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AMP + diphosphate + L-cysteinyl-tRNACys
ATP + L-cysteine + tRNACys
-
-
-
-
r
ATP + 2-aminobutyric acid + tRNACys
AMP + diphosphate + L-alpha-aminobutyryl-tRNACys
ATP + L-cysteine + tRNA1Cys
AMP + diphosphate + L-cysteinyl-tRNA1Cys
-
substrate tRNA1Cys isoacceptor 1
-
-
?
ATP + L-cysteine + tRNA1CysA33U
AMP + diphosphate + L-cysteinyl-tRNA1CysA33U
-
substrate tRNA1CysA33U isoacceptor 1, containing a A33U mutation
-
-
?
ATP + L-cysteine + tRNA2Cys
AMP + diphosphate + L-cysteinyl-tRNA2Cys
-
substrate tRNA2Cys isoacceptor 2
-
-
?
ATP + L-cysteine + tRNA3Cys
AMP + diphosphate + L-cysteinyl-tRNA3Cys
-
substrate tRNA3Cys isoacceptor 3
-
-
?
ATP + L-cysteine + tRNA3CysC20U/U21C/A44U/C46A/A47G
AMP + diphosphate + L-cysteinyl-tRNA3CysC20U/U21C/A44U/C46A/A47G
-
substrate tRNA3CysC20U/U21C/A44U/C46A/A47G isoacceptor 3, containing a C20U/U21C/A44U/C46A/A47G mutation
-
-
?
ATP + L-cysteine + tRNA3CysC20U/U21C/A44U/C46A/A47G/G57A
AMP + diphosphate + L-cysteinyl-tRNA3CysC20U/U21C/A44U/C46A/A47G/G57A
-
substrate tRNA3CysC20U/U21C/A44U/C46A/A47G/G57A isoacceptor 3, containing a C20U/U21C/A44U/C46A/A47G/G57A mutation
-
-
?
ATP + L-cysteine + tRNA3CysG57A
AMP + diphosphate + L-cysteinyl-tRNA3CysG57A
-
substrate tRNA3CysG57A isoacceptor 3, containing a G57A mutation
-
-
?
ATP + L-cysteine + tRNA3CysU33A
AMP + diphosphate + L-cysteinyl-tRNA3CysU33A
-
substrate tRNA3CysU33A isoacceptor 3, containing a U33A mutation
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
ATP + L-cysteine + tRNACys mutant
AMP + diphosphate + L-cysteinyl-tRNACys mutant
-
tRNA substrate is a tRNACys with mutation at the core tertiary Levitt pair from wild-type G15.C48 to mutant G15.G48, leading to a higher activity
-
?
ATP + L-cysteine + tRNACysA36G
AMP + diphosphate + L-cysteinyl-tRNACysA36G
-
relative activity compared to wild-type tRNACys as a substrate: 0.01
-
-
?
ATP + L-cysteine + tRNACysC35U
AMP + diphosphate + L-cysteinyl-tRNACysC35U
-
relative activity compared to wild-type tRNACys as a substrate: 0.005
-
-
?
ATP + L-cysteine + tRNACysG15C/C48G
AMP + diphosphate + L-cysteinyl-tRNACysG15C/C48G
-
relative activity compared to wild-type tRNACys as a substrate: 0.03
-
-
?
ATP + L-cysteine + tRNACysG34C
AMP + diphosphate + L-cysteinyl-tRNACysG34C
-
relative activity compared to wild-type tRNACys as a substrate: 0.001
-
-
?
ATP + L-cysteine + tRNACysU73G
AMP + diphosphate + L-cysteinyl-tRNACysU73G
-
relative activity compared to wild-type tRNACys as a substrate: 0.00002
-
-
?
ATP + L-cysteine + tRNAGln duoble-mutant
AMP + diphosphate + L-cysteinyl-tRNAGln double-mutant
-
tRNA substrate is a tRNAGln with introduced tRNACys indentitiy nucleotides at the acceptor and anticodon ends and a core tertiary Levitt pair equivalent to tRNAGln of G15.G48, poor activity
-
?
ATP + L-cysteine + tRNAGln mutant
AMP + diphosphate + L-cysteinyl-tRNAGln mutant
-
tRNA substrate is a tRNAGln with introduced tRNACys indentitiy nucleotides at the acceptor and anticodon ends and a core tertiary Levitt pair equivalent to tRNACys of G15.C48
-
?
ATP + selenocysteine + tRNACys
AMP + diphosphate + selenocysteinyl-tRNACys
L-Cysteinyl-tRNACys
Cysteine thiolactone + ?
-
deacylation in which nucleophilic sulfur of the side chain of cysteine in Cys-tRNACys attacks its carboxyl carbon, synthesis of Cys-tRNACys and cyclization of cysteine to thiolactone occur in a single active site
-
?
additional information
?
-
ATP + 2-aminobutyric acid + tRNACys
AMP + diphosphate + L-alpha-aminobutyryl-tRNACys
-
-
-
-
?
ATP + 2-aminobutyric acid + tRNACys
AMP + diphosphate + L-alpha-aminobutyryl-tRNACys
-
-
-
-
?
ATP + 2-aminobutyric acid + tRNACys
AMP + diphosphate + L-alpha-aminobutyryl-tRNACys
-
-
-
-
?
ATP + 2-aminobutyric acid + tRNACys
AMP + diphosphate + L-alpha-aminobutyryl-tRNACys
-
-
-
-
?
ATP + 2-aminobutyric acid + tRNACys
AMP + diphosphate + L-alpha-aminobutyryl-tRNACys
-
-
-
-
?
ATP + 2-aminobutyric acid + tRNACys
AMP + diphosphate + L-alpha-aminobutyryl-tRNACys
-
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
tRNACys mutants: greatest loss of activity caused by mutation of a single nucleotide, occurs when the discriminator U73 is changed, mutations in the wobble nucleotide of the anticodon also cause reductions in the specificity constant of 3 orders of magnitude, while mutations in the other anticodon nucleotides causes lesser effects
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
enzyme is highly specific for L-cysteine and does not possess the editing activity characteristic for other tRNA synthetases
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
enzyme is highly specific for L-cysteine without performing an editing reaction, tightly bound zinc is the primary determinant of selectivity against non-cognate amino acids
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
the attachment of cysteine to tRNACys by the class I cysteinyl-tRNA synthetase is flexible. The enzyme is capable of using either the 2' or 3'-hydroxyl group as the attachment site
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
the enzyme is rate-limited by release of aminoacyl-tRNA
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
a two-step process of amino acid activation as first step, and aminocylation as second step
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
the canonical enzyme is not essential for viability of the archaeon Methanococcus maripaludis probably due to the dual-specific ProCys-tRNA synthetase
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + selenocysteine + tRNACys
AMP + diphosphate + selenocysteinyl-tRNACys
-
-
-
-
?
ATP + selenocysteine + tRNACys
AMP + diphosphate + selenocysteinyl-tRNACys
-
-
-
-
?
ATP + selenocysteine + tRNACys
AMP + diphosphate + selenocysteinyl-tRNACys
-
-
-
-
?
ATP + selenocysteine + tRNACys
AMP + diphosphate + selenocysteinyl-tRNACys
-
-
-
-
?
ATP + selenocysteine + tRNACys
AMP + diphosphate + selenocysteinyl-tRNACys
-
-
-
-
?
additional information
?
-
-
ATP-diphosphate exchange
-
-
?
additional information
?
-
-
2-aminobutyric acid can replace cysteine in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
ATP-diphosphate exchange
-
-
?
additional information
?
-
-
selenocysteine can replace cysteine in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
2-aminobutyric acid can replace cysteine in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
ATP-diphosphate exchange
-
-
?
additional information
?
-
-
selenocysteine can replace cysteine in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
2-aminobutyric acid can replace cysteine in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
ATP-diphosphate exchange
-
-
?
additional information
?
-
-
selenocysteine can replace cysteine in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
2-aminobutyric acid can replace cysteine in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
probable regulation of enzyme activity by processing of polycistronic mRNA
-
?
additional information
?
-
-
probable regulation of enzyme activity by processing of polycistronic mRNA
-
?
additional information
?
-
-
selenocysteine can replace cysteine in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
alanine shows minor activity in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
2-aminobutyric acid can replace cysteine in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
ATP-diphosphate exchange
-
-
?
additional information
?
-
-
Halobacterium sp. contains an unusual peptide that is unique to several halophile archaeal CysRS, which catalyze attachment of cysteine to tRNACys to generate the essential cysteinyl-tRNACys required for protein synthesis, deletion of the peptide reduces the catalytic efficiency of aminoacylation by a factor of 100 that largely results from a defect in kcat, rather than the Km for tRNACys, the acidity of the peptide is not important for the kcat of tRNA aminoacylation
-
-
?
additional information
?
-
-
Halobacterium sp. contains an unusual peptide that is unique to several halophile archaeal CysRS, which catalyze attachment of cysteine to tRNACys to generate the essential cysteinyl-tRNACys required for protein synthesis, deletion of the peptide reduces the catalytic efficiency of aminoacylation by a factor of 100 that largely results from a defect in kcat, rather than the Km for tRNACys, the acidity of the peptide is not important for the kcat of tRNA aminoacylation
-
-
?
additional information
?
-
-
ATP-diphosphate exchange
-
-
?
additional information
?
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
in Methanosarcina mazei Cys-tRNACys is synthesized through a canonical cysteinyl-tRNA synthetase (CysRS) as well as via phosphoseryl-tRNACys synthesized by phosphoseryl-tRNA synthetase and this misacylated intermediate is then converted to Cys-tRNACys by Sep-tRNA:Cys-tRNA synthase via a pyridoxal phosphate-dependent mechanism. The genome of Methanosarcina mazei also features three distinct tRNACys isoacceptors, further indicating the unusual and complex nature of Cys-tRNACys synthesis in this organism
-
-
?
additional information
?
-
-
ATP-diphosphate exchange
-
-
?
additional information
?
-
-
selenocysteine can replace cysteine in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
2-aminobutyric acid can replace cysteine in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
ATP-diphosphate exchange
-
-
?
additional information
?
-
-
ATP-diphosphate exchange
-
-
?
additional information
?
-
-
selenocysteine can replace cysteine in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
selenocysteine can replace cysteine in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
selenocysteine can replace cysteine in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
2-aminobutyric acid can replace cysteine in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
2-aminobutyric acid can replace cysteine in ATP-diphosphate exchange
-
-
?
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2-L-aminobutyric acid
-
-
5'-O-[N-(L-cysteinyl)sulfamoyl] adenosine
-
i.e. Cys-AMS, a cysteinyl adenylate analogue
alpha,beta-CH2-ATP
-
competitive
Ba2+
-
10 mM, 43% inhibition in presence of 10 mM Mg2+, no activation in absence of Mg2+
BTB13069
i.e. 5-methyl-2,4-diphenyl-1,2,3,4,5,6-hexahydrobenzo[b]pyrimido[4,5h][1,6]naphthyridine-1,3,6-trione
Ca2+
-
10 mM, 28% inhibition in presence of 10 mM Mg2+, no activation in absence of Mg2+
CD10929
i.e. 5-[5-(2,4-difluorophenyl)furan-2-yl]-1-(2,4-difluorophenyl)sulfonylpyrazole
CD12049
i.e. N2-phenyl-5-(1,3-dibenzylhexahydropyrimidin-5-yl)-2H-1,2,3,4-tetraazole-2-carbox amide
clofazimine
i.e. N-5-bis(4-chlorophenyl)-3-propan-2-yliminophenazin-2-amine
Co2+
-
10 mM, complete inhibition in presence of 10 mM Mg2+, no activation in absence of Mg2+
Cu2+
-
10 mM, complete inhibition in presence of 10 mM Mg2+, no activation in absence of Mg2+
Cys-AMP
-
inhibits deacylation of Cys-tRNACys
dapsone
i.e. diaphenylsulfone
diphosphate
-
at high concentrations
DSSH00248
i.e. N1,N2-di[1-(2,3-dihydro-1,4-benzodioxin-6-yl)ethyl]phthalamide
Hg2+
-
10 mM, complete inhibition in presence of 10 mM Mg2+, no activation in absence of Mg2+
HTS01959
i.e. N-(2-hydroxy-1,3-dioxo-2,3-dihydro-1H-inden-2-yl)-9-oxo-9H-fluorene-4carboxamide
HTS08262
i.e. [2-(2,3-dihydro-1-benzofuran-5-yl)-1,3-thiazol-4-yl] [4-(9H-fluoren-9-yl)piperazino] methanone
HTS11201
i.e. 7-[(3,4-dichlorophenyl)methyl]-1,3-dimethyl-8-[2-(2-oxoindol-3-yl)hydrazinyl]purine-2,6-dione
HTS11989
i.e. 1-[2-[3-(4-nitrophenyl)-1-phenyl-1H-pyrazol-4-yl]-5-(4-pyridinyl)-1,3,4-oxadiazole-3(2H)-yl]-1-ethanone
HTS12673
i.e. 1-[3-(4-methoxyphenyl)-3,3a,4,5-tetrahydro-2H-benzo[g]indazol-2-yl]-2-{[5-(4-pyridinyl)-1,3,4-oxadiazol-2-yl] sulfanyl}-1-ethanone
KCl
-
the enzyme loses half of its activity at KCl concentrations below 2 M
Mg2+
-
free Mg2+ inhibits
NRB00567
i.e. 1-(9,10-dioxoanthracen-1-yl)sulfanylanthracene-9,10-dione
NRB04869
i.e. 7-(3-nitrophenyl)-6H,7H,8H-chromeno[3',4':5,6]pyrano[3,2-c]chromene-6,8-dione
PD00399
i.e. 2-[[1-benzothiophen-3-ylmethyl-[(1,3-dioxoisoindol-2-yl)methyl]amino]methyl]isoindole-1,3-dione
RF00088
i.e. 2-(5,7-dimethyl-4-oxochromen-3-yl)benzo[g]quinolone-4-carboxylic acid
rifampicin
i.e. (7S,9E,11S,12R,13S,14R,15R,16R,17S,18S,19E,21Z)-2,15,17,27,29-pentahydroxy-11-methoxy-3,7,12,14,16,18,22-heptamethyl-26-[(1E)-[(4-methylpiperazin-1-yl)imino]methyl]-6,23-dioxo-8,30-dioxa-24-azatetracyclo[23.3.1.14,7.05,28]triaconta-1(29),2,4,9,19,21,25,27-octaen-13-yl acetate
RJC02308
i.e. 2-isoquinolin-3-yl-2-(1-nitro-9,10-dioxoanthracen-2-yl)acetonitrile
S-methyl-L-cysteine
-
competitive
Sodium tripolyphosphate
-
-
Sulfhydryl group reagents
-
-
-
Zn2+
-
10 mM, complete inhibition in presence of 10 mM Mg2+, no activation in absence of Mg2+
ADP
-
-
ATP
-
free ATP inhibits
ATP
-
at high concentrations
cysteamine
-
-
cysteine
-
inhibits deacylation of Cys-tRNACys
cysteine
-
at high concentrations
D-cysteine
-
-
D-cysteine
-
weak, non-competitive
EDTA
-
-
glutathione
-
-
iodoacetamide
-
-
iodoacetamide
-
partially
L-homocysteine
-
-
NEM
-
-
O-acetylserine
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
phenylhydrazine
-
weak
S2-
-
-
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0.0125
L-Cys
-
ATP-diphosphate exchange
0.00047 - 3.61
L-cysteine
0.00159 - 0.063
selenocysteine
0.08
tRNA1Cys
-
value above, substrate tRNA1Cys isoacceptor 1
-
0.09
tRNA1CysA33U
-
value above, substrate tRNA1Cys isoacceptor 1, containing a A33U mutation
-
0.16
tRNA2Cys
-
value above, substrate tRNA2Cys isoacceptor 2
-
0.14
tRNA3Cys
-
value above, substrate tRNA3Cys isoacceptor 3
-
0.11
tRNA3CysC20U/U21C/A44U/C46A/A47G
-
value above, substrate tRNA3Cys isoacceptor 3, containing a C20U/U21C/A44U/C46A/A47G mutation
-
0.09
tRNA3CysC20U/U21C/A44U/C46A/A47G/G57A
-
value above, substrate tRNA3Cys isoacceptor 3, containing a C20U/U21C/A44U/C46A/A47G/G57A mutation
-
0.12
tRNA3CysG57A
-
value above, substrate tRNA3Cys isoacceptor 3, containing a G57A mutation
-
0.13
tRNA3CysU33A
-
value above, substrate tRNA3Cys isoacceptor 3, containing a U33A mutation
-
additional information
additional information
-
10
2-aminobutyric acid
-
ATP-diphosphate exchange
10
2-aminobutyric acid
-
ATP-diphosphate exchange
10
2-aminobutyric acid
-
ATP-diphosphate exchange
10
2-aminobutyric acid
-
ATP-diphosphate exchange
10
2-aminobutyric acid
-
ATP-diphosphate exchange
10
2-aminobutyric acid
-
ATP-diphosphate exchange
0.057
ATP
-
ATP-diphosphate exchange, pH 5.12, 37°C
0.083
ATP
-
ATP-diphosphate exchange, 17°C, pH 7.5
0.089
ATP
-
ATP-diphosphate exchange, 19°C, pH 7.5
0.094
ATP
-
ATP-diphosphate exchange, 21°C, pH 7.5
0.095
ATP
-
ATP-diphosphate exchange, pH 5.6, 37°C
0.1
ATP
-
ATP-diphosphate exchange, 23°C, pH 7.5
0.111
ATP
-
ATP-diphosphate exchange, 25°C, pH 7.5
0.147
ATP
-
ATP-diphosphate exchange, pH 6.04, 37°C
0.172
ATP
-
ATP-diphosphate exchange, pH 6.53, 37°C
0.22
ATP
-
ATP-diphosphate exchange reaction, recombinant His-tagged Co2+-wild-type enzyme
0.25
ATP
-
ATP-diphosphate exchange reaction, recombinant His-tagged Zn2+-wild-type enzyme
0.25
ATP
-
pH 8.0, wild-type enzyme, ATP-diphosphate exchange
0.29
ATP
-
ATP-diphosphate exchange reaction, recombinant Zn2+-wild-type enzyme
0.31
ATP
-
pH 8.0, mutant enzyme DELTA288-461, ATP-diphosphate exchange
0.338
ATP
-
30°C, pH 7.0, wild-type enzyme
0.412
ATP
-
30°C, pH 7.0, mutant enzyme V27E
0.77
ATP
-
ATP-diphosphate exchange reaction, recombinant W205Y mutant enzyme
1.15
ATP
-
ATP-diphosphate exchanhge
1.18
ATP
-
pH 8.0, mutant enzyme DELTA328-461, ATP-diphosphate exchange
1.33
ATP
-
ATP-diphosphate exchange
0.03
Cys
-
-
0.045
Cys
-
ATP-diphosphate exchange
0.06
Cys
-
ATP-diphosphate exchange
0.06
Cys
-
ATP-diphosphate exchange
0.062
Cys
-
ATP-diphosphate exchange
0.17
Cys
-
ATP-diphosphate exchange
0.16
diphosphate
-
-
0.3
diphosphate
-
ATP-diphosphate exchange
1
diphosphate
-
ATP-diphosphate exchange
0.00047
L-cysteine
mutant enzyme M294A, pH and temperature not specified in the publication
0.00052
L-cysteine
mutant enzyme E354Q, pH and temperature not specified in the publication
0.00055
L-cysteine
mutant enzyme H297A, pH and temperature not specified in the publication
0.00066
L-cysteine
mutant enzyme M294A/H297A, pH and temperature not specified in the publication
0.0012
L-cysteine
wild type enzyme, pH and temperature not specified in the publication
0.0018
L-cysteine
mutant enzyme R42A, pH and temperature not specified in the publication
0.002
L-cysteine
mutant enzyme H40A, pH and temperature not specified in the publication
0.0072
L-cysteine
-
30°C, pH 7.0, wild-type enzyme
0.0075
L-cysteine
mutant enzyme R427A, pH and temperature not specified in the publication
0.0076
L-cysteine
mutant enzyme M294A/R427A, pH and temperature not specified in the publication
0.0097
L-cysteine
recombinant wild-type enzyme, pH 7.0, 37°C
0.01
L-cysteine
mutant enzyme E354Q/R427A, pH and temperature not specified in the publication
0.0103
L-cysteine
-
recombinant His-tagged deletion mutant, amino acid activation step
0.011
L-cysteine
-
pH 7.5, 25°C
0.0203
L-cysteine
-
recombinant His-tagged wild-type full-length enzyme, amino acid activation step
0.022
L-cysteine
-
ATP-diphosphate exchange reaction, recombinant Zn2+-wild-type enzyme
0.0282
L-cysteine
-
30°C, pH 7.0, mutant enzyme V27E
0.029
L-cysteine
-
ATP-diphosphate exchange reaction, recombinant His-tagged Co2+-wild-type enzyme
0.031
L-cysteine
-
ATP-diphosphate exchange reaction, recombinant His-tagged Zn2+-wild-type enzyme
2.4
L-cysteine
mutant enzyme H40A/R42A, pH and temperature not specified in the publication
3.61
L-cysteine
-
ATP-diphosphate exchange reaction, recombinant W205Y mutant enzyme
0.00159
selenocysteine
-
ATP-diphosphate exchange
0.05
selenocysteine
-
ATP-diphosphate exchange
0.05
selenocysteine
-
ATP-diphosphate exchange
0.05
selenocysteine
-
ATP-diphosphate exchange
0.063
selenocysteine
-
ATP-diphosphate exchange
0.00035
tRNACys
-
aminoacylation reaction, recombinant Zn2+-wild-type enzyme
0.0004
tRNACys
-
aminoacylation reaction, recombinant His-tagged Co2+-wild-type enzyme
0.0005
tRNACys
mutant enzyme E354A, wild-type tRNACys(G15-G48)
0.00058
tRNACys
mutant enzyme E354Q, wild-type tRNACys(G15-G48)
0.00064
tRNACys
-
30°C, pH 7.0, wild-type enzyme
0.0009
tRNACys
-
recombinant His-tagged wild-type full-length enzyme, amino acid activation step
0.00092
tRNACys
-
30°C, pH 7.0, mutant enzyme V27E
0.00116
tRNACys
-
37°C, wild-type enzyme
0.00116
tRNACys
wild-type enzyme, wild-type tRNACys(G15-G48)
0.0012
tRNACys
-
aminoacylation reaction, recombinant His-tagged Zn2+-wild-type enzyme
0.0012
tRNACys
-
pH 7.5, 40°C, recombinant mutant D417A/E420A
0.0013
tRNACys
-
pH 7.5, 40°C, recombinant wild-type enzyme
0.0015
tRNACys
-
pH 7.0, 37°C
0.0017
tRNACys
-
pH 7.5, 40°C, recombinant mutant D239A/D240A
0.0023
tRNACys
-
pH 7.5, 40°C, recombinant mutant D435A/D436A
0.0045
tRNACys
-
recombinant His-tagged deletion mutant, amino acid activation step
0.0066
tRNACys
-
aminoacylation reaction, recombinant W205Y mutant enzyme
0.0088
tRNACys
mutant enzyme N351A, wild-type tRNACys(G15-G48)
0.0177
tRNACys
mutant enzyme N351D, mutant tRNACys(G15-C48)
0.0179
tRNACys
mutant enzyme E354Q, wild-type tRNACys(G15-G48)
0.0185
tRNACys
mutant enzyme N351D, wild-type tRNACys(G15-G48)
0.0332
tRNACys
mutant enzyme N351A, mutant tRNACys(G15-C48)
0.0358
tRNACys
wild-type enzyme, mutant tRNACys(G15-C48)
0.0435
tRNACys
mutant enzyme E354A, mutant tRNACys(G15-C48)
0.08
tRNACys
-
pH 7.5, 25°C
0.095
tRNACys
-
aminoacylation reaction, recombinant C28S/C209S mutant enzyme
additional information
additional information
-
dependence of Km value on pH and temperature
-
additional information
additional information
-
Km for ATP and tRNA is similar in normal and cystinotic cells
-
additional information
additional information
-
Km-values of mutant tRNA molecules
-
additional information
additional information
-
tRNAGln mutant substrates
-
additional information
additional information
-
steady-state, single turnover, and multiple turnover kinetics of recombinant His-tagged wild-type full-length enzyme, and recombinant His-tagged wild-type deletion mutant, kinetic analysis of the two reaction steps, overview
-
additional information
additional information
thermodynamics, single turnover and burst kinetics of CysRS, steady-state and transient kinetic analyses of class I CysRS, the enzyme is rate-limited by release of aminoacyl-tRNA, recombinant His-tagged enzyme, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.017
L-Cysteinyl-tRNACys
-
-
0.17
tRNA1Cys
-
value above, substrate tRNA1Cys isoacceptor 1
-
0.16
tRNA1CysA33U
-
value above, substrate tRNA1Cys isoacceptor 1, containing a A33U mutation
-
0.06
tRNA2Cys
-
value above, substrate tRNA2Cys isoacceptor 2
-
0.03
tRNA3Cys
-
value above, substrate tRNA3Cys isoacceptor 3
-
0.14
tRNA3CysC20U/U21C/A44U/C46A/A47G
-
value above, substrate tRNA3Cys isoacceptor 3, containing a C20U/U21C/A44U/C46A/A47G mutation
-
0.18
tRNA3CysC20U/U21C/A44U/C46A/A47G/G57A
-
value above, substrate tRNA3Cys isoacceptor 3, containing a C20U/U21C/A44U/C46A/A47G/G57A mutation
-
0.09
tRNA3CysG57A
-
value above, substrate tRNA3Cys isoacceptor 3, containing a G57A mutation
-
0.05
tRNA3CysU33A
-
value above, substrate tRNA3Cys isoacceptor 3, containing a U33A mutation
-
additional information
additional information
-
0.3
ATP
-
ATP-diphosphate exchange reaction, recombinant W205Y mutant enzyme
0.34
ATP
-
pH 8.0, mutant enzyme DELTA328-461, ATP-diphosphate exchange
0.48
ATP
-
30°C, pH 7.0, mutant enzyme V27E
2
ATP
-
pH 8.0, mutant enzyme DELTA288-461, ATP-diphosphate exchange
4.4
ATP
-
30°C, pH 7.0, wild-type enzyme
22.6
ATP
-
pH 8.0, wild-type enzyme, ATP-diphosphate exchange
57
ATP
-
ATP-diphosphate exchange reaction, recombinant His-tagged Co2+-wild-type enzyme
91
ATP
-
ATP-diphosphate exchange reaction, recombinant Zn2+-wild-type enzyme
142
ATP
-
ATP-diphosphate exchange reaction, recombinant His-tagged Zn2+-wild-type enzyme
0.001
L-cysteine
mutant enzyme H40A/R42A, pH and temperature not specified in the publication
0.0093
L-cysteine
mutant enzyme H40A, pH and temperature not specified in the publication
0.02
L-cysteine
mutant enzyme M294A/R427A, pH and temperature not specified in the publication
0.027
L-cysteine
mutant enzyme R427A, pH and temperature not specified in the publication
0.082
L-cysteine
mutant enzyme E354Q, pH and temperature not specified in the publication
0.088
L-cysteine
mutant enzyme M294A/H297A, pH and temperature not specified in the publication
0.14
L-cysteine
mutant enzyme M294A, pH and temperature not specified in the publication
0.16
L-cysteine
mutant enzyme H297A, pH and temperature not specified in the publication
0.28
L-cysteine
-
ATP-diphosphate exchange reaction, recombinant W205Y mutant enzyme
0.49
L-cysteine
mutant enzyme E354Q/R427A, pH and temperature not specified in the publication
0.86
L-cysteine
-
30°C, pH 7.0, mutant enzyme V27E
1.1
L-cysteine
mutant enzyme R42A, pH and temperature not specified in the publication
1.2
L-cysteine
wild type enzyme, pH and temperature not specified in the publication
2.2
L-cysteine
recombinant wild-type enzyme, pH 7.0, 37°C
2.5
L-cysteine
steady-state
4.8
L-cysteine
-
30°C, pH 7.0, wild-type enzyme
10.3
L-cysteine
-
recombinant His-tagged wild-type full-length enzyme, amino acid activation step
18.1
L-cysteine
-
recombinant His-tagged deletion mutant, amino acid activation step
35
L-cysteine
-
ATP-diphosphate exchange reaction, recombinant His-tagged Co2+-wild-type enzyme
79
L-cysteine
-
ATP-diphosphate exchange reaction, recombinant Zn2+-wild-type enzyme
100
L-cysteine
-
ATP-diphosphate exchange reaction, recombinant His-tagged Zn2+-wild-type enzyme
0.005
tRNACys
-
aminoacylation reaction, recombinant C28S/C209S mutant enzyme
0.007
tRNACys
-
aminoacylation reaction, recombinant W205Y mutant enzyme
0.014
tRNACys
-
pH 7.5, 40°C, recombinant mutant D417A/E420A
0.03
tRNACys
mutant enzyme N351D, mutant tRNACys(G15-C48)
0.03
tRNACys
-
pH 7.5, 40°C, recombinant mutant D435A/D436A
0.036
tRNACys
mutant enzyme E354A, mutant tRNACys(G15-C48)
0.06
tRNACys
-
pH 7.5, 40°C, recombinant mutant D239A/D240A
0.074
tRNACys
mutant enzyme E354Q, mutant tRNACys(G15-C48)
0.094
tRNACys
mutant enzyme N351D, wild-type tRNACys(G15-G48)
0.1
tRNACys
mutant enzyme E354A, wild-type tRNACys(G15-G48)
0.11
tRNACys
-
pH 7.5, 40°C, recombinant wild-type enzyme
0.14
tRNACys
mutant enzyme E354Q, wild-type tRNACys(G15-G48)
0.2
tRNACys
-
recombinant His-tagged deletion mutant, amino acid activation step
0.39
tRNACys
mutant enzyme N351A, mutant tRNACys(G15-C48)
0.45
tRNACys
wild-type enzyme, mutant tRNACys(G15-C48)
0.5
tRNACys
-
aminoacylation reaction, recombinant His-tagged Co2+-wild-type enzyme
0.59
tRNACys
mutant enzyme N351A, wild-type tRNACys(G15-G48)
0.68
tRNACys
-
30°C, pH 7.0, mutant enzyme V27E
0.9
tRNACys
-
aminoacylation reaction, recombinant Zn2+-wild-type enzyme
2.3
tRNACys
-
recombinant His-tagged wild-type full-length enzyme, amino acid activation step
2.46
tRNACys
-
37°C, wild-type enzyme
2.46
tRNACys
wild-type enzyme, wild-type tRNACys(G15-G48)
2.5
tRNACys
-
aminoacylation reaction, recombinant His-tagged Zn2+-wild-type enzyme
2.9
tRNACys
-
30°C, pH 7.0, wild-type enzyme
3 - 6
tRNACys
-
pH 7.0, 37°C
3.47
tRNACys
-
pH 7.0, 37°C
additional information
additional information
-
turnover numbers of mutant tRNA molecules
-
additional information
additional information
-
tRNAGln mutant substrates
-
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C209S
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.0031% of the wild-type ratio
C28S
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.012% of the wild-type ratio
C36S/C214S/C244S
-
site-directed mutagenesis, activity is similar to the wild-type enzyme, but the affinity for cysteine binding is increased
DELTA288-461
-
the ratio of turnover number to Km-value for ATP in ATP-diphosphate exchange is 7% of the wild-type ratio
DELTA328-461
-
the ratio of turnover number to Km-value for ATP in ATP-diphosphate exchange is 0.32% of the wild-type ratio, aminoacylation of tRNACys is not detectable
E354Q/R427A
the mutant has a decreased kcat and an increased Km leading to an overall decrease in kcat/Km by 22fold relative to the wild type enzyme
H206S
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 60% of the wild-type ratio
H224N/H235N
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.042% of the wild-type ratio
H224S
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 5.7% of the wild-type ratio
H234N/E238Q
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.0059% of the wild-type ratio
H234N/E238Q/H224N/H235N
-
aminoacylation of tRNACys is not detectable
H234S
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.015% of the wild-type ratio
H235S
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.38% of the wild-type ratio
H238S
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 30% of the wild-type ratio
H256S
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 10% of the wild-type ratio
H297A
the mutant has a decreased kcat and Km values leading to an overall decrease in kcat/Km by 3.4fold relative to the wild type enzyme
H404A/R42A
the mutant has a decreased kcat and an increased Km leading to an overall decrease in kcat/Km by 209fold relative to the wild type enzyme
H40A
the mutant has a decreased kcat and an increased Km leading to an overall decrease in kcat/Km by 204fold relative to the wild type enzyme
M294A
the mutant has decreased kcat and Km values leading to an overall decrease in kcat/Km by 3.7fold relative to the wild type enzyme
M294A/H297A
the mutant has a decreased kcat and Km values leading to an overall decrease in kcat/Km by 8.1fold relative to the wild type enzyme
M294A/R427A
the mutant has a decreased kcat and an increased Km leading to an overall decrease in kcat/Km by 370fold relative to the wild type enzyme
N351D
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.25% of the wild-type ratio
R427A
the mutant has a decreased kcat and an increased Km leading to an overall decrease in kcat/Km by 291fold relative to the wild type enzyme
R42A
the mutant has a decreased kcat and an increased Km leading to an overall decrease in kcat/Km by 1.5fold relative to the wild type enzyme
V27E
-
mutation does not affect the discrimination of the enzyme for serine. 4fold increase in Km-value for cysteine and 9fold reduction of turnover number for ATP
W205F
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.55% of the wild-type ratio
W205Y
-
site-directed mutagenesis, highly reduced activity, highly increased Km for cysteine
D239A/D240A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D417A/E420A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D435A/D436A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D239A/D240A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
D417A/E420A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
D435A/D436A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
E217del
the mutation leads to a severe epileptic encephalopathy and complex movement disorder
P251L
the mutation leads to a severe epileptic encephalopathy and complex movement disorder
C28S/C209S
-
site-directed mutagenesis, no ATP-diphosphate exchange activity, residual aminoacylation activity
C28S/C209S
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.0026% of the wild-type ratio
C28S/C209S/H234N/E238Q
-
site-directed mutagensis, mutation of all zinc binding ligands, complete loss of bound zinc, weak ability to bind serine, thus loss of amino acid substrate discrimination ability
C28S/C209S/H234N/E238Q
-
aminoacylation of tRNACys is not detectable
E354Q
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 10% of the wild-type ratio
E354Q
the mutant has decreased kcat and Km values leading to an overall decrease in kcat/Km by 6.8fold relative to the wild type enzyme
additional information
-
construction of a Co2+-substituted wild-type enzyme, similar properties as the Zn2+-wild-type enzyme but slightly reduced activity
additional information
-
construction of a fusion of a eukaryote-specific domain of human CysRS enabling recognition of the sequence differences in the tertiary core of tRNACys. The fused eukaryotic domain redirects the specificity of Escherichia coli CysRS from the A37 present in bacterial tRNACys to the G37 in mammals
additional information
-
deletion of the halophilic-specific peptide reduces the catalytic efficiency of aminoacylation by a factor of 100 that largely results from a defect in kcat, rather than the Km for tRNACys, maintaining the peptide length but substituting acidic residues in the peptide with neutral or basic residues has no major deleterious effect, suggesting that the acidity of the peptide is not important for the kcat of tRNA aminoacylation, construction of point mutants and deletion mutants, e.g. deletion mutant DELTA193-212, overview
additional information
-
deletion of the halophilic-specific peptide reduces the catalytic efficiency of aminoacylation by a factor of 100 that largely results from a defect in kcat, rather than the Km for tRNACys, maintaining the peptide length but substituting acidic residues in the peptide with neutral or basic residues has no major deleterious effect, suggesting that the acidity of the peptide is not important for the kcat of tRNA aminoacylation, construction of point mutants and deletion mutants, e.g. deletion mutant DELTA193-212, overview
-
additional information
-
construction of a DELTAC mutant of the enzyme that terminates at V642, removing residues 643 to 748 from the full-length enzyme, the mutant enzymes shows increased activity in the first amino acid activation step and reduced activity in the second aminoacylation step compared to the wild-type full-length enzyme
additional information
construction of a cysS gene disruption knockout mutant, which is viable under normal growth conditions
additional information
-
construction of a cysS gene disruption knockout mutant, which is viable under normal growth conditions
additional information
-
generation of conditional expression strains, conditional expression plasmids are electroporated into Mycobacterium smegmatis strain mc2155, analysis of inducer dependency of conditional expression strains, overview
additional information
generation of conditional expression strains, conditional expression plasmids are electroporated into Mycobacterium smegmatis strain mc2155, analysis of inducer dependency of conditional expression strains, overview
additional information
-
generation of conditional expression strains, conditional expression plasmids are electroporated into Mycobacterium smegmatis strain mc2155, analysis of inducer dependency of conditional expression strains, overview
-
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Burnell, J.N.; Whatley, F.R.
Sulphur metabolism in Paracoccus denitrificans. Purification, properties and regulation of cysteinyl- and methionyl-tRNA synthetase
Biochim. Biophys. Acta
481
266-278
1977
Paracoccus denitrificans
brenda
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
Eriani, G.; Dirheimer, G.; Gangloff, J.
Cysteinyl-tRNA synthetase: determination of the last E. coli aminoacyl-tRNA synthetase primary structure
Nucleic Acids Res.
19
265-269
1991
Escherichia coli
brenda
Cruzen, M.E.; Arfin, S.M.
Nucleotide and deduced amino acid sequence of human cysteinyl-tRNA synthetase
DNA Seq.
4
243-248
1994
Homo sapiens
brenda
Jakubowski, H.
Editing function of Escherichia coli cysteinyl-tRNA synthetase: cyclization of cysteine to cysteine thiolactone
Nucleic Acids Res.
22
1155-1160
1994
Escherichia coli
brenda
Komatsoulis, G.A.; Abelson, J.
Recognition of tRNACys by Escherichia coli cysteinyl-tRNA synthetase [published erratum appears in Biochemistry 1993 Dec 7;32(48):13374]
Biochemistry
32
7435-7444
1993
Escherichia coli
brenda
Chang, G.G.; Pan, F.; Deng, P.N.; Wu, B.Y.
Kinetic studies on human cysteinyl-tRNA synthetase
Int. J. Pept. Protein Res.
13
267-273
1979
Homo sapiens
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