Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

6.1.1.5: isoleucine-tRNA ligase

This is an abbreviated version!
For detailed information about isoleucine-tRNA ligase, go to the full flat file.

Word Map on EC 6.1.1.5

Reaction

ATP
+
L-isoleucine
 +
tRNAIle
=
AMP
 +
diphosphate
 +
L-isoleucyl-tRNAIle

Synonyms

EcIleRS, IARS2, Ile-tRNA synthetase, IleRS, ileS, ileS1, ileS2, IRS, Isoleucine translase, Isoleucine--tRNA ligase, Isoleucine-transfer RNA ligase, Isoleucine-tRNA synthetase, isoleucyl tRNA synthetase, Isoleucyl-transfer ribonucleate synthetase, Isoleucyl-transfer RNA synthetase, Isoleucyl-tRNA synthetase, mitochondrial isoleucyl-tRNA synthetase, More, mt isoleucyl-tRNA synthetase, mt-IleRS, Mupirocin resistance protein, ScIleRS, SgIleRS, Synthetase, isoleucyl-transfer ribonucleate

ECTree

     6 Ligases
         6.1 Forming carbon-oxygen bonds
             6.1.1 Ligases forming aminoacyl-tRNA and related compounds
                6.1.1.5 isoleucine-tRNA ligase

Engineering

Engineering on EC 6.1.1.5 - isoleucine-tRNA ligase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T233P
AIleRS
-
mutant enzymes IleRS(C922S) and AIleRS with replacement of Cys922 through Ala939 with a 33 amino acid peptide unable to bind zinc. Mutant enzymes have altered zinc binding and aminoacylation activity
D342A
IleRS(C922S)
-
mutant enzymes IleRS(C922S) and AIleRS with replacement of Cys922 through Ala939 with a 33 amino acid peptide unable to bind zinc. Mutant enzymes have altered zinc binding and aminoacylation activity
T243R
-
site-directed mutagenesis, the mutant retains tRNA-independent editing at a level identical to the WT enzyme and shows increased ATP hydrolysis compared to the wild-type enzyme
T243R/D342A
-
site-directed mutagenesis, the IleRS CP1 domain mutant is unable to deacylate misacylated tRNA even at high enzyme concentrations
Y59F
site-directed mutagenesis, mutation of a conserved residue located within the active site of bacterial IleRS, directly adjacent to the binding site for the 3'-terminal hydroxyl group of tRNA, aminacylation activity is about 35fold reduced compared to the wild-type enzyme
Y59F/D342A
site-directed mutagenesis, the mutant activity is similar to the wild-type
Y59T
site-directed mutagenesis, mutation of a conserved residue located within the active site of bacterial IleRS, directly adjacent to the binding site for the 3'-terminal hydroxyl group of tRNA, Km and kcat values measured for Y59T are increased by 10fold and decreased by 5fold, respectively, for both isoleucine and valine substrates compared to the wild-type enzyme, aminacylation activity is about 12fold reduced
Y59T/D342A
site-directed mutagenesis, kinetic analysis of Y59F/D342A IleRS does not provide reliable results because of the very slow aminoacylation/misacylation
E708K
naturally occuring mutation found in a heterozygous patient, the mutation is at the junction of the catalytic core domain and the anticodon-binding domain, and is predicted to be disease-causing
P909L
naturally occuring mutation causing the recessive disorder CAGSSS, phenotype, overview
W607X
naturally occuring mutation found in a heterozygous patient, the mutation truncates the protein removing 405 amino acids and is expected to be severely pathogenic
G590D
L810F
-
naturally occuring mutation in the cytoplasmic IleRS responsible for thiaisoleucine-resistance in the parasite, phenotype, overview
D333A
P184T
-
naturally occuring mutation that restores fitness in mupirocin resistant strains
Q420H
-
naturally occuring mutation that restores fitness in mupirocin resistant strains
F227L
the naturally occuring mutation affects the muciprocin binding
H581L/L583H
site-directed mutagenesis, slightly reduced enzyme activity
K226T
the naturally occuring mutation affects the muciprocin binding
P187F
the naturally occuring mutation affects the muciprocin binding
Q612H
the naturally occuring mutation is involved in stabilizing the conformation of the catalytic loop containing the KMSKS motif
V588F
the naturally occuring mutation affects the Rossman fold and leads to low-level mupirocin resistance
V767D
the naturally occuring mutation affects the muciprocin binding
D334A
-
site-directed mutagenesis, the post-transfer editing-defective mutant of SgIleRS displays the similar rates of aminoacylation and AMP formation in the presence of valine, exhibiting a kAMP/kVal-tRNA ratio of 1.1. Stoichiometric ATP consumption in Val-tRNAIle synthesis demonstrates the lack of proofreading by D334A SgIleRS, arguing against hydrolysis of Val-AMP alongside aminoacylation within the synthetic site, SgIleRS naturally lacks tRNA-dependent pre-transfer editing
H319A
site-directed mutagenesis, Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain, but the mutant shows detectable editing activities against the cognate isoleucine, mechanism, overview
T223A
site-directed mutagenesis, Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain, but the mutant shows detectable editing activities against the cognate isoleucine, mechanism, overview
W227A
site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme
W227F
site-directed mutagenesis, the mutant shows editing activities which are unaltered compared to the wild-type enzyme
W227H
site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme
W227L
site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme
W227V
site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme
W227Y
site-directed mutagenesis, the mutant shows editing activities which are unaltered compared to the wild-type enzyme
D539A/W541A
-
catalytically inactive
additional information