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ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
?
AMP + diphosphate + L-arginyl-tRNALys
ATP + L-arginine + tRNALys
-
-
-
-
r
AMP + diphosphate + L-lysyl-tRNALys
ATP + L-lysine + tRNALys
-
-
-
-
r
AMP + diphosphate + L-methionyl-tRNALys
ATP + L-methionine + tRNALys
-
-
-
-
r
AMP + L-threonyl-tRNALys + diphosphate
ATP + L-threonine + tRNALys
-
-
-
-
r
ATP + 4-aminobutanoate + tRNALys
AMP + 4-aminobutyryl-tRNALys + diphosphate
-
-
-
?
ATP + ATP
diadenosine 5',5''-P1,P3-triphosphate + ?
-
-
-
-
?
ATP + ATP
diadenosine 5',5''-P1,P4-tetraphosphate + diphosphate
-
-
-
-
?
ATP + D-lysine + tRNALys
AMP + D-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + L-alanine + tRNALys
AMP + L-alanyl-tRNALys + diphosphate
-
264000fold lower activity than with L-lysine, deacylation of the mischarged tRNALys, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + L-arginine + tRNALys
AMP + L-arginyl-tRNALys + diphosphate
ATP + L-cysteine + tRNALys
AMP + L-cysteinyl-tRNALys + diphosphate
-
750000fold lower activity than with L-lysine, deacylation of the mischarged tRNALys, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + L-glutamate + tRNALys
AMP + L-glutamyl-tRNALys + diphosphate
-
low activity
-
?
ATP + L-leucine + tRNALys
AMP + L-leucyl-tRNALys + diphosphate
-
132000fold lower activity than with L-lysine, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + L-lysinamide + tRNALys
AMP + L-aminolysyl-tRNALys + diphosphate
-
low activity
-
?
ATP + L-lysine
?
-
a small fraction of lysine is converted to lysine lactam in absence or presence of tRNALys
-
?
ATP + L-lysine + Borellia burgdorferi tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
ATP + L-lysine + Escherichia coli G2.U71 tRNA
?
-
-
-
-
?
ATP + L-lysine + Escherichia coli G2.U71 tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
r
ATP + L-lysine + Escherichia coli wild type tRNA
?
-
-
-
-
?
ATP + L-lysine + Escherichia coli wild type tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
r
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
ATP + L-lysine + tRNALysCUU
AMP + L-lysyl-tRNALysCUU + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNALysUUU
AMP + L-lysyl-tRNALysUUU + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNATyrCUA
AMP + L-lysyl-tRNATyrCUA + diphosphate
-
has a weak activity to tRNATyrCUA with L-lysine
-
-
?
ATP + L-lysine ethyl ester + tRNALys
AMP + ethyl-L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + L-lysine hydroxamate + tRNALys
AMP + L-lysine hydroxamoyl-tRNALys + diphosphate
-
-
-
?
ATP + L-lysine methyl ester + tRNALys
AMP + methyl-L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + L-methionine + tRNALys
AMP + L-methionyl-tRNALys + diphosphate
-
32000fold lower activity than with L-lysine, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + L-ornithine
?
-
L-ornithine is converted to ornithine lactam in absence or presence of tRNALys
-
?
ATP + L-serine + tRNALys
AMP + L-seryl-tRNALys + diphosphate
-
562000fold lower activity than with L-lysine, deacylation of the mischarged tRNALys, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + L-threonine + tRNALys
AMP + L-threonyl-tRNALys + diphosphate
-
16000fold lower activity than with L-lysine, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
ATP + ornithine + tRNALys
AMP + ornithyl-tRNALys + diphosphate
-
-
-
?
additional information
?
-
ATP + L-arginine + tRNALys
AMP + L-arginyl-tRNALys + diphosphate
-
low activity
-
?
ATP + L-arginine + tRNALys
AMP + L-arginyl-tRNALys + diphosphate
-
best noncognate amino acid substrate, 1600fold lower activity than with L-lysine, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
r
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
2-step reaction, the first step comprises the activation of the amino acid to form an enzyme-bound aminoacyl adenylate, the second step involves binding of this complex by tRNA, whose 3'-end is esterified with the aminoacyl-moiety followed by release of the resulting aminoacyl-tRNA, aminoacylation can be performed in absence of the tRNA
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
cognate amino acid, best substrate, two-step reaction mechanism, limited selectivity in the aminoacylation reaction due to inefficient editing of some amino acids, e.g. Met, Leu, Cys, Ala, Thr, by pre-transfer mechanism or the absence of post-transfer editing of other amino acids e.g. Arg, Ser, a small fraction of lysine is converted to lysine lactam
-
r
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
tRNA substrate from Borrelia burgdorferi or Escherichia coli, predicted secondary structure of tRNAlys from Escherichia coli
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
the enzymes major function is to provide Lys-tRNALys fpr protein biosynthesis
-
r
additional information
?
-
-
lysine-dependent ATP-diphosphate exchange reaction: lysine + ATP + enzyme/lysine-AMP-enzyme + diphosphate
-
-
?
additional information
?
-
-
synthesis of mixed dinucleoside 5',5'''-P1,P4-triphosphates or 5',5''''-P1,P4-tetraphosphates resulting from the reaction of lysyl adenylate with a variety of ribonucleotide 5'-triphosphates, ribonucleotide 5'-diphosphates, deoxyribonucleotide 5'-diphosphates or deoxyribonucleotide 5'-triphosphates
-
-
?
additional information
?
-
-
L-lysine-dependent synthesis of 5',5'-diadenosine tetraphosphate (Ap4A)
-
-
?
additional information
?
-
-
substrate recognition specificity, the enzyme also performs the ATP-diphosphate exchange reaction, class II lysine-tRNA synthetases recognize the same elements in tRNALys as their class I counterparts, namely the discriminator base N73 and the anticodon, but vary in the recognition of the G2.U71 wobble pair of spirochete tRNALys, which acts as a determinant for class II enzymes, but not for class I enzymes
-
?
additional information
?
-
-
the enzyme possesses an efficient pre-transfer editing mechanism which prevents misacylation of tRNALys with ornithine, which results in cyclization to ornithine lactam
-
?
additional information
?
-
-
the enzyme also converts ATP to diadenosine tri- and tetraphosphates in the presence of L-lysine/Mg2+/Zn2+
-
-
?
additional information
?
-
LysU-based preparation of potentially important ApnA analogues, overview. Dimeric LysU has dual diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) and diadenosine-5',5'''-P1,P3-triphosphate (Ap3A) synthase activities. Syntheses of both take place through the formation of a lysyl-adenylate 1 intermediate from ATP and L-lysine. Thereafter, the terminal phosphate of a second nucleotide substrate combines with the enzyme-bound lysyl-adenylate, thereby liberating free L-lysine and generating either Ap4A or Ap3A depending upon the identity of the second nucleotide substrate. The first step involving lysyladenylate intermediate formation is highly specific but reversible. Therefore inorganic diphosphatase-mediated controlled hydrolysis of diphosphate is required in order to prevent the back-reaction taking place, and thereby essentially rendering this first step committed. Fortunately, the second product formation step is highly promiscuous and a wide variety of nucleotide di-, tri-, and tetraphosphates are acceptable as second nucleotide substrates. This promiscuity also extends to inorganic phosphate and to tripolyphosphate. Surface mechanism of LysU catalyzed Ap4A and Ap3A synthase activities, reaction scheme and mechanism, overview. Bulkier putative diphosphate analogue substrates preclude molecular recognition and binding by LysU, hence preventing their use as bona fide LysU substrates able to couple to the ATP derived lysyl adenylate 1 intermediate with LysU assistance. Synthesis of analogues beta,gamma-methylene-P1,P4-bis(5'-adenosyl) tetraphosphate, beta,gamma-imido-P1,P4-bis(5'-adenosyl) tetraphosphate, (open-ring-ribosyl)2-beta,gamma-methylene-P1,P4-bis(5'-adenosyl) tetraphosphate, (open-ring-ribosyl)2-beta,gamma-imido-P1,P4-bis(5'-adenosyl) tetraphosphate, (open-ring-ribosyl)-beta,gamma-methylene-P1,P4-bis(5'-adenosyl) tetraphosphate, (open-ring-ribosyl)-beta,gamma-imido-P1,P4-bis(5'-adenosyl) tetraphosphate, alpha,beta-methylene 5'-P1,P3-bis(5'-adenosyl) triphosphate, alpha,beta-methylene-guanosine 5'-P1-triphospho-P3-5''-adenosine, beta,gamma-methylene-P1,P5-bis(5'-adenosyl) pentaphosphate, beta,gamma-imido-adenosine 5'-P1-pentaphospho-P5-5''-uridine, beta,gamma-methylene-adenosine 5'-P1-tretraphospho-P4-5''-guanosine, beta,gamma-imido-adenosine 5'-P1-tretraphospho-P4-5''-guanosine, and beta,gamma-delta,epsilon-dimethylene-P1,P6-bis(5'-adenosyl) hexaphosphate
-
-
?
additional information
?
-
-
LysU-based preparation of potentially important ApnA analogues, overview. Dimeric LysU has dual diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) and diadenosine-5',5'''-P1,P3-triphosphate (Ap3A) synthase activities. Syntheses of both take place through the formation of a lysyl-adenylate 1 intermediate from ATP and L-lysine. Thereafter, the terminal phosphate of a second nucleotide substrate combines with the enzyme-bound lysyl-adenylate, thereby liberating free L-lysine and generating either Ap4A or Ap3A depending upon the identity of the second nucleotide substrate. The first step involving lysyladenylate intermediate formation is highly specific but reversible. Therefore inorganic diphosphatase-mediated controlled hydrolysis of diphosphate is required in order to prevent the back-reaction taking place, and thereby essentially rendering this first step committed. Fortunately, the second product formation step is highly promiscuous and a wide variety of nucleotide di-, tri-, and tetraphosphates are acceptable as second nucleotide substrates. This promiscuity also extends to inorganic phosphate and to tripolyphosphate. Surface mechanism of LysU catalyzed Ap4A and Ap3A synthase activities, reaction scheme and mechanism, overview. Bulkier putative diphosphate analogue substrates preclude molecular recognition and binding by LysU, hence preventing their use as bona fide LysU substrates able to couple to the ATP derived lysyl adenylate 1 intermediate with LysU assistance. Synthesis of analogues beta,gamma-methylene-P1,P4-bis(5'-adenosyl) tetraphosphate, beta,gamma-imido-P1,P4-bis(5'-adenosyl) tetraphosphate, (open-ring-ribosyl)2-beta,gamma-methylene-P1,P4-bis(5'-adenosyl) tetraphosphate, (open-ring-ribosyl)2-beta,gamma-imido-P1,P4-bis(5'-adenosyl) tetraphosphate, (open-ring-ribosyl)-beta,gamma-methylene-P1,P4-bis(5'-adenosyl) tetraphosphate, (open-ring-ribosyl)-beta,gamma-imido-P1,P4-bis(5'-adenosyl) tetraphosphate, alpha,beta-methylene 5'-P1,P3-bis(5'-adenosyl) triphosphate, alpha,beta-methylene-guanosine 5'-P1-triphospho-P3-5''-adenosine, beta,gamma-methylene-P1,P5-bis(5'-adenosyl) pentaphosphate, beta,gamma-imido-adenosine 5'-P1-pentaphospho-P5-5''-uridine, beta,gamma-methylene-adenosine 5'-P1-tretraphospho-P4-5''-guanosine, beta,gamma-imido-adenosine 5'-P1-tretraphospho-P4-5''-guanosine, and beta,gamma-delta,epsilon-dimethylene-P1,P6-bis(5'-adenosyl) hexaphosphate
-
-
?
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0.0043
Borellia burgdorferi tRNALys
-
recombinant enzyme, pH 7.2, 37°C
-
0.0063
Escherichia coli G2.U71 tRNA
-
recombinant enzyme, pH 7.2, 37°C
-
0.0019
Escherichia coli wild type tRNA
-
recombinant enzyme, pH 7.2, 37°C
-
0.004
Lys
-
aminoacylation
0.0078
ATP
-
pH 7.2, 37°C, mutant enzyme E278Q
0.0078
ATP
-
pH 7.2, 37°C, mutant enzyme E428Q
0.011
ATP
-
pH 7.2, 37°C, mutant enzyme E240D
0.012
ATP
-
pH 7.2, 37°C, wild-type enzyme
0.014
ATP
-
pH 7.2, 37°C, mutant enzyme E240Q
0.016
ATP
-
pH 7.2, 37°C, mutant enzyme E278D
0.019
ATP
-
pH 7.2, 37°C, mutant enzyme F426H
0.02
ATP
-
pH 7.2, 37°C, mutant enzyme E428D
0.021
ATP
-
pH 7.2, 37°C, mutant enzyme N424D
0.037
ATP
-
aminoacylation, enzyme form EII
0.062
ATP
-
pH 7.2, 37°C, mutant enzyme Y280F
0.11
ATP
-
pH 7.2, 37°C, mutant enzyme F426W
0.147
ATP
-
pH 7.2, 37°C, mutant enzyme Y280S
0.195
ATP
-
pH 7.2, 37°C, mutant enzyme G216A
0.33
ATP
-
aminoacylation, enzyme form EI
0.83
ATP
-
pH 7.2, 37°C, mutant enzyme N424Q
0.0025
L-Lys
-
-
0.005
L-Lys
-
aminoacylation, enzyme form EII
0.006
L-Lys
-
aminoacylation, enzyme form EI
0.0013
L-lysine
-
pH 7.2, 37°C, mutant enzyme E428Q
0.0014
L-lysine
-
pH 7.2, 37°C, mutant enzyme E278Q
0.0026
L-lysine
-
pH 7.2, 37°C, wild-type enzyme
0.0033
L-lysine
-
pH 7.2, 37°C, mutant enzyme E240D
0.0036
L-lysine
-
pH 7.2, 37°C, mutant enzyme E240Q
0.0052
L-lysine
-
pH 7.2, 37°C, mutant enzyme N424D
0.016
L-lysine
-
pH 7.2, 37°C, mutant enzyme F426W
0.022
L-lysine
-
pH 7.2, 37°C, mutant enzyme E428D
0.024
L-lysine
-
pH 7.2, 37°C, mutant enzyme Y280F
0.052
L-lysine
-
pH 7.2, 37°C, mutant enzyme N424Q
0.114
L-lysine
-
pH 7.2, 37°C, mutant enzyme Y280S
0.196
L-lysine
-
pH 7.2, 37°C, mutant enzyme G216A
0.203
L-lysine
-
pH 7.2, 37°C, mutant enzyme F426H
0.254
L-lysine
-
pH 7.2, 37°C, mutant enzyme E278D
0.002
tRNALys
-
aminoacylation, enzyme form EI
0.0057
tRNALys
-
aminoacylation, enzyme form EII
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0035
Borellia burgdorferi tRNALys
-
recombinant enzyme, pH 7.2, 37°C
-
0.0025
Escherichia coli G2.U71 tRNA
-
recombinant enzyme, pH 7.2, 37°C
-
0.055
Escherichia coli wild type tRNALys
-
recombinant enzyme, pH 7.2, 37°C
-
0.00067
L-arginyl-tRNALys
-
deacylation reaction, pH 7.4, 37°C, in absence or presence of 50 mM DTT
0.00023 - 0.0088
L-lysyl-tRNALys
0.00056
L-methionyl-tRNALys
-
deacylation reaction, pH 7.4, 37°C, in absence or presence of 50 mM DTT
-
0.00076
L-threonyl-tRNALys
-
deacylation reaction, pH 7.4, 37°C, in absence or presence of 50 mM DTT
-
0.013
ATP
-
pH 7.2, 37°C, mutant enzyme E240Q
0.017
ATP
-
pH 7.2, 37°C, mutant enzyme E278Q
0.017
ATP
-
pH 7.2, 37°C, mutant enzyme E428Q
0.054
ATP
-
pH 7.2, 37°C, mutant enzyme E278D
0.14
ATP
-
pH 7.2, 37°C, mutant enzyme E240D
0.17
ATP
-
pH 7.2, 37°C, mutant enzyme Y280F
0.35
ATP
-
pH 7.2, 37°C, mutant enzyme Y280S
0.67
ATP
-
pH 7.2, 37°C, mutant enzyme F426H
0.8
ATP
-
pH 7.2, 37°C, mutant enzyme G216A
1
ATP
-
pH 7.2, 37°C, mutant enzyme E428D
1
ATP
-
pH 7.2, 37°C, mutant enzyme N424D
2.2
ATP
-
pH 7.2, 37°C, mutant enzyme N424Q
2.4
ATP
-
pH 7.2, 37°C, mutant enzyme F426W
3.4
ATP
-
pH 7.2, 37°C, wild-type enzyme
0.00065
L-lysine
-
L-lysine lactam formation, pH 7.4, 37°C
0.0087
L-lysine
-
pH 7.2, 37°C, mutant enzyme E240Q
0.015
L-lysine
-
pH 7.2, 37°C, mutant enzyme E278Q
0.02
L-lysine
-
pH 7.2, 37°C, mutant enzyme E428D
0.031
L-lysine
-
pH 7.2, 37°C, mutant enzyme Y280F
0.086
L-lysine
-
pH 7.2, 37°C, mutant enzyme E240D
0.16
L-lysine
-
pH 7.2, 37°C, mutant enzyme E278D
0.6
L-lysine
-
pH 7.2, 37°C, mutant enzyme F426W
0.65
L-lysine
-
pH 7.2, 37°C, mutant enzyme N424Q
1
L-lysine
-
pH 7.2, 37°C, mutant enzyme E428D
1.6
L-lysine
-
pH 7.2, 37°C, mutant enzyme N424D
1.6
L-lysine
-
pH 7.2, 37°C, mutant enzyme Y280S
1.8
L-lysine
-
pH 7.2, 37°C, wild-type enzyme
2.4
L-lysine
-
pH 7.2, 37°C, mutant enzyme F426H
3.4
L-lysine
-
pH 7.2, 37°C, mutant enzyme G216A
0.00023
L-lysyl-tRNALys
-
deacylation reaction, pH 7.4, 37°C, in absence of DTT
0.0088
L-lysyl-tRNALys
-
deacylation reaction, pH 7.4, 37°C, in presence of 50 mM DTT
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00001 - 0.0013
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
12
D-Lysine
-
pH 7.2, 37°C
0.0015 - 1.31
S-(2-aminoethyl)-L-cysteine
0.00001
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
-
pH 7.2, 37°C, mutant enzyme E240Q
0.000011
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
-
pH 7.2, 37°C, mutant enzyme E428Q
0.000023
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
-
pH 7.2, 37°C, mutant enzyme E278Q
0.000028
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
-
pH 7.2, 37°C, wild-type enzyme
0.000029
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
-
pH 7.2, 37°C, mutant enzyme E240D
0.000039
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
-
pH 7.2, 37°C, mutant enzyme N424D
0.000041
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
-
pH 7.2, 37°C, mutant enzyme E278D
0.00005
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
-
pH 7.2, 37°C, mutant enzyme F426W
0.000055
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
-
pH 7.2, 37°C, mutant enzyme N424Q
0.000059
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
-
pH 7.2, 37°C, mutant enzyme G216A
0.000061
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
-
pH 7.2, 37°C, mutant enzyme E428D
0.00022
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
-
pH 7.2, 37°C, mutant enzyme Y280S
0.00027
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
-
pH 7.2, 37°C, mutant enzyme Y280F
0.0013
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
-
pH 7.2, 37°C, mutant enzyme F426H
0.0015
S-(2-aminoethyl)-L-cysteine
-
pH 7.2, 37°C, mutant enzyme E428Q
0.0031
S-(2-aminoethyl)-L-cysteine
-
pH 7.2, 37°C, mutant enzyme E240D
0.0039
S-(2-aminoethyl)-L-cysteine
-
pH 7.2, 37°C, wild-type enzyme
0.004
S-(2-aminoethyl)-L-cysteine
-
pH 7.2, 37°C, mutant enzyme N424D
0.005
S-(2-aminoethyl)-L-cysteine
-
pH 7.2, 37°C, mutant enzyme E278Q
0.0054
S-(2-aminoethyl)-L-cysteine
-
pH 7.2, 37°C, mutant enzyme E240Q
0.025
S-(2-aminoethyl)-L-cysteine
-
pH 7.2, 37°C, mutant enzyme F426W
0.034
S-(2-aminoethyl)-L-cysteine
-
pH 7.2, 37°C, mutant enzyme E428D
0.072
S-(2-aminoethyl)-L-cysteine
-
pH 7.2, 37°C, mutant enzyme Y280F
0.076
S-(2-aminoethyl)-L-cysteine
-
pH 7.2, 37°C, mutant enzyme N424Q
0.34
S-(2-aminoethyl)-L-cysteine
-
pH 7.2, 37°C, mutant enzyme Y280S
1.24
S-(2-aminoethyl)-L-cysteine
-
pH 7.2, 37°C, mutant enzyme G216A
1.29
S-(2-aminoethyl)-L-cysteine
-
pH 7.2, 37°C, mutant enzyme E278D
1.31
S-(2-aminoethyl)-L-cysteine
-
pH 7.2, 37°C, mutant enzyme F426H
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E240D
-
1.2fold increase in Km-value for Lys, 21fold decrease in turnover number for Lys, Km-value for ATP is nearly identical to wild-type value, 24fold decrease in turnover number for ATP
E240Q
-
1.4fold increase in Km-value for Lys, 207fold decrease in turnover number for Lys, 1.2fold increase in Km-value for ATP, 261fold decrease in turnover number for ATP
E246D
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
E246R
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
E264A
-
the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme
E264K
-
the mutant catalyses the production of glycerol-3-phosphate, powered by ATP turnover to ADP but shows little formation of diadenosine tri- and tetraphosphates under normal conditions (additional Zn2+/L-lysine/Mg2+)
E264N
-
the mutant catalyses the production of glycerol-3-phosphate, powered by ATP turnover to ADP but shows little formation of diadenosine tri- and tetraphosphates under normal conditions (additional Zn2+/L-lysine/Mg2+)
E264Q
-
the mutant catalyses the production of glycerol-3-phosphate, powered by ATP turnover to ADP but shows little formation of diadenosine tri- and tetraphosphates under normal conditions (additional Zn2+/L-lysine/Mg2+)
E273A
-
the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme
E278D
-
98fold increase in Km-value for Lys, 11fold decrease in turnover number for Lys, 1.3fold increase in Km-value for ATP, 63fold decrease in turnover number for ATP
E278Q
-
1.9fold decrease in Km-value for Lys, 120fold decrease in turnover number for Lys, 1.5fold decrease in Km-value for ATP, 200fold decrease in turnover number for ATP
E414A
-
the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme
E421A
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
E428D
-
8.5fold increase in Km-value for Lys, 1.8fold decrease in turnover number for Lys, 1.7fold increase in Km-value for ATP, 3.4fold decrease in turnover number for ATP
E428Q
-
2fold decrease in Km-value for Lys, 9fold decrease in turnover number for Lys, 1.5fold decrease in Km-value for ATP, 200fold decrease in turnover number for ATP
F261A
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
F274A
-
the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme
F426H
-
78fold increase in Km-value for Lys, 1.3fold decrease in turnover number for Lys, 1.6fold increase in Km-value for ATP, 5fold decrease in turnover number for ATP
F426W
-
6.2fold increase in Km-value for Lys, 3fold decrease in turnover number for Lys, 9.2fold increase in Km-value for ATP, 1.4fold decrease in turnover number for ATP
G216A
-
75fold increase in Km-value for Lys, 1.9fold increase in turnover number for Lys, 16fold increase in Km-value for ATP, 4.25fold decrease in turnover number for ATP
G265A
-
the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme
H270A
-
the mutant catalyses the production of glycerol-3-phosphate, powered by ATP turnover to ADP but shows little formation of diadenosine tri- and tetraphosphates under normal conditions (additional Zn2+/L-lysine/Mg2+)
I266A
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
N424D
-
2fold increase in Km-value for Lys, 1.1fold decrease in turnover number for Lys, 1.8fold increase in Km-value for ATP, 3.4fold decrease in turnover number for ATP
N424Q
-
20fold increase in Km-value for Lys, 2.8fold decrease in turnover number for Lys, 69fold increase in Km-value for ATP, 1.5fold decrease in turnover number for ATP
P272A
-
the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme
R480A
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
S267A
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
Y280F
-
9.2fold increase in Km-value for Lys, 58fold decrease in turnover number for Lys, 5.2fold increase in Km-value for ATP, 20fold decrease in turnover number for ATP
Y280S
-
44fold increase in Km-value for Lys, 1.1fold decrease in turnover number for Lys, 3.9fold increase in Km-value for ATP, 9.7fold decrease in turnover number for ATP
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Airas, R.K.
Differences in the magnesium dependences of the class I and class II aminoacyl-tRNA synthetases from Escherichia coli
Eur. J. Biochem.
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223-231
1996
Escherichia coli
brenda
Onesti, S.; Miller, A.D.; Brick, P.
The crystal structure of the lysyl-tRNA synthetase from Escherichia coli
Structure
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163-176
1995
Escherichia coli
brenda
Hele, P.; Barber, R.
Lysyl tRNA synthetase of Escherichia coli. Formation and reactions of ATP-enzyme and lysyl-AMP-enzyme complexes
Biochim. Biophys. Acta
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1972
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Kisselev, L.L.; Baturina, I.D.
Two enzymatically active forms of lysyl-tRNA synthetase from E. coli B
FEBS Lett.
22
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1972
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Baturina, I.D.; Gnutchev, N.V.; Khomutov, R.M.; Kisselev, L.L.
Substrate specificity of lysyl-tRNA synthetase from E. coli B
FEBS Lett.
22
235-237
1972
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Dittgen, R.M.; Leberman, R.
Multiple forms of lysyl-tRNA synthetase from Escherichia coli
Hoppe-Seyler's Z. Physiol. Chem.
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1976
Escherichia coli, Escherichia coli MRE 600
brenda
Plateau, P.; Blanquet, S.
Zinc-dependent synthesis of various dinucleoside 5', 5'''-P1, P3-tri or 5', 5'''-P1,P4-tetraphosphates by Escherichia coli lysyl-tRNA synthetase
Biochemistry
21
5273-5279
1982
Escherichia coli
brenda
Jakubowski, H.
Misacylation of tRNALys with noncognate amino acids by lysyl-tRNA synthetase
Biochemistry
38
8088-8093
1999
Escherichia coli
brenda
Onesti, S.; Desogus, G.; Brevet, A.; Chen, J.; Plateau, P.; Blanquet, S.; Brick, P.
Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding
Biochemistry
39
12853-12861
2000
Escherichia coli (P0A8N3), Escherichia coli
brenda
Levengood, J.D.; Ataide, S.F.; Roy, H.; Ibba, M.
Divergence in non-cognate amino acid recognition between class I and class II lysyl-tRNA synthetases
J. Biol. Chem.
279
17707-17714
2004
Borreliella burgdorferi, Escherichia coli
brenda
Ibba, M.; Losey, H.C.; Kawarabayasi, Y.; Kikuchi, H.; Bunjun, S.; Soll, D.
Substrate recognition by class I lysyl-tRNA synthetases: a molecular basis for gene displacement
Proc. Natl. Acad. Sci. USA
96
418-423
1999
Aeropyrum pernix (Q9YFT9), Borreliella burgdorferi, Escherichia coli, Methanococcus maripaludis
brenda
Ataide, S.F.; Ibba, M.
Discrimination of cognate and noncognate substrates at the active site of class II lysyl-tRNA synthetase
Biochemistry
43
11836-11841
2004
Escherichia coli
brenda
Wright, M.; Boonyalai, N.; Tanner, J.A.; Hindley, A.D.; Miller, A.D.
The duality of LysU, a catalyst for both Ap4A and Ap3A formation
FEBS J.
273
3534-3544
2006
Escherichia coli
brenda
Fukunaga, J.; Yokogawa, T.; Ohno, S.; Nishikawa, K.
Misacylation of yeast amber suppressor tRNA(Tyr) by E. coli lysyl-tRNA synthetase and its effective repression by genetic engineering of the tRNA sequence
J. Biochem.
139
689-696
2006
Escherichia coli
brenda
Chou, T.F.; Wagner, C.R.
Lysyl-tRNA synthetase-generated lysyl-adenylate is a substrate for histidine triad nucleotide binding proteins
J. Biol. Chem.
282
4719-4727
2007
Escherichia coli, Homo sapiens
brenda
Fukunaga, J.; Ohno, S.; Nishikawa, K.; Yokogawa, T.
A base pair at the bottom of the anticodon stem is reciprocally preferred for discrimination of cognate tRNAs by Escherichia coli lysyl- and glutaminyl-tRNA synthetases
Nucleic Acids Res.
34
3181-3188
2006
Escherichia coli
brenda
Chen, X.; Boonyalai, N.; Lau, C.; Thipayang, S.; Xu, Y.; Wright, M.; Miller, A.D.
Multiple catalytic activities of Escherichia coli lysyl-tRNA synthetase (LysU) are dissected by site-directed mutagenesis
FEBS J.
280
102-114
2013
Escherichia coli
brenda
Wright, M.; Azhar, M.A.; Kamal, A.; Miller, A.D.
Syntheses of stable, synthetic diadenosine polyphosphate analogues using recombinant histidine-tagged lysyl tRNA synthetase (LysU)
Bioorg. Med. Chem. Lett.
24
2346-2352
2014
Escherichia coli (P0A8N5), Escherichia coli
brenda