5, 37°C
0.00515
tRNAHis
mutant E83A, pH 7.5, 37°C
0.034
tRNAHis
-
pH 8.0, 37°C, aminoacylation
0.0055
tRNAHisCUA
-
tuncated enzyme form NcatHisRS, aminoacylation
-
0.013
tRNAHisCUA
-
full-length HisRS, aminoacylation
-
0.00031
U73tRNAHisGUG
-
tuncated enzyme form NcatHisRS, aminoacylation
-
0.0016
U73tRNAHisGUG
-
full-length HisRS, aminoacylation
-
0.00034
wild-type full length tRNAHis G-1
-
7.5, 37°C, wild-type enzyme
-
0.0048
wild-type full length tRNAHis G-1
-
7.5, 37°C, enzyme mutant R123A
-
0.0058
wild-type full length tRNAHis G-1
-
7.5, 37°C, enzyme mutant R116A
-
0.015
wild-type full length tRNAHis G-1
-
7.5, 37°C, enzyme mutant R9H
-
additional information
additional information
-
kinetics and substrate specificity
-
additional information
additional information
-
kinetics with diverse tRNAHIs variants, overview
-
additional information
additional information
-
Michaelis-Menten kinetics for the wild-type enzyme and recombinant HisRS active site fragments, HisRS1-HisRS4, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0013 - 0.024
RNA microhelix
-
0.002 - 0.024
synthetic tRNAHis A-1
-
0.11 - 6.08
synthetic tRNAHis G-1
-
0.005 - 0.016
U73tRNAHisGUG
-
0.64 - 2.6
wild type tRNAHis
-
0.12 - 4
wild-type full length tRNAHis G-1
-
additional information
additional information
-
-
-
0.17
ATP
-
truncated enzyme form NcatHisRS, ATP-diphosphate exchange
0.2
ATP
-
mutant enzyme form des(A2-G10)-HisRS, ATP-diphosphate exchange
0.4
ATP
-
mutant enzyme form V-HisRS-R259Q, ATP-diphosphate exchange
0.48
ATP
-
mutant enzyme Y330C, at pH 7.5 and 25°C
5.8
ATP
-
wild type enzyme, at pH 7.5 and 25°C
8
ATP
-
enzyme form with N-terminal addition of valine V-HisRS, mutant enzyme form des(A2-Q6)-HisRS, ATP-diphosphate exchange
34
ATP
-
HisRS, ATP-diphosphate exchange
40
ATP
-
pH 8.0, 37°C, diphosphate exchange
120
ATP
-
wild-type HisRS, ATP-diphosphate exchange
130
ATP
-
pH 8.0, 37°C, diphosphate exchange
0.1
His
-
mutant enzyme form V-HisRS-R259K, aminoacylation
0.19
His
-
truncated enzyme form NcatHisRS, ATP-diphosphate exchange
1
His
-
mutant enzyme form des(A2-G10)-HisRS, aminoacylation
6
His
-
enzyme form with N-terminal addition of methionine M-HisRS, enzyme form with N-terminal addition of valineV-HisRS, aminoacylation
7
His
-
wild-type HisRS, aminoacylation
9
His
-
mutant enzyme form des(A2-Q6)-HisRS, aminoacylation, ATP, and mutant enzyme form with N-terminal addition of methionine M-HisRS, ATP-diphosphate exchange
142
His
-
wild-type HisRS, ATP-diphosphate exchange
0.39
L-histidine
-
mutant enzyme S365N, at pH 7.5 and 25°C
0.74
L-histidine
-
mutant enzyme Y330C, at pH 7.5 and 25°C
2.08
L-histidine
-
mutant enzyme V155G, at pH 7.5 and 25°C
4.1
L-histidine
-
wild type enzyme, at pH 7.5 and 25°C
40
L-histidine
-
pH 8.0, 37°C, diphosphate exchange
130
L-histidine
-
pH 8.0, 37°C, diphosphate exchange
0.0013
RNA microhelix
-
pH 8.0, 37°C, aminoacylation
-
0.024
RNA microhelix
-
pH 8.0, 37°C, aminoacylation
-
0.002
synthetic tRNAHis A-1
-
7.5, 37°C, enzyme mutant R123A
-
0.012
synthetic tRNAHis A-1
-
7.5, 37°C, enzyme mutant R116A
-
0.018
synthetic tRNAHis A-1
-
7.5, 37°C, wild-type enzyme
-
0.024
synthetic tRNAHis A-1
-
7.5, 37°C, enzyme mutant R9H
-
0.11
synthetic tRNAHis G-1
-
7.5, 37°C, enzyme mutant R123A
-
0.13
synthetic tRNAHis G-1
-
7.5, 37°C, enzyme mutant R116A
-
0.76
synthetic tRNAHis G-1
-
7.5, 37°C, enzyme mutant R9H
-
4.75
synthetic tRNAHis G-1
-
7.5, 37°C, wild-type enzyme
-
6.08
synthetic tRNAHis G-1
-
7.5, 37°C, enzyme mutant R9H
-
0.0004
tRNAHis
mutant E83A, pH 7.5, 37°C
0.0006
tRNAHis
mutant R159H, pH 7.5, 37°C
0.01
tRNAHis
mutant E83Q, pH 7.5, 37°C
0.048
tRNAHis
mutant Q127A, pH 7.5, 37°C
0.3
tRNAHis
-
mutant enzyme S365N, at pH 7.5 and 25°C
0.417
tRNAHis
-
pH 7.2, 37°C, wild-type substrate
0.42
tRNAHis
-
pH 8.0, 37°C, aminoacylation
0.56
tRNAHis
-
mutant enzyme Y330C, at pH 7.5 and 25°C
1.71
tRNAHis
-
pH 8.0, 37°C, aminoacylation
2.02
tRNAHis
wild-type, pH 7.5, 37°C
3.05
tRNAHis
-
mutant enzyme V155G, at pH 7.5 and 25°C
4
tRNAHis
-
wild-type Caulobacter crescentus tRNAHis, pH 7.5, 30°C
5.4
tRNAHis
-
wild type enzyme, at pH 7.5 and 25°C
0.26
tRNAHisCUA
-
truncated enzyme form NcatHisRS, aminoacylation
-
1.5
tRNAHisCUA
-
full-length HisRS, aminoacylation
-
0.005
U73tRNAHisGUG
-
full-length HisRS, aminoacylation
-
0.016
U73tRNAHisGUG
-
truncated enzyme form NcatHisRS, aminoacylation
-
0.64
wild type tRNAHis
-
truncated enzyme form NcatHisRS, aminoacylation
-
2.6
wild type tRNAHis
-
full-length HisRS, aminoacylation
-
0.12
wild-type full length tRNAHis G-1
-
7.5, 37°C, enzyme mutant R123A
-
1.76
wild-type full length tRNAHis G-1
-
7.5, 37°C, enzyme mutant R116A
-
2.04
wild-type full length tRNAHis G-1
-
7.5, 37°C, wild-type enzyme
-
2.5 - 4
wild-type full length tRNAHis G-1
-
7.5, 37°C, enzyme mutant R9H
-
2.54
wild-type full length tRNAHis G-1
-
7.5, 37°C, enzyme mutant R9H
-
2.94
wild-type full length tRNAHis G-1
-
7.5, 37°C, enzyme mutant R116A
-
2.94
wild-type full length tRNAHis G-1
-
7.5, 37°C, wild-type enzyme
-
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C88V/C196S/C241L
denoted as clHisRS, can not be labeled with maleimide probes
E83A
15fold increase in Km-value, decrease in kcat-value
E83Q
2fold decrease in Km-value, decrease in kcat-value
L276C clHisRS
an additional cysteine is introduced at a solvent-accessible position proximal to substrate binding sites
L402C clHisRS
an additional cysteine is introduced at a solvent-accessible position proximal to substrate binding sites
MDCC-HisRS
fluorescently labeled version of HisRS, conjugated with 7-diethylamino-3-((((2-maleimidyl)ethyl)amino)carbonyl)-coumarin, MDCC, to a cysteine introduced at residue 212, located in the insertion domain
N212C clHisRS
an additional cysteine is introduced at a solvent-accessible position proximal to substrate binding sites
N368C clHisRS
an additional cysteine is introduced at a solvent-accessible position proximal to substrate binding sites
NcatHisRS
-
320-residue fragment, NcatHisRS, truncated immediately following motif 3 catalyzes both the the specific aminoacylation of tRNA and ATP-diphosphate exchange, albeit less efficiently than the full length enzyme. NcatHisRs shows no mischarging of noncognate tRNAs but exhibits reduced selectivity for the C73 discriminator base. NcatHisRs is monomeric, indicating that the C-terminal domain is essential for maintaining the dimeric structure of the enzyme
Q118E
-
site-directed point mutagenesis of an active site residue, reduced kcat but unaltered Km with wild-type tRNAHis G-1
Q127A
decrease in kcat-value
R116A
-
site-directed mutagenesis, reduced activity, increased specificity for the wild-type full length tRNAHis G-1
R123A
-
site-directed point mutagenesis of an active site residue, reduced activity, increased specificity for the wild-type full length tRNAHis G-1
R9H
-
site-directed point mutangenesis, increased activity with wild-type full length tRNAHis G-1, reduced activity with the synthetic tRNAHis G-1 and A-1 substrates, increased specificity for the wild-type full length tRNAHis G-1
V-HisRS-R259K
-
mutants: V-HisRS-R259K, V-HisRS-R259Q, des(A2-G10)-HisRS, des(A2-Q6)-HisRS, V-His-RS with N-terminal addition of valine, and M-HisRS with N-terminal addition of methionine. N-terminal addition of either methionine or valine, or the deletion of 6 amino terminal amino acids deceases the specific aminoacylation activity 2fold to 7fold. Further N-terminal deletions of 10 or 17 amino acids causes 100fold reduced aminoacylation and 10fold reduced ATP-diphosphate exchange. Removal of 18 or more amino acids from the N-terminus results in an inactive enzyme mutants. The two point mutations R259Q and R259K, show blocked histidyl-tRNA synthetase activity without affecting histidine or ATP binding
D175E
-
the mutant with reduced aminoacylation activity is associated with Charcot-Marie-Tooth disease type 2W
D364Y
-
the mutant with reduced aminoacylation activity is associated with Charcot-Marie-Tooth disease type 2W
D48A
-
site-directed mutagenesis, the mutant is cleaved by caspase-6, but not by granzyme B
L200V
-
naturally occuring mutations in HARS2 involved in the Perrault syndrome, the mutant shows reduced activity compared to wild-type enzyme
P134H
-
the mutant with reduced aminoacylation activity is associated with Charcot-Marie-Tooth disease type 2W
R137Q
-
the mutant with reduced aminoacylation activity is associated with Charcot-Marie-Tooth disease type 2W
S356N
-
the mutant with reduced aminoacylation activity is associated with Charcot-Marie-Tooth disease type 2W
T132I
-
the mutant with reduced aminoacylation activity is associated with Charcot-Marie-Tooth disease type 2W
V155G
-
the mutant with reduced aminoacylation activity is associated with Charcot-Marie-Tooth disease type 2W
V368L
-
naturally occuring mutations in HARS2 involved in the Perrault syndrome, the mutant shows reduced activity compared to wild-type enzyme
Y330C
-
the mutant with reduced aminoacylation activity is associated with Charcot-Marie-Tooth disease type 2W
Y454S
-
the mutation is associated with childhood deafness, blindness, and episodic hallucinations during acute illness
325-328Del
the mutant shows about 20% of wild type activity
328insTTET
the mutant shows about 80% of wild type activity
E388A
the mutant shows about 15% of wild type activity
G286A
the mutant shows about 2% of wild type activity
G72V
the mutant shows about 50% of wild type activity
G72V/G73V
the mutant shows about 15% of wild type activity
K209A
the mutant shows about 80% of wild type activity
K397Q
the mutant shows about 10% of wild type activity
Q404A
the mutant shows about 90% of wild type activity
R115A
the mutant shows about 20% of wild type activity
R120A
the mutant shows about 8% of wild type activity
R122A
the mutant shows about 15% of wild type activity
R122K
the mutant shows about 55% of wild type activity
R197A
the mutant shows about 50% of wild type activity
R7A
the mutant shows about 20% of wild type activity
R259H
-
mutant Arg259His, with 1000fold decreased second order rate constant kcat/Km for the ATP-diphosphate exchange, and 500fold decreased kcat/Km for aminoacylation
R259H
10fold increase in Km-value, decrease in kcat-value
additional information
construction of GFP-fusion proteins with the first 71 amino acids of the enzyme sequence, transformation of and expression in Nicotiana tabacum protoplasts, functional targeting to the mitochondria and chloroplasts of tobacco
additional information
-
construction of GFP-fusion proteins with the first 71 amino acids of the enzyme sequence, transformation of and expression in Nicotiana tabacum protoplasts, functional targeting to the mitochondria and chloroplasts of tobacco
additional information
-
RNAi-dependent downregulation of hars-1, embryos from wild-type animals are laid onto bacteria expressing double-stranded RNA and the progeny are exposed to RNAi throughout development
additional information
-
construction of four minimal, active site fragments, urzymes, of Escherichia coli class II HisRS by PCR-based subcloning, the fragments comprise: HisRS1 residues 16-134, HisRS2 residues 10-134, HisRS3 residues 16-134 and 301-320, and HisRS4 residues 10-134 and 301-320. HisRS-3 binds ATP far more tightly and histidine less strongly than native, full-length HisRS or its intact catalytic domain. HisRS-3 urzyme steady-state kinetic parameters differ substantially from those of native full-length HisRS. All urzymes show relative rate enhancements compared to the wild-type enzyme, overview
additional information
-
HisRS granzyme B site mapping using site-directed mutagenesis
additional information
-
identification of a deletion mutant HARS2 DELTA200-211, probably involved in the Perrault syndrome, that is not stably expressed in mammalian mitochondria, its also shows no dimerization
additional information
-
construction of Egr1 null or defect mutants affects HisRS genes, Egr1, Zif268, is an immediate early gene encoding an inducible transcription factor involved in synaptic plasticity and several forms of memory in rodents, allelic differences between mouse strains can introduce variations in differential proteomic analyses of genetically modified organisms
additional information
-
mutational study of the 1:73 base pair recognition by yeats HisRS using two chemically synthesized 24-nucleotide RNA microhelices, overview
additional information
-
overexpression in Escherichia coli, as a fusion protein containing additional 15 amino acids
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Walker, E.J.; Treacy, G.B.; Jeffrey, P.D.
Molecular weights of mitochondrial and cytoplasmic aminoacyl-tRNA synthetases of beef liver and their complexes
Biochemistry
22
1934-1941
1983
Bos taurus
brenda
Airas, R.K.
Differences in the magnesium dependences of the class I and class II aminoacyl-tRNA synthetases from Escherichia coli
Eur. J. Biochem.
240
223-231
1996
Escherichia coli
brenda
Arnez, J.G.; Augustine, J.G.; Francklyn, C.S.
The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase
Proc. Natl. Acad. Sci. USA
8
7144-7149
1997
Escherichia coli
brenda
Menguito, C.A.; Papaconstantinou, J.; Weigel, P.H.
The histidyl-tRNA synthetase from Streptococcus equisimilis: overexpression in Escherichia coli. Purification and characterization
Prep. Biochem.
23
499-472
1993
Streptococcus dysgalactiae subsp. equisimilis
-
brenda
Francklyn, C.; Harris, D.; Moras, D.
Crystallization of histidyl-tRNA synthetase from Escherichia coli
J. Mol. Biol.
241
275-277
1994
Escherichia coli, Escherichia coli overproducing
brenda
Yaremchuk, A.D.; Cusack, S.; Aberg, A.; Gudzera, O.; Kryklivyi, I.; Tukalo, M.
Crystallization of Thermus thermophilus histidyl-tRNA synthetase and its complex with tRNAHis
Proteins Struct. Funct. Genet.
22
426-428
1995
Thermus thermophilus
brenda
Ruhlmann, A.; Cramer, F.; Englisch, U.
Isolation and analysis of mutated histidyl-tRNA synthetases from Escherichia coli
Biochem. Biophys. Res. Commun.
237
192-201
1997
Escherichia coli
brenda
Augustine, J.; Francklyn, C.
Design of an active fragment of a class II aminoacyl-tRNA synthetase and its significance for synthetase evolution
Biochemistry
36
3473-3482
1997
Escherichia coli
brenda
Aberg, A.; Yaremchuk, A.; Tukalo, M.; Rasmussen, B.; Cusack, S.
Crystal structure analysis of the activation of histidine by Thermus thermophilus histidyl-tRNA synthetase
Biochemistry
36
3084-3094
1997
Thermus thermophilus
brenda
Menguito, C.A.; Keherly, M.J.; Tang, C.Y.; Papaconstantinou, J.; Weigel, P.H.
Molecular cloning, sequence, structural analysis and expression of the histidyl-tRNA synthetase gene from Streptococcus equisimilis
Nucleic Acids Res.
21
615-620
1993
Streptococcus dysgalactiae subsp. equisimilis
brenda
Rudinger, J.; Felden, B.; Florentz, C.; Giege, R.
Strategy for RNA recognition by yeast histidyl-tRNA synthetase
Bioorg. Med. Chem.
5
1001-1009
1997
Saccharomyces cerevisiae
brenda
Vazquez-Abad, D.; Carson, J.H.; Rothfield, N.
Localization of histidyl-tRNA synthetase (Jo-1) in human laryngeal epithelial carcinoma cell line HEp-2 cells)
Cell Tissue Res.
286
487-491
1996
Homo sapiens
brenda
Arnez, J.G.; Harris, D.C.; Mitschler, A.; Rees, B.; Francklyn, C.S.; Moras, D.
Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate
EMBO J.
14
4143-4155
1995
Escherichia coli
brenda
De Lorenzo, F.; di Natale, P.; Schechter, A.N.
Chemical and physical studies on the structure of the histidyl transfer ribonucleic acid synthetase from Salmonella typhimurium
J. Biol. Chem.
249
908-913
1974
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
De Lorenzo, F.; Ames, B.N.
Histidine regulation in Salmonella typhimurium. VII. Purification and general properties of the histidyl transfer ribonucleic acid synthetase
J. Biol. Chem.
245
1710-1716
1970
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Kalousek, F.; Konigsberg, W.H.
Purification and characterization of histidyl transfer ribonucleic acid synthetase of Escherichia coli
Biochemistry
13
999-1006
1974
Escherichia coli
brenda
Boguslawski, G.; Vodkin, M.H.; Finkelstein, D.B.; Fink, G.R.
Histidyl-tRNAs and histidyl-tRNA synthetases in wild type and cytoplasmic petite mutants of Saccharomyces cerevisiae
Biochemistry
13
4659-4667
1974
Saccharomyces cerevisiae
brenda
Lepore, G.C.; di Natale, P.; Guarini, L.; de Lorenzo, F.
Histidyl-tRNA synthetase from Salmonella typhimurium: specificity in the binding of histidine analogues
Eur. J. Biochem.
56
369-374
1975
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Di Natale, P.; Schechter, A.N.; Lepore, G.C.; de Lorenzo, F.
Histidyl transfer ribonucleic acid synthetase from Salmonella typhimurium. Interaction with substrate and ATP analogues
Eur. J. Biochem.
62
293-298
1976
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Kane, S.M.; Vugrincic, C.; Finbloom, D.S.; Smith, D.W.E.
Purification and some properties of the histidyl-tRNA synthetase from cytosol of rabbit reticulocytes
Biochemistry
17
1509-1514
1978
Oryctolagus cuniculus
brenda
Chen, C.C.; Somberg, E.W.
Purification and characterization of histidyl-transfer RNA synthetase from Neurospora crassa
Biochim. Biophys. Acta
613
514-525
1980
Neurospora crassa
brenda
Eisenbeis, S.J.; Parker, J.
Strains of Escherichia coli carrying the structural gene for histidyl-tRNA synthetase on a high copy-number plasmid
Mol. Gen. Genet.
183
115-122
1981
Escherichia coli
brenda
Yang, D.C.H.; Dang, C.V.; Arnett, F.C.
Rat liver histidyl-tRNA synthetase. Purification and inhibition by the myositis-specific anti-Jo-1 autoantibody
Biochem. Biophys. Res. Commun.
120
15-21
1984
Homo sapiens, Rattus norvegicus
brenda
Gerken, S.C.; Andrulis, I.L.; Arfin, S.M.
Histidyl-tRNA synthetase of Chinese hamster ovary cells contains phosphoserine
Biochim. Biophys. Acta
869
215-217
1986
Cricetulus griseus
brenda
Walker, E.J.; Jeffrey, P.D.
Purification of bovine liver histidyl-tRNA synthetase, the Jo-1 antigen of polymyositis
Biol. Chem. Hoppe-Seyler
368
531-537
1987
Bos taurus
brenda
Tsui, F.W.L.; Siminovitch, L.
Isolation, structure and expression of mammalian genes for histidyl-tRNA synthetase
Nucleic Acids Res.
15
3349-3367
1987
Homo sapiens
brenda
Fahoum, S.K.; Yang, D.C.H.
Purification of mammalian histidyl-tRNA synthetase and its interaction with myositis-specific anti-Jo-1 antibodies
Biochemistry
26
5871-5877
1987
Rattus norvegicus
brenda
Biswas, T.; Miller, F.W.; Plotz, P.H.
Stimulation and partial stabilization of human histidyl-tRNA synthetase by hemoglobin
FEBS Lett.
229
203-205
1988
Homo sapiens
brenda
Castronuovo Lepore, G.; Geraci, G.; Abrescia, P.; de Lorenzo, F.
Histidyl-transfer-ribonucleic-acid synthetase from Salmonella typhimurium. Studies of the sulfhydryl groups
Eur. J. Biochem.
65
171-176
1976
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
O'Hanlon, T.P.; Miller, F.W.
Genomic organization, transcriptional mapping, and evolutionary implications of the human bi-directional histidyl-tRNA synthetase locus (HARS/HARSL)
Biochem. Biophys. Res. Commun.
294
609-614
2002
Homo sapiens (P12081), Homo sapiens (P49590), Homo sapiens
brenda
Qiu, X.; Janson, C.A.; Blackburn, M.N.; Chhohan, I.K.; Hibbs, M.; Abdel-Meguid, S.S.
Cooperative structural dynamics and a novel fidelity mechanism in histidyl-tRNA synthetases
Biochemistry
38
12296-12304
1999
Staphylococcus aureus (P60911), Staphylococcus aureus
brenda
Connolly, S.A.; Rosen, A.E.; Musier-Forsyth, K.; Francklyn, C.S.
G-1:C73 recognition by an arginine cluster in the active site of Escherichia coli histidyl-tRNA synthetase
Biochemistry
43
962-969
2004
Escherichia coli
brenda
Freist, W.; Verhey, J.F.; Ruhlmann, A.; Gauss, D.H.; Arnez, J.G.
Histidyl-tRNA synthetase
Biol. Chem.
380
623-646
1999
Archaeoglobus fulgidus (O28631), Salmonella enterica subsp. enterica serovar Typhimurium (O52765), Mesocricetus auratus (P07178), Saccharomyces cerevisiae (P07263), Homo sapiens (P12081), Homo sapiens (P49590), Streptococcus dysgalactiae subsp. equisimilis (P30053), Caenorhabditis elegans (P34183), Haemophilus influenzae (P43823), Mycobacterium leprae (P46696), Mycoplasma genitalium (P47281), Porphyra purpurea (P51348), Thermus thermophilus (P56194), Thermus thermophilus, Helicobacter pylori (P56455), Escherichia coli (P60906), Escherichia coli, Takifugu rubripes (P70076), Mycoplasma pneumoniae (P75069), Oryza sativa (P93422), Mycobacterium tuberculosis (P9WFV5), Synechococcus sp. (Q55267), Synechocystis sp. (Q55653), Methanocaldococcus jannaschii (Q58406), Mus musculus (Q61035), Mycobacterium tuberculosis H37Rv (P9WFV5)
brenda
Akashi, K.; Grandjean, O.; Small, I.
Potential dual targeting of an Arabidopsis archaebacterial-like histidyl-tRNA synthetase to mitochondria and chloroplasts
FEBS Lett.
431
39-44
1998
Arabidopsis thaliana (O82413), Arabidopsis thaliana
brenda
Howard, O.M.; Dong, H.F.; Yang, D.; Raben, N.; Nagaraju, K.; Rosen, A.; Casciola-Rosen, L.; Hartlein, M.; Kron, M.; Yiadom, K.; Dwivedi, S.; Plotz, P.H.; Oppenheim, J.J.
Histidyl-tRNA synthetase and asparaginyl-tRNA synthetase, autoantigens in myositis, activate chemokine receptors on T lymphocytes and immature dendritic cells
J. Exp. Med.
196
781-791
2002
Homo sapiens
brenda
Felden, B.; Giege, R.
Resected RNA pseudoknots and their recognition by histidyl-tRNA synthetase
Proc. Natl. Acad. Sci. USA
95
10431-10436
1998
Saccharomyces cerevisiae
brenda
Guth, E.; Connolly, S.H.; Bovee, M.; Francklyn, C.S.
A substrate-assisted concerted mechanism for aminoacylation by a class II aminoacyl-tRNA synthetase
Biochemistry
44
3785-3794
2005
Escherichia coli (P60906), Escherichia coli
brenda
Rosen, A.E.; Musier-Forsyth, K.
Recognition of G-1:C73 atomic groups by Escherichia coli histidyl-tRNA synthetase
J. Am. Chem. Soc.
126
64-65
2004
Escherichia coli
brenda
Kamei, H.
Intracellular localization of histidyl-tRNA synthetase/Jo-1 antigen in T24 cells and some other cells
J. Autoimmun.
22
201-210
2004
Homo sapiens
brenda
Levine, S.M.; Raben, N.; Xie, D.; Askin, F.B.; Tuder, R.; Mullins, M.; Rosen, A.; Casciola-Rosen, L.A.
Novel conformation of histidyl-transfer RNA synthetase in the lung: the target tissue in Jo-1 autoantibody-associated myositis
Arthritis Rheum.
56
2729-2739
2007
Homo sapiens
brenda
Chardonnet, S.; Decottignies, P.; Amar, L.; Le Caer, J.P.; Davis, S.; Laroche, S.; Le Marechal, P.
New mortalin and histidyl tRNA synthetase isoforms point out a pitfall in proteomic analysis of Egr1 genetically modified mice
Proteomics
7
289-298
2007
Mus musculus
brenda
Rosen, A.E.; Brooks, B.S.; Guth, E.; Francklyn, C.S.; Musier-Forsyth, K.
Evolutionary conservation of a functionally important backbone phosphate group critical for aminoacylation of histidine tRNAs
RNA
12
1315-1322
2006
Saccharomyces cerevisiae, Escherichia coli
brenda
Wegner, N.; Wait, R.; Venables, P.J.
Evolutionarily conserved antigens in autoimmune disease: Implications for an infective aetiology
Int. J. Biochem. Cell Biol.
41
390-397
2008
Homo sapiens
brenda
Polosa, R.; Di Mauro, C.; Spampinato, B.; Castelli, L.; DAmico, G.; Edwards, C.J.; Russo, C.
A patient with antihistidyl-tRNA synthetase positive polymyositis presenting as acute respiratory distress syndrome
J. Clin. Rheumatol.
14
219-221
2008
Homo sapiens
brenda
Ardell, D.H.; Andersson, S.G.
TFAM detects co-evolution of tRNA identity rules with lateral transfer of histidyl-tRNA synthetase
Nucleic Acids Res.
34
893-904
2006
Ruegeria pomeroyi (Q5LVN3), Ruegeria pomeroyi
brenda
Guth, E.; Farris, M.; Bovee, M.; Francklyn, C.S.
Asymmetric amino acid activation by class II histidyl-tRNA synthetase from Escherichia coli
J. Biol. Chem.
284
20753-20762
2009
Escherichia coli (P60906), Escherichia coli
brenda
Merritt, E.A.; Arakaki, T.L.; Gillespie, J.R.; Larson, E.T.; Kelley, A.; Mueller, N.; Napuli, A.J.; Kim, J.; Zhang, L.; Verlinde, C.L.; Fan, E.; Zucker, F.; Buckner, F.S.; van Voorhis, W.C.; Hol, W.G.
Crystal structures of trypanosomal histidyl-tRNA synthetase illuminate differences between eukaryotic and prokaryotic homologs
J. Mol. Biol.
397
481-494
2010
Trypanosoma brucei (Q4DA54), Trypanosoma brucei, Trypanosoma cruzi (Q4DA54), Trypanosoma cruzi
brenda
Banik, S.D.; Nandi, N.
Aminoacylation reaction in the histidyl-tRNA synthetase: fidelity mechanism of the activation step
J. Phys. Chem. B
114
2301-2311
2010
Escherichia coli (P60906), Escherichia coli
brenda
Casciola-Rosen, L.
Histidyl-transfer RNA synthetase: A key participant in idiopathic inflammatory myopathies
Arthritis Rheum.
63
331-333
2011
Homo sapiens, Mus musculus
brenda
Banik, S.D.; Nandi, N.
Influence of the conserved active site residues of histidyl tRNA synthetase on the mechanism of aminoacylation reaction
Biophys. Chem.
158
61-72
2011
Escherichia coli, Thermus thermophilus, Staphylococcus aureus
brenda
Li, L.; Weinreb, V.; Francklyn, C.; Carter, C.W.
Histidyl-tRNA synthetase urzymes: class I and II aminoacyl tRNA synthetase urzymes have comparable catalytic activities for cognate amino acid activation
J. Biol. Chem.
286
10387-10395
2011
Escherichia coli
brenda
Yuan, J.; Gogakos, T.; Babina, A.M.; Soell, D.; Randau, L.
Change of tRNA identity leads to a divergent orthogonal histidyl-tRNA synthetase/tRNAHis pair
Nucleic Acids Res.
39
2286-2293
2011
Caulobacter vibrioides
brenda
Su, D.; Lieberman, A.; Lang, B.F.; Simonovic, M.; Soell, D.; Ling, J.
An unusual tRNAThr derived from tRNAHis reassigns in yeast mitochondria the CUN codons to threonine
Nucleic Acids Res.
39
4866-4874
2011
Saccharomyces cerevisiae
brenda
Pierce, S.B.; Chisholm, K.M.; Lynch, E.D.; Lee, M.K.; Walsh, T.; Opitz, J.M.; Li, W.; Klevit, R.E.; King, M.C.
Mutations in mitochondrial histidyl tRNA synthetase HARS2 cause ovarian dysgenesis and sensorineural hearing loss of Perrault syndrome
Proc. Natl. Acad. Sci. USA
108
6543-6548
2011
Caenorhabditis elegans, Homo sapiens
brenda
van Dooren, S.H.; Raijmakers, R.; Pluk, H.; Lokate, A.M.; Koemans, T.S.; Spanjers, R.E.; Heck, A.J.; Boelens, W.C.; van Venrooij, W.J.; Pruijn, G.J.
Oxidative stress-induced modifications of histidyl-tRNA synthetase affect its tRNA aminoacylation activity but not its immunoreactivity
Biochem. Cell Biol.
89
545-553
2011
Homo sapiens
brenda
Fernandez, I.; Harlow, L.; Zang, Y.; Liu-Bryan, R.; Ridgway, W.M.; Clemens, P.R.; Ascherman, D.P.
Functional redundancy of MyD88-dependent signaling pathways in a murine model of histidyl-transfer RNA synthetase-induced myositis
J. Immunol.
191
1865-1872
2013
Homo sapiens
brenda
Nagatoyo, Y.; Iwaki, J.; Suzuki, S.; Kuno, A.; Hasegawa, T.
Molecular recognition of histidine tRNA by histidyl-tRNA synthetase from hyperthermophilic archaeon, Aeropyrum pernix K1
Nucleic Acids Symp. Ser.
2005
307-308
2005
Aeropyrum pernix (Q9YEB2), Aeropyrum pernix DSM 11879 (Q9YEB2)
brenda
Koh, C.Y.; Siddaramaiah, L.K.; Ranade, R.M.; Nguyen, J.; Jian, T.; Zhang, Z.; Gillespie, J.R.; Buckner, F.S.; Verlinde, C.L.; Fan, E.; Hol, W.G.
A binding hotspot in Trypanosoma cruzi histidyl-tRNA synthetase revealed by fragment-based crystallographic cocktail screens
Acta Crystallogr. Sect. D
71
1684-1698
2015
Trypanosoma cruzi (Q4DA54), Trypanosoma cruzi
brenda
Abbott, J.A.; Guth, E.; Kim, C.; Regan, C.; Siu, V.M.; Rupar, C.A.; Demeler, B.; Francklyn, C.S.; Robey-Bond, S.M.
The Usher Syndrome Type IIIB histidyl-tRNA synthetase mutation confers temperature sensitivity
Biochemistry
56
3619-3631
2017
Homo sapiens
brenda
Englert, M.; Vargas-Rodriguez, O.; Reynolds, N.M.; Wang, Y.S.; Soell, D.; Umehara, T.
A genomically modified Escherichia coli strain carrying an orthogonal E. coli histidyl-tRNA synthetase tRNAHis pair
Biochim. Biophys. Acta
1861
3009-3015
2017
Caulobacter vibrioides
brenda
Koh, C.Y.; Wetzel, A.B.; de van der Schueren, W.J.; Hol, W.G.
Comparison of histidine recognition in human and trypanosomatid histidyl-tRNA synthetases
Biochimie
106
111-120
2014
Homo sapiens (P12081), Homo sapiens, Trypanosoma brucei (Q4DA54), Trypanosoma brucei, Trypanosoma brucei CL Brener (Q4DA54)
brenda
Lee, Y.H.; Chang, C.P.; Cheng, Y.J.; Kuo, Y.Y.; Lin, Y.S.; Wang, C.C.
Evolutionary gain of highly divergent tRNA specificities by two isoforms of human histidyl-tRNA synthetase
Cell. Mol. Life Sci.
74
2663-2677
2017
Bacillus subtilis, Saccharomyces cerevisiae, Homo sapiens
brenda
Abbott, J.A.; Meyer-Schuman, R.; Lupo, V.; Feely, S.; Mademan, I.; Oprescu, S.N.; Griffin, L.B.; Alberti, M.A.; Casasnovas, C.; Aharoni, S.; Basel-Vanagaite, L.; Zuechner, S.; De Jonghe, P.; Baets, J.; Shy, M.E.; Espinos, C.; Demeler, B.; Antonellis, A.; Francklyn, C.
Substrate interaction defects in histidyl-tRNA synthetase linked to dominant axonal peripheral neuropathy
Hum. Mutat.
39
415-432
2018
Homo sapiens
brenda
Zhou, J.J.; Wang, F.; Xu, Z.; Lo, W.S.; Lau, C.F.; Chiang, K.P.; Nangle, L.A.; Ashlock, M.A.; Mendlein, J.D.; Yang, X.L.; Zhang, M.; Schimmel, P.
Secreted histidyl-tRNA synthetase splice variants elaborate major epitopes for autoantibodies in inflammatory myositis
J. Biol. Chem.
289
19269-19275
2014
Homo sapiens
brenda
Dutta, S.; Kundu, S.; Saha, A.; Nandi, N.
Dynamics of the active site loops in catalyzing aminoacylation reaction in seryl and histidyl tRNA synthetases
J. Biomol. Struct. Dyn.
36
878-892
2018
Thermus thermophilus
brenda
Tian, Q.; Wang, C.; Liu, Y.; Xie, W.
Structural basis for recognition of G-1-containing tRNA by histidyl-tRNA synthetase
Nucleic Acids Res.
43
2980-2990
2015
Thermus thermophilus (P62374)
brenda