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L-lysine + O2 = ? + H2O2
-
L-lysine + electron acceptor = ?
-
L-lysine + O2 + H2O = 6-amino-2-oxohexanoate + NH3 + H2O2
-
L-lysine + O2 = 2-keto-6-amino-n-hexanoate + NH3 + H2O2
-
L-lysine + O2 = 5-aminopentanamide + CO2 + H2O
744567, 745703, 745704, 746458, 742530, 763035, 745567, 746434, 390102, 440264, 440265, 440266, 440270, 440274, 440276, 440278, 765065
-
L-lysine + O2 = 5-aminovaleramide + CO2 + H2O
-
L-lysine + phenazine methosulfate = 2-keto-6-amino-n-hexanoate + NH3 + reduced phenazine methosulfate
-
L-lysine + NADPH + H+ + O2 = L-lysine N6-oxide + NADP+ + H2O
-
L-lysine + NADPH + H+ + O2 = N6-hydroxy-L-lysine + NADP+ + H2O
-
L-Lys + NADPH + O2 = N6-Hydroxy-L-Lys + NADP+ + H2O
-
L-lysine + iodine + O2 = N6-hydroxy-L-lysine + iodate + H2O
-
L-lysine + NADH + H+ + O2 = N6-hydroxy-L-lysine + NAD+ + H2O
-
L-lysine + NADPH + H+ + O2 = N6-hydroxy-L-lysine + NADP+ + H2O
-
L-lysine + NADPH + O2 = N6-hydroxy-L-lysine + NADP+ + H2O
-
L-lysine + NAD+ + H2O = 1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
L-lysine + NAD+ = 1,2-didehydropiperidine-2-carboxylate + NH3 + NADH
-
L-lysine + NAD+ = 1,2-didehydropiperidine-2-carboxylate + NH3 + NADH + H+
-
L-lysine + 3-acetylpyridine-NAD+ + H2O = alpha-aminoadipate delta-semialdehyde + NH3 + 3-acetylpyridine-NADH
-
L-lysine + deamino-NAD+ + H2O = alpha-aminoadipate delta-semialdehyde + NH3 + deamino-NADH
-
L-lysine + NAD(P)+ + H2O = (S)-2-aminoadipate 6-semialdehyde + NAD(P)H + H+ + NH3
-
L-lysine + NAD+ + H2O = (S)-2-amino-6-oxohexanoate + NADH + H+ + NH3
-
L-lysine + NAD+ + H2O = 2-aminoadipate-6-semialdehyde + NADH + H+ + NH3
-
L-lysine + NAD+ + H2O = alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
L-lysine + NADP+ = 2-aminoadipate-6-semialdehyde + NADPH
-
L-lysine + nicotinamide guanine dinucleotide + H2O = alpha-aminoadipate delta-semialdehyde + NH3 + nicotinamide guanine dinucleotide
-
L-Lysine + H2O + NAD+ = ? + NH3 + NADH
-
L-lysine + H2O + NAD+ = 6-amino-2-oxohexanoate + NH3 + NADH + H+
-
6,6-dideutrolysine + O2 + H2O = ? + NH3 + H2O2
-
L-lysine + O2 + H2O = 6-amino-2-oxohexanoate + NH3 + H2O2
391752, 391745, 487988, 690068, 742804, 764336, 742803, 391750, 742220, 741611, 741812, 741873, 763875, 684396, 711868, 725912, 765287, 391748, 391751, 391746, 391747, 391749, 725911, 765065, 765729
-
L-lysine + semicarbazide + ? = 4-methyl-2-oxopentanoate + ?
-
L-Lys + H2O + O2 = 6-amino-2-oxo-hexanoic acid + NH3 + H2O2
741737, 742047, 743869, 741736, 697466, 741749, 742345, 742530, 742930, 743253, 741725
-
L-Lys + H2O + O2 = 6-amino-2-oxohexanoate + NH3 + H2O2
-
L-Lys + H2O + O2 = 6-amino-2-oxohexanoic acid + NH3 + H2O2
-
L-lysine + H2O + O2 = 6-amino-2-oxohexanoate + NH3 + H2O2
-
L-lysine + H2O + O2 = 6-amino-2-oxohexanoic acid + NH3 + H2O2
391789, 391808, 391784, 711874, 692650, 694300, 391824, 695208, 670963, 668580, 692408, 724814, 692863, 695209, 711872, 763035, 391770, 711980, 711786, 651026, 695281
-
lysine + H2O + O2 = 6-amino-2-oxohexanoic acid + NH3 + H2O2
-
L-lysine + O2 + H2O = (S)-2-amino-6-oxohexanoate + H2O2 + NH3
-
L-lysine + O2 + H2O = 2-aminoadipate 6-semialdehyde + H2O2 + NH3
-
L-lysine + O2 + H2O2 = 2-aminoadipate 6-semialdehyde + NH3 + H2O2
-
lysine + H2O + O2 = 2-aminohexanoic acid + NH3 + H2O2
-
L-lysine + H2O + O2 = 2-oxolysine + NH3 + H2O2
-
L-Lys + pyruvate + NADH = Lysopine + NAD+ + H2O
-
L-Lys + pyruvate + NADPH = Lysopine + NADP+ + H2O
-
L-lysine + pyruvate + NADH + H+ = ?
-
L-lysine + pyruvate + NADPH + H+ = ? + NADP+ + H2O
-
lysine + pyruvate + NADPH = N7-(1-carboxyethyl)lysine + NADP+ + H2O
-
L-lysine + 2-oxoglutarate + NADH + H+ = N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
-
L-lysine + 2-oxoglutarate + NADH = N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
-
L-lysine + alpha-ketoadipate + NADH = ?
-
L-lysine + alpha-ketobutyrate + NADH = ?
-
L-lysine + alpha-ketomalonate + NADH = ?
-
L-lysine + alpha-ketovalerate + NADH = ?
-
L-lysine + glyoxylate + NADH = ?
-
L-lysine + pyruvate + NADH = ?
-
L-Lys + 2-oxoglutarate + NADPH = N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
L-lysine + 2-oxoglutarate + NADH + H+ = N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
-
L-lysine + 2-oxoglutarate + NADPH + H+ = N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
L-lysine + 2-oxoglutarate + NADPH = N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
392365, 392374, 655470, 392372, 657056, 392369, 392375, 392360, 392361, 392357, 392358, 392368, 392362, 392359, 392363, 392364, 392366, 392356, 392367, 392371, 392373, 392370
-
glucose 6-phosphate + L-lysine + ? = fructosyl-6-phosphate L-lysine + ?
-
2 lysine + homocystine = glutathione disulfide + 2 homocysteine
-
S-adenosyl-L-methionine + L-Lys = S-adenosyl-L-homocysteine + methyl-L-Lys
-
S-adenosyl-L-methionine + L-Lys = S-adenosyl-L-homocysteine + N6-methyl-L-lysine
-
carbamoyl phosphate + L-lysine = phosphate + ?
-
carbamoyl phosphate + lysine = phosphate + homocitrulline
-
carbamoyl phosphate + L-lysine = phosphate + L-homocitrulline
-
arginine + lysine = homoarginine + ornithine
-
L-arginine + L-lysine = L-ornithine + L-homoarginine
-
benzoyl-CoA + lysine = ?
-
acetyl-CoA + L-lysine = CoA + N6-acetyl-L-lysine
-
Acs (AMP forming) + L-Lys = ?
-
acetyl phosphate + L-lysine = phosphate + N6-acetyl-L-lysine
-
acetyl-CoA + L-lysine = CoA + N6-acetyl-L-lysine
-
Cbz-Gln-Gly + L-lysine = Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
-
5-L-glutamyl-4-nitroanilide + L-Lys = 4-nitroaniline + 5-L-glutamyl-L-Lys
-
5-L-glutamyl-4-nitroanilide + L-lysine = 4-nitroaniline + 5-L-glutamyl-L-lysine
-
L-gamma-glutamyl-4-nitroanilide + L-lysine = 4-nitroaniline + 5-L-glutamyl-L-lysine
-
5-L-glutamyl-4-nitroanilide + Lys = 4-nitroaniline + 5-L-glutamyl-Lys
-
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-L-lysine
-
thiamine + L-lysine = ?
-
D-glyceraldehyde 3-phosphate + L-lysine = N2-(2-carboxyethyl)-L-lysine + phosphate
-
L-Lys + 2-oxo-4-phenyl-butanoic acid = L-homophenylalanine + 2-keto-6-aminocaproate
-
L-lysine + 8-amino-7-oxononanoate = (S)-2-amino-6-oxohexanoate + 7,8-diaminononanoate
-
L-lysine + 2-oxoglutarate = glutamate + 2-amino-7-oxooctanoic acid
-
pyruvate + L-lysine = L-alanine + ?
-
L-lysine + 2-oxoglutarate = L-glutamate + (S)-2-amino-6-oxohexanoate
-
L-lysine + 2-oxoadipate = 2-aminoadipate 6-semialdehyde + L-homoglutarate
-
L-lysine + 2-oxobutanoate = 2-aminoadipate 6-semialdehyde + 2-aminobutanoate
-
L-lysine + 2-oxoglutarate = (S)-2-amino-6-oxohexanoate + L-glutamate
-
L-lysine + 2-oxoglutarate = 2-aminoadipate 6-semialdehyde + 1-piperideine-6-carboxylic acid + L-glutamate
-
L-lysine + 2-oxoglutarate = 2-aminoadipate 6-semialdehyde + ?
-
L-lysine + 2-oxoglutarate = 2-aminoadipate 6-semialdehyde + L-glutamate
637023, 671149, 637026, 637031, 392143, 637017, 637018, 637019, 637020, 637021, 637022, 637024, 700004, 675405, 637016, 637027, 637030
-
L-lysine + 2-oxohexanoate = 2-aminoadipate 6-semialdehyde + 2-aminohexanoate
-
L-lysine + 2-oxopentanoate = 2-aminoadipate 6-semialdehyde + 2-aminopentanoate
-
L-lysine + oxaloacetate = 2-aminoadipate 6-semialdehyde + L-aspartate
-
L-lysine + pyruvate = 2-aminoadipate 6-semialdehyde + L-alanine
-
L-lysine + 2-oxoglutarate = 2-oxo-6-aminohexanoate + L-glutamate
-
L-lysine + 4-methyl-2-oxovalerate = 2-oxo-6-aminohexanoate + L-leucine
-
L-lysine + pyruvate = 2-oxo-6-aminohexanoate + L-alanine
-
L-lysine + 4,5-dioxopentanoate = 5-aminolevulinate + 6-amino-2-oxohexanoate
-
lysine + pyruvate = 6-amino-2-oxohexanoate + alanine
-
L-lysine + alpha-ketomethiobutyrate = 2-oxo-6-amino-hexanoate + L-methionine
-
L-lysine + glyoxylate = ?
-
L-lysine + pyruvate = 2-aminoadipate 6-semialdehyde + L-alanine
-
L-lysine + oxaloacetic acid = ?
-
L-lysine + pyruvate = DELTA1-piperideine-2-carboxylate + L-alanine
-
L-lysine + pyruvate = DELTA1-piperidine-2-carboxylate + L-alanine
-
L-lysine + H2O = ? + NH3
-
L-Lys = 1,5-diaminopentane + CO2
-
L-lysine = 1,5-diaminopentane + CO2
-
L-lysine = cadaverine + CO2
-
L-Lys = Cadaverine + CO2
704086, 37288, 37286, 37289, 37292, 37293, 37299, 690597, 37297, 690395, 37294, 37295, 37296, 37298, 37290, 37283, 37285, 37300, 37284, 37287, 37291, 654982, 690269, 654984, 655829
-
L-lysine = 1,5-diaminopentane + CO2
-
L-lysine = cadaverine + CO2
680484, 747039, 747358, 747357, 747655, 748513, 749097, 749101, 680477, 748380, 714832, 746801, 747369, 747396, 748377, 748386, 749315, 727766, 749366, 748382, 749226, 747594, 748418, 747444, 715142, 728013
-
L-lysine = 1,5-diaminopentane + CO2
-
L-lysine = 1,5-diaminopentane + CO2
-
L-lysine = cadaverine + CO2
-
L-lysine = L-pipecolate + NH3
-
(S)-lysine = (S)-beta-lysine
-
alpha-lysine = beta-lysine
-
L-Lys = (3R)-3,6-diaminohexanoic acid
-
L-Lys = (3S)-3,6-diaminohexanoic acid
3380, 3376, 3381, 3385, 3386, 3387, 3390, 3391, 3392, 3393, 3394, 3378, 3382, 3383, 3384, 3388, 3389, 678459, 677675, 3375, 3377, 3379, 678156
-
L-lysine = (3S)-3,6-diaminohexanoate
-
L-lysine = (3S)-3,6-diaminohexanoic acid
-
L-lysine = L-beta-lysine
-
L-lysine = 2,5-diaminohexanoate
-
L-lysine = L-2,5-diaminohexanoate
-
L-lysine = (3R)-3-methyl-D-ornithine
-
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
-
ATP + L-lysine + Escherichia coli tRNALys = AMP + diphosphate + L-lysyl-tRNALys
-
ATP + L-lysine + Escherichia coli tRNALys CNBr-treated = AMP + diphosphate + L-lysyl-tRNALys CNBr-treated
-
ATP + L-lysine + Escherichia coli wild type tRNA = ?
-
ATP + L-lysine + Escherichia coli wild type tRNALys = AMP + diphosphate + L-lysyl-tRNALys
-
ATP + L-lysine + human tRNALys3 = AMP + diphosphate + L-lysyl-tRNALys3
-
ATP + L-lysine + Methanococcus maripaludis tRNALys = AMP + diphosphate + L-lysyl-tRNALys
-
ATP + L-lysine + Methanococcus maripaludis tRNALys CNBr-treated = AMP + diphosphate + L-lysyl-tRNALys CNBr-treated
-
ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
652046, 727475, 727934, 728305, 728835, 744423, 745539, 504, 479, 727514, 727275, 691093, 694885, 744901, 693367, 726591, 744902, 746197, 744162, 744283, 744501
-
ATP + L-lysine + tRNALys = AMP + L-lysyl-tRNALys + diphosphate
652528, 653627, 661087, 673550, 676209, 674885, 653072, 662382, 662735, 662738, 663247, 673690, 674597, 674805, 674869, 675937, 674875, 672047, 653644, 650620, 652053, 653323, 649930, 649906, 651752, 661755, 661858, 663381
-
ATP + L-lysine + tRNALys from rat liver = AMP + diphosphate + L-lysyl-tRNALys
-
ATP + L-lysine + tRNALysCUU = AMP + L-lysyl-tRNALysCUU + diphosphate
-
ATP + L-lysine + tRNALysGUU = AMP + L-lysyl-tRNALysGUU + diphosphate
-
ATP + L-lysine + tRNALysUCU = AMP + L-lysyl-tRNALysUCU + diphosphate
-
ATP + L-lysine + tRNALysUGU = AMP + L-lysyl-tRNALysUGU + diphosphate
-
ATP + L-lysine + tRNALysUUC = AMP + L-lysyl-tRNALysUUC + diphosphate
-
ATP + L-lysine + tRNALysUUG = AMP + L-lysyl-tRNALysUUG + diphosphate
-
ATP + L-lysine + tRNALysUUU = AMP + L-lysyl-tRNALysUUU + diphosphate
-
ATP + L-lysine + tRNALysUUUmodified = AMP + L-lysyl-tRNALysUUUmodified + diphosphate
-
ATP + L-lysine + tRNATyrCUA = AMP + L-lysyl-tRNATyrCUA + diphosphate
-
ATP + L-lysine + yeast tRNALys = AMP + diphosphate + L-lysyl-tRNALys
-
formycin 5'-triphosphate + L-lysine + tRNALys = formycin 5'-monophosphate + diphosphate + L-lysyl-tRNALys
-
2-chloroadenosine 5'-triphosphate + lysine + tRNALys = 2-chloroadenosine 5'-monophosphate + Lys-tRNALys + diphosphate
-
ATP + lysine + tRNALys = ?
-
ATP + lysine + tRNALys = AMP + L-lysyl-tRNALys + diphosphate
489, 481, 482, 484, 485, 486, 490, 499, 652421, 653377, 488, 494, 495, 497, 498, 500, 501, 503, 504, 505, 273, 480, 487, 496, 60, 483, 91, 479, 652901, 651752, 439, 652250, 506, 649906
-
ATP + lysine + tRNALys,3'-59mer = AMP + L-lysyl-tRNALys, 3'-59mer + diphosphate
-
ATP + lysine + tRNALysU35A = AMP + L-lysyl-tRNALysU35A + diphosphate
-
ATP + lysine + tRNALysU35C = AMP + L-lysyl-tRNALysU35C + diphosphate
-
ATP + lysine + tRNALysU36A = AMP + L-lysyl-tRNALysU36A + diphosphate
-
ATP + lysine + tRNALysU36C = AMP + L-lysyl-tRNALysU36C + diphosphate
-
dATP + lysine + tRNALys = dAMP + L-lysyl-tRNALys + diphosphate
-
ATP + L-lysine + beta-alanine = ADP + phosphate + ?
-
ATP + Lys + beta-Ala = AMP + phosphate + beta-Ala-Lys
-
ATP + UDP-MurNAc-L-Ala-D-Glu + L-Lys = ?
-
ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-L-lysine
-
ATP + indoleacetate + L-Lys = ?
-
ATP + indoleacetate + L-Lys = ADP + N6-[(indole-3-yl)acetyl]-L-Lys + phosphate
-
ATP + L-arginine + lysine = ? + AMP
-
ATP + L-tyrosine + lysine = ? + AMP
-
alpha-aminoadipic acid + L-valine + L-lysine + ? = L-delta-alpha-aminoadipyl-L-cysteinyl-D-valine + ?
-
UDP-N-acetylmuramoyl-L-Ala-D-Glu + L-Lys + ATP = UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys + ADP + phosphate
-
ATP + L-phenylalanine + L-lysine = ADP + phosphate + L-phenylalanyl-L-lysine
-
ATP + L-tryptophan + L-lysine = ADP + phosphate + L-tryptophyl-L-lysine
-
ATP + lysine + histidine = ADP + phosphate + L-lysyl-L-histidine
-
ATP + lysine + phenylalanine = ADP + phosphate + L-lysyl-L-phenylalanine
-
ATP + (3R)-3-methyl-D-ornithine + L-lysine = ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
-
ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu + L-Lys = ?
-
ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu + L-Lys = ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys
-
ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine
-
2 ATP + 2 L-Val + L-Lys = 2 ADP + 2 phosphate + L-Val-L-Val-L-Lys
-
mature [tRNAIle2]-cytidine34 + L-lysine + ATP = mature [tRNAIle2]-2-lysylcytidine34 + AMP + diphosphate
-
precursor [tRNAIle2]-cytidine34 + L-lysine + ATP = precursor [tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
[tRNAIle2]-cytidine34 + L-lysine + 7-deazaadenosine 5'-triphosphate = [tRNAIle2]-2-L-lysylcytidine34 + 7-deazaadenosine 5'-phosphate + diphosphate
-
[tRNAIle2]-cytidine34 + L-lysine + 8-azidoadenosine 5'-triphosphate = [tRNAIle2]-2-L-lysylcytidine34 + 8-azidoadenosine 5'-phosphate + diphosphate
-
[tRNAIle2]-cytidine34 + L-lysine + ATP = [tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
[tRNAIle2]-cytidine34 + L-lysine + ATP = [tRNAIle2]-lysidine34 + AMP + diphosphate + H2O
-
[tRNAIle2]-cytidine34 + L-lysine + N6-methyladenosine-5'-triphosphate = [tRNAIle2]-2-L-lysylcytidine34 + N6-methyladenosine-5'-phosphate + diphosphate
-
ATP + H2O + L-Lys/out = ADP + phosphate + L-Lys/in
-
ATP + H2O + L-lysine/out = ADP + phosphate + L-lysine/in
-
ATP + H2O + lysine/out = ADP + phosphate + lysine/in
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6-oxohexanoic acid + NADH + H+ + NH3 = L-lysine + NAD+ + H2O
-
alpha-N-(5'-phospho-4'-pyridoxyl)-L-lysine + H2O + O2 = pyridoxal 5'-phosphate + L-lysine + H2O2
-
epsilon-pyridoxyllysine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + lysine + H2O2
-
N2-(D-1-carboxyethyl)-L-lysine + NADP+ + H2O = L-lysine + pyruvate + NADPH
-
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-lysine + 2-oxoglutarate + NADH
-
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-lysine + 2-oxoglutarate + NADH + H+
-
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-lysine + 2-oxoglutarate + NADH + H+
-
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-lysine + 2-oxoglutarate + NADPH + H+
-
deoxy-D-fructosyl-AcGly-Lys + O2 + H2O = ? + L-lysine + H2O2
-
deoxy-D-fructosyl-AcPhe-Lys + O2 + H2O = ? + L-lysine + H2O2
-
deoxy-D-fructosyl-Lys-Phe + O2 + H2O = ? + L-lysine + H2O2
-
deoxy-D-fructosyl-Lys-Ser + O2 + H2O = ? + L-lysine + H2O2
-
fructosyl L-lysine + O2 + H2O = glucosone + L-lysine + H2O2
-
fructosyl-L-lysine + O2 + H2O = glucosone + L-lysine + H2O2
-
Nalpha-fructosyl L-lysine + O2 + H2O = glucosone + L-lysine + H2O2
-
Nepsilon-(1-deoxy-D-fructos-1-yl)-L-lysine + O2 + H2O = ? + L-lysine + H2O2
-
Nepsilon-fructosyl L-lysine + O2 + H2O = glucosone + L-lysine + H2O2
-
Nepsilon-fructosyl-L-lysine + O2 + H2O = glucosone + L-lysine + H2O2
-
D-difructosyllysin + O2 + H2O = glucosone + lysine + H2O2
-
N6,N6-dimethyl-L-lysine + O2 + H2O = L-lysine + formaldehyde + H2O2
-
N6-ethyl-L-lysine + H2O + O2 = L-lysine + acetaldehyde + H2O2
-
N6-methyl-L-lysine + O2 + H2O = L-lysine + formaldehyde + H2O2
-
epsilon-N-methyl-L-lysine + acceptor + H2O = formaldehyde + L-lysine + reduced acceptor
-
homoarginine + glycine = homoornithine + guanidinoacetate
-
L-ornithine + L-homoarginine = L-arginine + L-lysine
-
5-L-glutamyl-L-lysine + acceptor = L-lysine + 5-L-glutamyl-acceptor
-
L-Lys-tRNALys + H2O = L-lysine + tRNALys
-
Lys-tRNA + H2O = Lys + tRNA
-
L-lysine ethyl ester + H2O = L-lysine + ethanol
-
L-lysine methyl ester + H2O = L-lysine + methanol
-
L-lysine-7-amido-4-methylcoumarin + H2O = L-lysine + 7-amino-4-methylcoumarin
-
lysine-4-nitroanilide + H2O = lysine + 4-nitroaniline
-
L-Lys-4-nitroanilide + H2O = L-Lys + 4-nitroaniline
-
L-Lys-4-nitroanilide + H2O = L-lysine + 4-nitroaniline
-
L-lysine-4-methylcoumaryl-7-amide + H2O = L-lysine + 7-amino-4-methylcoumarin
-
L-lysine-4-nitroanilide + H2O = L-lysine + 4-nitroaniline
-
L-lysyl-4-nitroanilide + H2O = L-lysine + 4-nitroaniline
-
L-lysyl-7-amido-4-methylcoumarin + H2O = L-lysine + 7-amino-4-methylcoumarin
-
Lys-4-nitroanilide + H2O = L-lysine + 4-nitroaniline
-
Lys 4-nitroanilide + H2O = Lys + 4-nitroaniline
-
Lys-4-nitroanilide + H2O = Lys + 4-nitroaniline
-
L-Lys-4-nitroanilide + H2O = 4-nitroaniline + L-Lys
-
L-Lys-4-nitroanilide + H2O = L-Lys + 4-nitroaniline
-
L-Lys-p-nitroanilide + H2O = L-Lys + p-nitroaniline
-
Lys-4-nitroanilide + H2O = Lys + 4-nitroaniline
-
Lys-Gly + H2O = Lys + Gly
-
Ala-Lys + H2O = Ala + Lys
-
L-lysine-4-methylcoumaryl-7-amide + H2O = L-lysine + 7-amino-4-methylcoumarin
-
Lys-2-naphthylamide + H2O = Lys + 2-naphthylamine
-
Lys-7-amido-4-methylcoumarin = Lys + 7-amino-4-methylcoumarin
-
Lys-p-nitroanilide + H2O = Lys + p-nitroaniline
-
Met-Lys-bradykinin + H2O = Met + Lys + bradykinin
-
L-lysine 4-nitroanilide + H2O = L-lysine + 4-nitroaniline
-
L-lysyl-4-nitroanilide + H2O = L-lysine + 4-nitroaniline
-
(Lys)3 + H2O = Lys + Lys-Lys
-
Lys-4-nitroanilide + H2O = Lys + 4-nitroaniline
-
Lys-7-amido-4-methylcoumarin + H2O = Lys + 7-amino-4-methylcoumarin
-
Lys-Ala + H2O = Lys + Ala
-
Lys-Ala-4-methylcoumaryl-7-amide + H2O = Lys + Ala-4-methylcoumaryl-7-amide
-
Lys-Gly-Gly + H2O = Lys + Gly-Gly
-
Lys-Gly-Gly-Lys + H2O = Lys + Gly-Gly-Lys
-
Lys-Leu + H2O = Lys + Leu
-
Lys-Lys-Lys + H2O = Lys + Lys-Lys
-
Lys-Lys-Lys-Lys + H2O = Lys + Lys-Lys-Lys
-
Lys-Phe + H2O = Lys + Phe
-
L-Lys-2-naphthylamide + H2O = L-Lys + 2-naphthylamine
-
L-Lys-4-nitroanilide + H2O = L-Lys + 4-nitroaniline
-
L-Lys-4-nitroanilide = 4-nitroaniline + L-Lys
-
L-Lys-7-amido-4-carbamoylmethylcoumarin + H2O = L-Lys + 7-amino-4-carbamoylmethylcoumarin
-
L-Lys-L-Arg + H2O = L-Lys + L-Arg
-
L-Lys-L-Lys + H2O = L-Lys
-
L-Lys-L-Phe + H2O = L-Lys + L-Phe
-
L-lysine 4-methylcoumaryl-7-amide + H2O = L-lysine + 7-amino-4-methylcoumarin
-
Lys-4-methylcoumarin 7-amide + H2O = Lys + 7-amino-4-methylcoumarin
-
Lys-4-nitroanilide + H2O = Lys + 4-nitroaniline
-
Lys-beta-naphthylamide + H2O = Lys + beta-naphthylamine
-
Lys-p-nitroanilide + H2O = Lys + p-nitroaniline
-
Met-Lys-bradykinin + H2O = Met + Lys + bradykinin
-
L-Lys 4-nitroanilide + H2O = L-Lys + 4-nitroaniline
-
L-Lys-p-nitroanilide + H2O = L-Lys + p-nitroaniline
-
Lys-Ala + H2O = L-Lys + L-Ala
-
Asp-Lys + H2O = Asp + Lys
-
Lys 2-naphthylamide + H2O = Lys + 2-naphthylamine
-
L-Lys-2-naphthylamide + H2O = L-Lys + 2-naphthylamine
-
L-Lys-4-nitroanilide + H2O = L-Lys + 4-nitroaniline
-
Lys 2-naphthylamide + H2O = Lys + 2-naphthylamine
-
Lys 4-nitroanilide + H2O = Lys + 4-nitroaniline
-
Lys-4-nitroanilide + H2O = Lys + 4-nitroaniline
-
L-Lys-4-nitroanilide + H2O = L-Lys + 4-nitroaniline
-
L-lysine-4-nitroanilide + H2O = L-lysine + 4-nitroaniline
-
Lys-4-nitroanilide + H2O = Lys + 4-nitroaniline
-
L-Lys-2-naphthylamide + H2O = L-Lys + 2-naphthylamine
-
L-lysine-p-nitroanilide + H2O = L-lysine + p-nitroaniline
-
Lys-4-methylcoumaryl-7-amide + H2O = Lys + 7-amino-4-methylcoumarin
-
L-Lys-4-nitroanilide + H2O = 4-nitroaniline + L-Lys
-
Lys-Gly-Gly + H2O = Lys + Gly-Gly
-
Lys-4-nitroanilide + H2O = L-lysine + p-nitroaniline
-
Pro-Lys + H2O = Pro + Lys
-
L-Lys-(Met)enkephalin + H2O = L-Lys + (Met)enkephalin
-
L-Lys-2-naphthylamide + H2O = L-Lys + 2-naphthylamine
-
L-Lys-4-nitroanilide + H2O = L-Lys + 4-nitroaniline
-
L-Lys-7-amido-4-methylcoumarin + H2O = L-Lys + 7-amino-4-methylcoumarin
-
L-Lys-p-nitroanilide + H2O = L-Lys + p-nitroaniline
-
L-Lys-peptide + H2O = L-Lys + peptide
-
L-lysine-2-naphthylamide + H2O = 2-naphthylamine + L-Lys
-
Arg-Lys + H2O = Arg + Lys
-
Arg-Lys-somatostatin-14 + 2 H2O = Arg + Lys + somatostatin-14
-
kallidin-10 + H2O = Lys + bradykinin
-
Lys 4-methylcoumarin 7-amide + H2O = Lys + 7-amino-4-methylcoumarin
-
Lys-2-naphthylamide + H2O = Lys + 2-naphthylamine
-
Lys-4-methylcoumarin 7-amide + H2O = Lys + 7-amino-4-methylcoumarin
-
Lys-4-nitroanilide + H2O = Lys + 4-nitroaniline
-
Lys-7-amido-4-methylcoumarin + H2O = Lys + 7-amino-4-methylcoumarin
-
Lys-Ala + H2O = Lys + Ala
-
Lys-Leu-2-naphthylamide + H2O = Lys + Leu-2-naphthylamide
-
Lys-Lys + H2O = Lys + Lys
-
L-lysine-beta-naphthylamide + H2O = L-lysine + beta-naphthylamine
-
kallidin + H2O = Lys + bradykinin
-
L-Lys-Pro-7-amido-4-carbamoylmethylcoumarin + H2O = L-Lys + Pro-7-amido-4-carbamoylmethylcoumarin
-
KPSFVRFamide + H2O = Lys + PSFVRFamide
-
Lys-Pro-Arg + H2O = Lys + Pro-Arg
-
Lys-Pro-p-nitroanilide + H2O = Lys + Pro-p-nitroanilide
-
L-lysyl 4-nitroanilide + H2O = L-lysine + 4-nitroaniline
-
L-lysyl 4-nitroanilide + H2O = L-lysine + 4-nitroaniline
-
Gly-L-Lys + H2O = Gly + L-Lys
-
L-Lys-4-methylcoumarin 7-amide + H2O = L-Lys + 7-amino-4-methylcoumarin
-
Pro-Lys + H2O = Pro + Lys
-
L-Ala-L-Lys + H2O = L-Ala + L-Lys
-
Lys-Gly + H2O = Lys + Gly
-
L-Lys-4-nitroanilide + H2O = L-Lys + 4-nitroaniline
-
L-Asp-L-Lys + H2O = L-Asp + L-Lys
-
L-Val-L-Lys + H2O = L-valine + L-lysine
-
aminoacyl-L-lysine + H2O = L-lysine + acylamine
-
Nalpha-(gamma-aminobutryryl)-Lys + H2O = 4-aminobutyrate + Lys
-
L-Lys-L-Pro + H2O = L-Lys + L-Pro
-
Lys-Pro + H2O = Lys + Pro
-
L-Ala-gamma-D-Glu-L-Lys + H2O = L-Ala-D-Glu + L-Lys
-
benzoyl-Gly-Lys + H2O = benzoyl-Gly + Lys
-
furylacryloyl-Ala-Lys + H2O = furylacryloyl-Ala + Lys
-
benzyloxycarbonyl-Gly-Lys + H2O = benzyloxycarbonyl-Gly + L-lysine
-
alpha-factor-Lys-Arg + H2O = mature active alpha-factor + Lys + Arg
-
furylacryloyl-Ala-Lys + H2O = furylacryloyl-Ala + Lys
-
(Met)enkephalin-Lys + H2O = Tyr-Gly-Gly-Phe-Met + Lys
-
D-Tyr-Ala-His-Lys-Lys + H2O = D-Tyr-Ala-His-Lys + Lys
-
dansyl-Gly-Lys + H2O = dansyl-Gly + Lys
-
Hippuryl-L-Lys + H2O = Hippuric acid + L-Lys
-
benzoyl-Ala-Lys + H2O = benzoyl-Ala + Lys
-
benzoyl-Gly-Lys + H2O = benzoyl-Gly + Lys
-
dynorphin A(1-13) + H2O = Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu + Lys
-
furylacryloyl-Ala-Lys + H2O = furylacryloyl-Ala + Lys
-
SDF-1alpha + H2O = des-lys SDF-1alpha + lysine
-
N-carbobenzoxy-Ala-Ala-Lys + H2O = N-carbobenzoxy-Ala-Ala + Lys
-
hippuryl-L-Lys = hippuric acid + L-Lys
-
furylacryloyl-L-alanyl-L-lysine + H2O = furylacryloyl-L-alanine + L-lysine
-
hippuryl-Lys + H2O = hippuric acid + Lys
-
Val-Asp-Asp-Asp-Lys + H2O = Lys + Asp + ?
-
fibrin + H2O = fibrin + L-Lys
-
Fibrin, partially degraded + H2O = Fibrin, partially degraded + L-Lys + L-Arg
-
Hippuryl-L-Lys + H2O = Hippuric acid + L-Lys
-
N-[3-(2-Furylacryloyl)]-L-Ala-L-Lys + H2O = N-[3-(2-Furylacryloyl)]-L-Ala + L-Lys
-
hippuryl-L-lysine + H2O = hippuric acid + L-lysine
-
anisylazoformyl-Lys + H2O = anisylazoformic acid + Lys
-
fibrin + H2O = fibrin + Lys
-
Lys-plasminogen + H2O = Lys + plasmin
-
Lys6-Leu5-enkephalin + H2O = Tyr-Gly-Gly-Phe-Leu + Lys
-
Lys6-Met5-enkephalin + H2O = Tyr-Gly-Gly-Phe-Met + Lys
-
pGlu-Leu-Thr-Phe-Ser-Pro-Asp-Trp-Gly-Lys + H2O = pGlu-Leu-Thr-Phe-Ser-Pro-Asp-Trp-Gly + Lys
-
Tyr-Gly-Gly-Phe-Leu-Lys + H2O = Tyr-Gly-Gly-Phe-Leu + Lys
-
YGGFLRRIRPKLK + H2O = YGGFLRRIRPKL + L-Lys
-
dynorphin A 1-13 + H2O = dynorphin A 1-12 + Lys
-
dynorphin A(1-13) + H2O = YGGFLRRIRPKL + Lys
-
Hippuryl-L-Lys + H2O = Hippuric acid + L-Lys
-
benzoyl-Gly-Lys + H2O = benzoyl-Gly + Lys
-
benzyloxycarbonyl-Val-Gly-Lys-Lys + H2O = Lys + benzyloxycarbonyl-Val-Gly-Lys
-
furylacryloyl-Ala-L-Lys + H2O = furylacryloylalanine-Ala + Lys
-
furylacryloyl-Gly-Lys + H2O = furylacryloyl-Gly + Lys
-
furylacryloyl-L-Ala-L-Lys + H2O = furylacryloyl-L-Ala + Lys
-
Gly-His-Lys + H2O = Gly-His + Lys
-
Pro-Phe-Gly-Lys + H2O = Pro-Phe-Gly + Lys
-
Pro-Phe-Lys + H2O = Pro-Phe + Lys
-
Thr-Pro-Arg-Lys + H2O = Thr-Pro-Arg + Lys
-
YFPGQFAFSK + H2O = YFPGQFAFS + lysine
-
N-[3-(2-Furylacryloyl)]-L-Ala-L-Lys + H2O = N-[3-(2-Furylacryloyl)]-L-Ala + L-Lys
-
benzoyl-glycyl-L-lysine + H2O = benzoyl-glycine + L-lysine
-
N-carboxybenzoyl-Ala-Lys + H2O = N-carboxybenzoyl-Ala + L-lysine
-
2-aminobenzoyl-Phe-Arg-Lys + H2O = 2-aminobenzoyl-Phe-Arg + Lys
-
N-acetyl-Ala-Lys + H2O = N-acetyl-Ala + Lys
-
N-acetyl-Met-epsilon-Lys + H2O = N-acetyl-Met + Lys
-
N-acetyl-Met-Lys + H2O = N-acetyl-Met + Lys
-
N2-Lys-ubiquitin + H2O = ubiquitin + Lys
-
N6-Lys-ubiquitin + H2O = ubiquitin + Lys
-
pyroglutamyl-Lys + H2O = pyroglutamate + Lys
-
beta-L-Asp-L-Lys + H2O = L-Asp + L-Lys
-
beta-Asp-Lys + H2O = Asp + Lys
-
L-Lys-4-nitroanilide + H2O = L-Lys + 4-nitroaniline
-
Lys-p-nitroanilide + H2O = Lys + p-nitroaniline
-
Lys-2-naphthylamide + H2O = Lys + 2-naphthylamine
-
L-Lys-7-amido-4-methylcoumarin + H2O = L-Lys + 7-amino-4-methylcoumarin
-
L-Lys-beta-naphthylamide + H2O = L-Lys + beta-naphthylamine
-
Lys-4-methylcoumaryl-7-amide + H2O = Lys + 7-amino-4-methylcoumarin
-
Gly-Lys + H2O = Gly + Lys
-
Lys-p-nitroanilide + H2O = Lys + 4-nitroaniline
-
acetyl-CDEVDK + H2O = acetyl-CDEVD + Lys
-
biotinylated acetyl-CDEVDK + H2O = biotinylated acetyl-CDEVD + Lys
-
Abz-TTKLKAAK(Dnp)-NH2 + H2O = Abz-TTKL + L-Lys + L-Ala + AK(Dnp)-NH2
-
Abz-TTKLKAAK(Dnp)-NH2 + H2O = Abz-TTKL + L-Lys + L-Ala + AK(Dnp)-NH2
-
FVNQHLCGSHLVEALYVCGERGFFYTPKA + H2O = FVNQHLCGSH + Lys-Val-Glu-Ala + Lys + YVCGERGF + FYTPKA
-
N-acetyl-L-lysine + H2O = acetate + L-lysine
-
1'-N-methoxycarbonyl-biocytin + H2O = 1-N-methoxycarbonyl-biotin + L-lysine
-
biocytin + ? = biotin + L-lysine
-
biocytin + H2O = biotin + L-lysine
-
epsilon-N-biotinyl-L-lysine + H2O = biotin + L-lysine
-
L-Lys beta-naphthylamide + H2O = Lys + beta-naphthylamine
-
[carrier protein LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate + H2O = [carrier protein LysW]-C-terminal-L-glutamate + L-lysine
-
[CT10-LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate + H2O = [CT10-LysW]-C-terminal-L-glutamate + L-lysine
-
N-lauroyl-L-Lys + H2O = laurate + L-Lys
-
N-alpha-acetyl-L-lysine + H2O = acetate + L-lysine
-
N-lauryl-L-lysine + H2O = laurate + L-lysine
-
Nalpha-lauroyl-L-lysine + H2O = laurate + L-lysine
-
Nepsilon-lauroyl-L-lysine + H2O = laurate + L-lysine
-
N-acetyllysine + H2O = lysine + acetate
-
N-acetyllysine + H2O = acetate + lysine
-
Nalpha-acetyl-L-lysine + H2O = L-lysine + acetate
-
N2-acetyl-L-lysine + H2O = L-lysine + acetate
-
N2-benzoyl-L-lysine + H2O = L-lysine + benzoate
-
N6-acetyl-L-lysine + H2O = L-lysine + acetate
-
N6-acyl-L-lysine + H2O = a carboxylate + L-lysine
-
N6-acyl-L-lysine + H2O = L-lysine + carboxylic acid
-
N6-alpha-naphthoyl-L-lysine + H2O = L-lysine + 1-naphthol
-
N6-benzoyl-L-lysine + H2O = L-lysine + benzoate
-
N6-butyryl-L-lysine + H2O = L-lysine + butanoate
-
N6-caproyl-L-lysine + H2O = L-lysine + n-hexanoate
-
N6-caprylyl-L-lysine + H2O = L-lysine + caprylic acid
-
N6-carbobenzoxy-L-lysine + H2O = L-lysine + benzoate
-
N6-chloroacetyl-L-lysine + H2O = L-lysine + chloroacetate
-
N6-cyclohexanecarboxyl-L-lysine + H2O = L-lysine + cyclohexanecarboxylate
-
N6-dichloroacetyl-L-lysine + H2O = L-lysine + dichloroacetate
-
N6-formyl-L-lysine + H2O = L-lysine + formate
-
N6-glycyl-L-lysine + H2O = L-lysine + glycine
-
N6-iodoacetyl-L-lysine + H2O = L-lysine + iodoacetate
-
N6-isobutyryl-L-lysine + H2O = L-lysine + isobutyrate
-
N6-m-nitrobenzoyl-L-lysine + H2O = L-lysine + 3-nitrobenzoate
-
N6-metacrylyl-L-lysine + H2O = L-lysine + ?
-
N6-nicotinyl-L-Lysine + H2O = L-lysine + nicotinate
-
N6-p-nitrobenzoyl-L-lysine + H2O = L-lysine + 4-nitrobenzoate
-
N6-phenylacetyl-L-lysine + H2O = L-lysine + phenylacetate
-
N6-propionyl-lysine + H2O = L-lysine + propionate
-
N6-trichloroacetyl-L-lysine + H2O = L-lysine + trichloroacetate
-
DL-alpha-amino-beta-caprolactam + H2O = D-alpha-amino-beta-caprolactam + L-lysine
-
L-lysine-1,6-lactam + H2O = L-lysine
-
L-homoarginine + H2O = L-2,6-diaminohexanoate + urea
-
D,D-2,6-diaminoheptanedioate = L-lysine + CO2
-
DD-2,6-diaminoheptanedioate = L-lysine + CO2
-
diaminopimelate = L-lysine + CO2
-
DL-2,6-diaminoheptanedioate = L-lysine + CO2
-
meso-2,6-Diaminoheptanedioate = L-Lysine + CO2
4112, 4119, 4111, 4108, 4110, 4121, 4127, 649192, 4120, 2153, 4118, 2142, 4115, 4116, 4123, 4113, 4114, 4125, 4122, 4124, 0, 4109, 4128, 653897, 652392
-
epsilon-(gamma-L-glutamyl)-L-lysine = L-lysine + 5-oxo-L-proline
-
Nepsilon-(L-gamma-glutamyl)-L-lysine = L-lysine + 5-oxo-L-proline
-
2-N-(5-L-glutamyl)L-lysine = 5-oxoproline + L-lysine
-
alpha-N-(gamma-L-glutamyl)-L-lysine = L-lysine + 5-oxo-L-proline
-
L-gamma-glutamyl-L-epsilon-lysine = 5-oxoproline + L-lysine
-
Nepsilon-(5-L-glutamyl)-L-lysine = 5-oxoproline + L-lysine
-
AMP + diphosphate + L-lysyl-tRNALys = ATP + L-lysine + tRNALys
-
ATP + H2O + L-Lys/out = ADP + phosphate + L-Lys/in
-
ATP + H2O + L-lysine/out = ADP + phosphate + L-lysine/in
-
ATP + H2O + L-lysine-[L-lysine-binding protein][side 1] = ADP + phosphate + L-lysine[side 2] + [L-lysine-binding protein][side 1]
-
ATP + H2O + lysine/out = ADP + phosphate + lysine/in
-
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allosteric regulation of recombinant engineered homoserine dehydrogenase by nonnatural inhibitor L-lysine
-
substrate inhibition of the wild-type and mutant P14G enzymes
-
at 1 mM: 22% repression of the enzyme synthesis, at 5 mM: 44% repression of the enzyme synthesis, at 10 mM: 28% inhibition of the enzyme activity assayed in the reverse reaction
-
enzyme assayed in the reverse reaction at pH 10
-
slightly represses the enzyme
-
20% inhibition at 50 mM
-
54% inhibition at 1 mM and 80% inhibition at 4 mM
-
70% inhibition at 50 mM
-
competitive with respect to alpha-aminoadipate, non-competitive with respect to both ATP and NADPH
-
competitive with respect to alpha-aminoadipate. Presence of Lysine inhibits incorporation of alpha-aminoadipate into protein-bound lysine
-
enzyme from Schizosaccharomyces pombe is more sensitive to feedback inhibition by lysine in vitro than the enzyme of Saccharomyces cerevisiae
-
in strains Q176, D6/1014/A, and P2, in vivo activity of alpha-aminoadipate reductase from superior penicillin producer strains is more strongly inhibited by lysine, and this is related to their ability to accumulate increased amounts of alpha-aminoadipate, and hence penicillin
-
weak inhibition at pH 8.5, strong inhibition at pH 10.0
-
the presence of L-lysine during the oxidation of benzylamine results in time- and dose-dependent inhibition of SSAO activity, in a process that is dependent on the H2O2 formed during benzylamine oxidation
-
substrate inhibition, competitive versus NADH
-
1 mM, 43% inhibition of DEAE-unabsorbed transglutaminase, 90% inhibition of DEAE-absorbed transglutaminase
-
inhibition of alpha-S1-casein-dependent reaction
-
0.02 mM required for half-maximal inhibition of the enzyme from wild-type strain, enzyme from S-(beta-aminoethyl)-L-cysteine resistant mutant strain is not inhibited
-
10 mM, 80% inhibition. No inhibition by 10 mM D-Lys
-
5 mM, complete inhibition
-
50 mM, 48% inhibition. Feed-back inhibition
-
50% inhibition by 0.053 mM, at 6 mM 2-oxoglutarate
-
feedback inhibition of homocitrate synthase by lysine modulates the activation of LYS gene expression by transcriptional activator Lys14p
-
24.4% residual activity at 50 mM
-
competitive inhibitor versus 2-oxoglutarate up to a concentration of 1 mM
-
isoform Lys20 is one order of magnitude less sensitive to L-lysine inhibition than Lys21
-
binding to the less active enzyme conformer
-
feedback inhibitor, competitive versus 2-oxoglutarate and linear in the physiological range of lysine concentrations up to 5 mM
-
mutant enzyme lacking the RAM domain is insensitive to inhibition by lysine
-
regulated via feedback inhibition by the endproduct
-
strong allosteric inhibitor of Lys21p. Induces positive cooperativity for alpha-ketoglutarate binding
-
about 80% residual activity at 0.5 mM
-
1 mM, more than 80% reemaining activity
-
35% inhibition at 10 mM after 20 min
-
noncompetitive inhibition with respect to delta-aminovalerate, competitive inhibition to 2-oxoglutarate
-
5 mM decreases KAT II activity
-
less than 35% inhibition at 5 mM
-
higher inhibitory effect than with D-lysine
-
-
642308, 642312, 642314, 642315, 642316, 642317, 642319, 642324, 642325, 642326, 642331, 642334, 642335, 642337, 642339, 722849, 723377, 762121, 762473
-
2 mM, significant inhibition
-
40.72% residual activity at 10 mM
-
85.43% residual activity at 10 mM
-
85.43% residual activity at 10 mM. The inhibition rate for the single inhibitor is about 10%, this rate is further increased to 65% under the combined action of two inhibitors (Lys+Thr, Lys+Met, and Thr+Met)
-
AK is inhibited moderately by Lys, the enzyme is inhibited dramatically by simultaneous addition of Lys and Thr, dimerization of the regulatory subunit induced by Thr binding is a key step in the inhibitory mechanism of AK; feedback inhibition, inhibits moderately, simultaneous addition of lysine and threonine inhibits dramatically
-
AK1 is inhibited in a synergistic manner by lysine and S-adenosyl-L-methionine, in the absence of S-adenosyl-L-methionine AK1 displays low apparent affinity for lysine compared to AK2 and AK3; AK1 is inhibited in a synergistic manner by lysine and SAM; AK2 is inhibited by lysine, SAM by itself has no effect on the enzyme activity; AK3 is inhibited only by lysine, SAM by itself has no effect on the enzyme activity
-
Ask2-Oh545o2 and Ask2-Oh51Ao2 have similar lysine-sensitivity properties but differ in basal activity; Ask2-Oh545o2 and Ask2-Oh51Ao2 have similar lysine-sensitivity properties but differ in basal activity, to measure inhibition of AK activity by lysine, reaction rates using 50 mM Asp substrate are measured in the presence of 5 microM to 10 mM L-lysine
-
binding of L-lysine to the regulatory ACT1 domain in R-state AKIII instigates a series of changes that release a 'latch', the beta15-alphaK loop, from the catalytic domain, which in turn undergoes large rotational rearrangements, promoting tetramer formation and completion of the transition to the T-state. L-lysine-induced allosteric transition in AKIII involves both destabilizing the R-state and stabilizing the T-state tetramer. Rearrangement of the catalytic domain blocks the ATP-binding site, which is therefore the structural basis for allosteric inhibition of AKIII by L-lysine
-
concerted feedback inhibition with L-threonine
-
concerted feedback inhibition with L-threonine; L-threonine methyl ester and L-threonine amide are able to substitute for L-threonine in feedback inhibition, but the requirement for L-lysine is strict
-
each dimer contains two lysine binding sites, in which one site is exclusively found in the dimer with A and B chains located at the interface between alpha and beta subunits
-
enzyme is inhibited by lysine and threonine in a concerted manner: comparison of the crystal structures between inhibitory and active forms reveal that binding inhibitors causes a conformational change to a closed inhibitory form, and the interaction between the catalytic domain in the alpha subunit and beta subunit
-
enzyme is inhibited synergistically by L-threonine and L-lysine with the binding of threonine first. In the absence of L-lysine, the enzyme displays partial inhibition by L-threonine (50% residual activity at saturation with L-threonine) with a K0.5 value of 0.7 mM
-
feedback resistance of Ask, more than 20% relative activity of Ask in the assay mixture even with extremely high concentrations of 100 mM L-lysine and L-threonine each, L-Lysine alone has no effect on activity; more than 20% relative activity of rAsk is detected in the assay mixture even with extremely high concentrations of L-lysine and L-threonine (100 mM each), L-lysine alone has no effect on activity
-
inhibited 50% by 0.7 mM, almost completely by 5.0 mM
-
inhibits the activity of ThrA2 by 87% at 1 mM and by 96% at 10 mM, no concerted inhibition by L-lysine plus L-threonine
-
L-lysine inhibits Ask_LysC only in a mixture with L-threonine
-
no inhibition is observed
-
no inhibition is observed; the truncated protein is no longer inhibited by lysine, even at 10 mM, wild type protein is inhibited by lysine
-
no significant effect on AK activity at 5 and 20 mM
-
partially inhibits the first isoenzyme
-
repression of aspartokinase gene transcription
-
threonine and lysine exhibit concerted feedback inhibition of asparatate kinase. Large conformational changes in the catalytic domain are associated with the lysine binding at the regulatory domains, L-lysine binding site structure, overview
-
total and cytosolic creatine kinase activities are significantly inhibited by L-lysine, in contrast to the mitochondrial isoform which is not affected, the inhibitory effect of L-lysine on total creatine kinase activity is totally prevented by reduced glutathione
-
5fold higher concentration than L-Arg, 25% inhibition
-
3% enzyme inhibition at 2 mM
-
with hippuryl-argininic acid as substrate
-
slight inhibition of coaggregation of Porphyromonas gingivalis with other oral bacteria by L-lysine and more slightly by D-lysine
-
38.5% residual activity at 5 mM
-
binds to isoform arginase I with Kd of 13.1 microM
-
at 2 mM arginine, 42% and 67% inhibition of arginase 2 is observed by lasine at 1 mM and 10 mM. At 0.1 mM arginine, the conversion of arginine to ornithine by arginase 2 is inhibited by 44% and 88% in the presence of 1 mM and 10 mM lysine. No significant inhibition of arginase 2 is observed at physiological lysine concentrations; at concentrations of 1 and 10 mM, 39% and 78% inhibition of arginase 1 activity at Km concentration (3 mM) of the substrate arginine, and 44% and 81% inhibition at physiological arginine concentrations. No significant inhibitory effects of arginase 1 activity are observed with physiological concentrations of lysine, 0.1-1.0 mM
-
competitive inhibitor; potential competitive inhibitor
-
inhibition of the recombinant enzyme at high concentrations
-
competitive inhibition, 10 mM
-
substrate inhibition at high concentrations
-
substrate inhibition is observed from 1.25 M
-
involved in sequential feedback inhibition, pH-dependent
-
no detectable amounts of decarboxylation products
-
reversed by diaminoheptanedioate addition
-
50% inhibition at 0.2 mM, inhibits wild-type enzyme, but not mutant enzymes
-
partial mixed inhibition with respect to pyruvate and partial non-competitive inhibition with resoect to L-aspartate 4-semialdehyde
-
allosteric feedback inhibition; allosteric feedback inhibition; allosteric feedback inhibition; allosteric feedback inhibition; allosteric feedback inhibition; allosteric feedback inhibition; allosteric feedback inhibition, allosteric site modeling; allosteric feedback inhibition, allosteric site modeling; allosteric feedback inhibition, allosteric site modeling; allosteric feedback inhibition, allosteric site modeling
-
feedback inhibition, feedback inhibition of the Escherichia coli enzyme by lysine is successfully alleviated after substitution of the residues around the inhibitor's binding sites with those of the Corynabacterium glutamicum enzyme
-
feedback inhibition, the tetrameric enzyme has two allosteric sites, each of which binds two molecules of lysine. Lysine binds highly cooperatively, and primarily to the F form of the enzyme during the ping-pong mechanism. (S)-Lysine is an uncompetitive partial inhibitor with respect to its first substrate, pyruvate, and a mixed partial inhibitor with respect to its second substrate, (S)-aspartate-4-semialdehyde
-
feedback inhibitor, docking study with enzyme crystals
-
increasing amounts of (S)-lysine (0-200 mM) added, not inhibited under physiological conditions, binding site of the allosteric inhibitor lysine appears not to be conserved
-
mutant enzymes R138H and R138A show the same IC50 values as the wild-type enzyme, but different partial inhibition patterns
-
no significant conformational change between the pyruvate-bound and (S)-lysine-bound enzyme, presence of substrate has substantial effect on the nature of enzyme-inhibitor association, solvent plays a key role in binding of inhibitor
-
partial mixed inhibition with respect to (S)-aspartate 4-semialdehyde, partial non-ncompetitive inhibition with respect to pyruvate in wild-type and in Y107W mutant, Y107W mutant still retains over 25% of uninhibited activity, even at high inhibitor concentrations compared to the wild-type enzyme retaining less than 10% of normal activity
-
partial mixed inhibition with respect to its first substrate, pyruvate
-
0.1 mM, complete inhibition, I0.5: 0.02 mM
-
allosteric inhihitor. Allostery is mediated by changes in the extent of thermally activated conformational fluctuations
-
at 1 mM 23% residual activity, at 100 mM 13% residual activity
-
binding interaction of L-lysine is characterised as a cooperative event in which an entropic pre-organisation step precedes a secondary enthalpic association. This allosteric association is of a mixed competitive nature in which heterotropic ligand cooperativity is observed to subtly influence the binding events
-
binds at three sites to the enzyme, binding structure, overview
-
discussion of plant inhibition versus bacterial inhibition
-
feedback inhibition, binding of lysine to the allosteric cleft of the enzyme, cooperative binding, structural mechanism for allosteric inhibition, overview. With respect to L-aspartate-4-semialdehyde, lysine is a noncompetitive inhibitor
-
inhibition of the tetrameric wild-type enzyme, but not of the disrupted minimeric mutant enzyme. Allosteric binding by two molecules of (S)-lysine at the DHDPS tight-dimer interface cleft has been observed to operate via a cooperative mechanism and to result in incomplete partial mixed inhibition, inhibition kinetics, overview
-
is significantly more sensitive to feedback inhibition than Escherichia coli DHDPS
-
lack of feedback inhibition, not regulated under normal physiological conditions
-
natural feedback inhibitor
-
no difference in its sensitivity or behaviour with respect to L-lysine when compared to the wild-type
-
poor feedback inhibition by
-
inhibition of wild-type DHDPS by lysine with respect to pyruvate is partial and uncompetitive, and partial non-competitive with respect to L-aspartate 4-semialdehyde. Ethanolamine, n-butylamine, 1-amino-2-propanol, 3-amino-1-propanol, iso-butylamine and Tris-HCl cannot rescue activity
-
1% cell growth, 1% viability of cells
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.8
-
mutant D238F, pH 7, 30°C
2.7
-
mutant D238A, pH 7, 30°C
4.5
-
wild-type, pH 7, 30°C
8.1
-
mutant D238E, pH 7, 30°C
0.146
-
pH 7.5, 25°C, recombinant mutant P238R, with NADPH
0.18
-
pH 7.5, 25°C, recombinant mutant K64A, with NADH
0.34
-
pH 7.5, 25°C, recombinant mutant K64A, with NADPH
0.43
-
pH 7.5, 25°C, with NADH
0.55
-
pH 7.5, 25°C, with NADPH
6.1
-
pH 4.0, 50°C, L-lysine oxidase precursor prLysOX
17
-
pH 7.4, 40°C, mutant enzyme D212A/D315A
24.3
-
pH 7.4, 40°C, mutant enzyme D315A
26.4
-
pH 7.4, 40°C, mutant enzyme D212A
59.1
-
pH 7.4, 40°C, recombinant enzyme from Streptomyces lividans
62.8
-
pH 7.4, 40°C, recombinant enzyme from Escherichia coli
65.5
-
pH 7.4, 50°C, mature L-lysine oxidase
0.00085
-
pH 7, 37°C, EDTA-treated protein
0.0302
-
pH 7, 37°C, untreated protein
0.04
-
at pH 7.0 and 30°C
0.09
-
at pH 8.5 and 30°C
0.17
-
mutant D238F, pH 7, 30°C
0.5
-
mutant D238A, pH 7, 30°C
0.8
-
wild-type, pH 7, 30°C
2.3
-
mutant D238E, pH 7, 30°C
2.6
-
37°C, isozyme MPLAO1
4.7
-
37°C, isozyme MPLAO3
0.19
-
mutant enzyme Y211F, at pH 7.5 and 25°C
0.22
-
at pH 7.5 and 25°C
0.29
-
mutant enzyme C448D, at pH 7.5 and 25°C
0.34
-
wild type enzyme, at pH 7.5 and 25°C
0.39
-
mutant enzyme C448A, at pH 7.5 and 25°C
0.68
-
mutant enzyme K530R, at pH 7.5 and 25°C
1.2
-
mutant enzyme K530A, at pH 7.5 and 25°C
5.55
-
mutant enzyme R292E/L18H
0.92
-
wild-type, pH not specified in the publication, temperature not specified in the publication
1.17
-
mutant E243A, pH not specified in the publication, temperature not specified in the publication
0.0033
-
pH 7.0, 45°C, enzyme covalently immobilized on dextran
0.004
-
pH 7.0, 45°C, soluble enzyme
0.0043
-
pH 7.0, 45°C, PEGylated enzyme
0.98
-
pH 6.0, 37°C, recombinant enzyme
2.6
-
pH 6.0, 30°C, mutant enzyme M50V/A52C/P54D/T55S
4.12
-
pH 6.0, 37°C, recombinant wild-type enzyme
4.8
-
pH 6.0, 30°C, mutant enzyme S322A
5.43
-
pH 6.0, 37°C, recombinant mutant E583G
5.5
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322A
5.6
-
pH 6.0, 30°C, mutant enzyme G319W
6.8
-
pH 6.0, 30°C, mutant enzyme A52C/P54D
9.8
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D
10
-
pH 6.0, 30°C, mutant enzyme A52C
13
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P
16
-
pH 6.0, 30°C, mutant enzyme P54D
16
-
pH 6.0, 30°C, wild-type enzyme
19
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322T/I326L
21
-
pH 6.0, 30°C, mutant enzyme S322T/I326L
30
-
at pH 6.5, between 4°C and 10°C
146.4
-
pH 5.6, 45°C, recombinant His6-tagged wild-type enzyme
149.3
-
pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C
172.1
-
pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C/L7M/N8G
0.008
-
at pH 7.5 and 30°C
1.18
-
wild-type, pH 7.5, 37°C
1.85
-
pH 7.5, 37°C, recombinant enzyme
3.88
-
mutant M341L, pH 7.5, 37°C
6.33
-
mutant F344Y, pH 7.5, 37°C
143
-
mutant F344H, pH 7.5, 37°C
0.61
-
0.1 mM NAD+, in 100 mM HEPES (pH 8.0), at 30°C
4.17
-
pH 8.0, 30°C, recombinant mutant I222T/Y354W
0.0013
-
pH 8.5, 37°C, recombinant enzyme
0.16
-
pH 8.0, 30°C, recombinant mutant T224I/W355Y
0.32
-
pH 8.0, 30°C, recombinant mutant T224I
1.03
-
pH 8.0, 30°C, recombinant mutant W355Y
2.57
-
pH 9.0, 50°C, recombinant His-tagged mutant T391Y/S394Y
3.5
-
pH 8.0, 30°C, recombinant wild-type enzyme
5.1
-
in 50 mM Tris-HCl (pH 8.0), 2 mM cobalt chloride at 30°C
14.93
-
pH 8.0, 50°C, recombinant mutant S394Y
23.07
-
pH 9.0, 50°C, recombinant His-tagged mutant T391Y
31.25
-
pH 8.0, 50°C, recombinant mutant S394N
50.68
-
pH 8.0, 50°C, recombinant mutant S394C
55.43
-
pH 8.0, 50°C, recombinant wild-type enzyme
55.43
-
pH 9.0, 50°C, recombinant His-tagged wild-type enzyme
62.5
-
pH 8.0, 50°C, recombinant mutant S394T
84.9
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
109
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
0.00012
-
mutant enzyme H242A
0.00017
-
mutant enzyme W220L
0.00065
-
L-lysine lactam formation, pH 7.4, 37°C
0.00075
-
mutant enzyme W220A
0.0026
-
mutant enzyme Y269S
0.0046
-
mutant enzyme T31G
0.0087
-
pH 7.2, 37°C, mutant enzyme E240Q
0.0143
-
at 25°C, in 250 mM KCl, 100 mM HEPES, pH 7.5, 10 mM dithiothreitol, 10 mM MgCl2, 0.05 mg/ml bovine serum albumin
0.015
-
pH 7.2, 37°C, mutant enzyme E278Q
0.02
-
pH 7.2, 37°C, mutant enzyme E428D
0.031
-
pH 7.2, 37°C, mutant enzyme Y280F
0.086
-
pH 7.2, 37°C, mutant enzyme E240D
0.099
-
mutant enzyme Y269F
0.13
-
mutant enzyme W220Y
0.16
-
pH 7.2, 37°C, mutant enzyme E278D
0.29
-
mutant enzyme H242L
0.45
-
mutant enzyme G29A
0.53
-
mutant enzyme T31S
0.6
-
pH 7.2, 37°C, mutant enzyme F426W
0.65
-
pH 7.2, 37°C, mutant enzyme N424Q
1
-
pH 7.2, 37°C, mutant enzyme E428D
1.6
-
pH 7.2, 37°C, mutant enzyme N424D
1.6
-
pH 7.2, 37°C, mutant enzyme Y280S
1.8
-
pH 7.2, 37°C, wild-type enzyme
2.4
-
pH 7.2, 37°C, mutant enzyme F426H
3
6
aminoacylation reaction, recombinant mutant W332F, pH 8.0, 37°C
3.13
-
aminoacylation reaction, recombinant mutant W314F, pH 8.0, 37°C
3.13
-
aminoacylation reaction, recombinant wild-type enzyme, pH 8.0, 37°C
3.2
-
native enzyme, pH 8.0, 30°C
3.23
-
aminoacylation reaction, recombinant mutant W332F, pH 8.0, 37°C
3.3
-
aminoacylation reaction, recombinant mutant W314F/W332F, pH 8.0, 37°C
3.4
-
pH 7.2, 37°C, mutant enzyme G216A
3.53
-
aminoacylation reaction, recombinant wild-type enzyme, pH 8.0, 37°C
3.58
-
aminoacylation reaction, recombinant mutant W314F, pH 8.0, 37°C
3.6
-
recombinant enzyme without t7-tag
4.1
-
recombinant T7-tagged enzyme, pH 8.0, 30°C
5.1
-
recombinant N-terminally truncated enzyme, pH 7.5, 25°C
5.8
-
recombinant wild-type enzyme, pH 7.5, 25°C
8.2
-
mutant enzyme G469A, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C
41.7
-
wild type enzyme, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C
45.7
-
forward reaction, pH 8.0, 30°C
85
-
mutant enzyme A233S, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C
0.001
-
pH 8.6, 37°C, recombinant mutant D406A
0.283
-
pH 8.6, 37°C, recombinant mutant P408A
4.833
-
pH 8.6, 37°C, recombinant wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.043
-
mutant D238E, pH 7, 30°C
0.061
-
wild-type, pH 7, 30°C
0.072
-
mutant D238F, pH 7, 30°C
0.091
-
dehydrogenation with phenazine methosulfate
0.26
-
mutant D238A, pH 7, 30°C
2.4
-
pH 7.5, 25°C, with NADH
12
-
pH 7.5, 25°C, with NADPH
13
-
pH 7.5, 25°C, recombinant mutant K64A, with NADPH
40
-
pH 7.5, 25°C, recombinant mutant K64A, with NADH
0.01015
-
at pH 7.5 and 37°C
0.013
-
pH 7.4, 40°C, recombinant enzyme from Escherichia coli
0.013
-
pH 7.4, 40°C, recombinant enzyme from Streptomyces lividans
0.013
-
pH 7.4, 50°C, mature L-lysine oxidase
0.04
-
70 mM potassium phosphate buffer pH 8.0
0.18
-
at pH 7.5 and 70°C
0.28
-
pH 4.0, 50°C, L-lysine oxidase precursor prLysOX
0.28
-
pH 7.4, 40°C, mutant enzyme D315A
0.4
-
100 mM potassium phosphate buffer pH 7.4 and 500 mM semicarbazide
0.56
-
pH 7.4, 40°C, mutant enzyme D212A
7.6
-
pH 7.4, 40°C, mutant enzyme D212A/D315A
0.01
-
at pH 8.0 and 20°C, measured at the rate of H2O2 production
0.016
-
pH and temperature not specified in the publication
0.018
-
mutant D238E, pH 7, 30°C
0.027
-
wild-type, pH 7, 30°C
0.035
-
pH and temperature not specified in the publication
0.059
-
mutant D238F, pH 7, 30°C
0.16
-
37°C, isozymes MPLAO1 and MPLAO3
0.61
-
mutant D238A, pH 7, 30°C
3.39
-
at pH 7.0 and 30°C
13
-
pH 7, 37°C, EDTA-treated protein
64
-
pH 7.5, 0.9% NaCl, at 25°C
67.7
-
pH 7, 37°C, untreated protein
0.0018
-
in 15 mM potassium phosphate buffer (pH 7.0), at 25°C
0.0032
-
at pH 7.5 and 25°C
0.0039
-
wild type enzyme, at pH 7.5 and 25°C
0.048
-
mutant enzyme C448A, at pH 7.5 and 25°C
0.052
-
mutant enzyme K530A, at pH 7.5 and 25°C
0.113
-
mutant enzyme K530R, at pH 7.5 and 25°C
0.129
-
mutant enzyme Y211F, at pH 7.5 and 25°C
0.142
-
mutant enzyme C448D, at pH 7.5 and 25°C
1.4
-
GST-tagged enzyme, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
1.8
-
crude extract enzyme, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
1.8
-
recombinant enzyme, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
1.8
-
L-Arg, with pyruvate as cosubstrate
6.1
-
2-ketobutanoate, brain enzyme
0.62
-
mutant E78A, 25°C, pH 7.2
0.89
-
mutant enzyme C205S, at pH 7.0 and 25°C
0.89
-
wild type enzyme, in 100 mM HEPES, pH 7.0, at 25°C
1.1
-
wild type enzyme, at pH 7.0 and 25°C
1.1
-
wild-type, 25°C, pH 7.2
3
-
mutant enzyme C205V, at pH 7.0 and 25°C
4
-
mutant E78Q, 25°C, pH 7.2
11
-
mutant E122Q, 25°C, pH 7.2
25
-
mutant enzyme K77M, in 100 mM HEPES, pH 7.0, at 25°C
27.1
-
mutant E78Q/E122Q, 25°C, pH 7.2
36.5
-
mutant E122A, 25°C, pH 7.2
96
-
mutant enzyme K77M/H96Q, in 100 mM HEPES, pH 7.0, at 25°C
190.7
-
mutant E78A/E122A, 25°C, pH 7.2
267
-
mutant enzyme H96Q, in 100 mM HEPES, pH 7.0, at 25°C
0.4
-
enzyme from L3 larva, at pH 7.0, temperature not specified in the publication
0.5
-
enzyme from L3 larva, at pH 7.0, temperature not specified in the publication
0.7
-
enzyme from adult, at pH 7.0, temperature not specified in the publication
0.9
-
enzyme from adult, at pH 7.0, temperature not specified in the publication
6.3
-
in mitochondrial extracts
23
-
alpha-transamidinase
23.5
-
beta-transamidinase
2.9
-
pH 8.0, 37°C, recombinant wild-type enzyme
4.5
-
pH 8.0, 37°C, recombinant chimeric mutant
6.4
-
pH 8.0, 37°C, recombinant wild-type enzyme
6.5
-
pH 8.0, 37°C, recombinant wild-type enzyme
9.9
-
pH 8.0, 37°C, recombinant chimeric mutant
15.8
-
pH 8.0, 37°C, recombinant wild-type enzyme
105
-
mutant enzyme R292E/L18H
1.2
-
wild-type, pH not specified in the publication, temperature not specified in the publication
1.7
-
mutant E243A, pH not specified in the publication, temperature not specified in the publication
12.34
-
pH 7.0, 45°C, soluble enzyme
15.48
-
pH 7.0, 45°C, enzyme covalently immobilized on dextran
18.42
-
pH 7.0, 45°C, PEGylated enzyme
0.0192
-
recombinant His-tagged enzyme, pH 8.0, 37°C
0.42
-
at pH 6.5, between 4°C and 10°C
0.92
-
recombinant enzyme, pH 7.5, 37°C
1.22
-
pH 5.6, 45°C, recombinant His6-tagged wild-type enzyme
1.33
-
pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C
1.47
-
pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C/L7M/N8G
1.5
-
pH 6.0, 30°C, wild-type enzyme
1.9
-
pH 6.0, 30°C, mutant enzyme A52C
2.4
-
pH 6.0, 30°C, mutant enzyme A52C/P54D
3
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P
3.23
-
pH 6.0, 37°C, recombinant mutant E583G
3.6
-
pH 6.0, 30°C, mutant enzyme M50V/A52C/P54D/T55S
4
-
pH 6.0, 30°C, mutant enzyme G319W
4.93
-
pH 6.0, 37°C, recombinant wild-type enzyme
5.7
-
pH 6.0, 30°C, mutant enzyme P54D
6.7
-
pH 6.0, 30°C, mutant enzyme S322A
7.7
-
pH 6.0, 37°C, recombinant enzyme
8
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D
17
-
pH 6.0, 30°C, mutant enzyme S322T/I326L
22
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322T/I326L
270
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322A
0.878
-
pH 7.5, 37°C, recombinant enzyme
2.37
-
wild-type, pH 7.5, 37°C
2.49
-
mutant M341L, pH 7.5, 37°C
5.26
-
mutant F344Y, pH 7.5, 37°C
97.8
-
mutant F344H, pH 7.5, 37°C
0.046
-
0.1 mM NAD+, in 100 mM HEPES (pH 8.0), at 30°C
1.39
-
in 100 mM potassium phosphate buffer, pH 8.0 containing 10% (v/v) glycerol, at 37°C
32
-
pH 8.0, 30°C, recombinant mutant I222T/Y354W
27.9
-
pH 8.5, 37°C, recombinant enzyme
2
3
pH 8.0, 30°C, recombinant mutant W355Y
2
6
pH 8.0, 50°C, recombinant mutant S394C
2
6
pH 8.0, 50°C, recombinant mutant S394N
11
-
pH 8.0, 30°C, recombinant wild-type enzyme
15
-
pH 8.0, 30°C, recombinant mutant T224I
16.21
-
in 50 mM Tris-HCl (pH 8.0), 2 mM cobalt chloride at 30°C
21.8
-
pH 8.0, 50°C, recombinant wild-type enzyme
21.8
-
pH 9.0, 50°C, recombinant His-tagged wild-type enzyme
25.2
-
pH 8.0, 50°C, recombinant mutant S394T
26.5
-
pH 8.0, 50°C, recombinant mutant S394Y
27
-
pH 8.0, 30°C, recombinant mutant T224I/W355Y
34.3
-
pH 9.0, 50°C, recombinant His-tagged mutant T391Y/S394Y
37.6
-
pH 9.0, 50°C, recombinant His-tagged mutant T391Y
1.8
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
2.4
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
0.0013
-
pH 7.2, 37°C, mutant enzyme E428Q
0.0014
-
pH 7.2, 37°C, mutant enzyme E278Q
0.0026
-
pH 7.2, 37°C, wild-type enzyme
0.0033
-
pH 7.2, 37°C, mutant enzyme E240D
0.0036
-
pH 7.2, 37°C, mutant enzyme E240Q
0.0037
-
lysylation, 18S synthetase complex
0.0047
-
lysylation, free enzyme
0.005
-
aminoacylation, enzyme form EII
0.005
-
ATP, , lysylation, free enzyme
0.0052
-
pH 7.2, 37°C, mutant enzyme N424D
0.006
-
aminoacylation, enzyme form EI
0.0066
-
at 25°C, in 250 mM KCl, 100 mM HEPES, pH 7.5, 10 mM dithiothreitol, 10 mM MgCl2, 0.05 mg/ml bovine serum albumin
0.009
-
ATP-diphosphate exchange reaction, recombinant wild-type enzyme and mutant W314F/W332F, pH 8.0, 37°C
0.01
-
ATP-diphosphate exchange reaction, recombinant mutant W314F, pH 8.0, 37°C
0.016
-
aminoacylation reaction, recombinant wild-type enzyme, pH 8.0, 37°C
0.016
-
native enzyme, pH 8.0, 30°C
0.016
-
pH 7.2, 37°C, mutant enzyme F426W
0.017
-
aminoacylation reaction, recombinant mutants W314F and W314F/W332F, pH 8.0, 37°C
0.018
-
ATP-diphosphate exchange reaction, recombinant mutant W332F, pH 8.0, 37°C
0.022
-
aminoacylation reaction, recombinant mutant W332F, pH 8.0, 37°C
0.022
-
pH 7.2, 37°C, mutant enzyme E428D
0.023
-
recombinant T7-tagged enzyme, pH 8.0, 30°C
0.0236
-
ATP-diphosphate exchange
0.024
-
pH 7.2, 37°C, mutant enzyme Y280F
0.024
-
recombinant enzyme without t7-tag
0.052
-
pH 7.2, 37°C, mutant enzyme N424Q
0.092
-
recombinant wild-type enzyme, pH 7.5, 25°C
0.104
-
recombinant N-terminally truncated enzyme, pH 7.5, 25°C
0.114
-
pH 7.2, 37°C, mutant enzyme Y280S
0.16
-
wild type enzyme, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C
0.18
-
mutant enzyme H242L
0.196
-
pH 7.2, 37°C, mutant enzyme G216A
0.2
1
mutant enzyme A233S, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C
0.203
-
pH 7.2, 37°C, mutant enzyme F426H
0.254
-
pH 7.2, 37°C, mutant enzyme E278D
0.33
-
mutant enzyme W220A
0.4
-
mutant enzyme Y269F
0.76
-
mutant enzyme T31S
2.8
-
mutant enzyme Y269S
3.3
-
mutant enzyme H242A
3.3
-
mutant enzyme W220L
3.9
-
mutant enzyme G469A, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C
4.7
-
mutant enzyme W220Y
8.1
-
ATP-diphosphate exchange reaction, recombinant mutant Y271F, pH 8.0, 37°C
0.37
-
in presence of 30 mM K2HPO4
0.42
-
in presence of 2 mM K2HPO4
0.44
-
in presence of 60 mM KCl
0.49
-
in presence of 60 mM KCl
0.55
-
pH 8.6, 37°C, recombinant wild-type enzyme
2.8
-
pH 8.6, 37°C, recombinant mutant D406A
3.1
-
pH 8.6, 37°C, recombinant mutant P408A
20
-
above, pH 8.6, 37°C, recombinant mutant A409R
20
-
above, pH.6, 37°C, recombinant mutant E460A
0.629
-
pH 7.8, 60°C, wild-type enzyme
1.01
-
pH 7.8, 60°C, mutant enzyme R205A
1.04
-
pH 7.8, 60°C, mutant enzyme H133A
1.15
-
pH 7.8, 60°C, mutant enzyme R174A
1.3
-
pH 7.8, 60°C, mutant enzyme E106A
1.37
-
pH 7.8, 60°C, mutant enzyme E140A
3.05
-
pH 7.8, 60°C, mutant enzyme Y114A
0.00736
-
pH 4.5, 30°C, recombinant enzyme
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Show all BRENDA pathways known for L-lysine
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