Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
2-aminomuconate semialdehyde + CO2
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
-
-
-
?
additional information
?
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
key enzyme in the regulation of the tryptophan-nicotinamide adenine dinucleotide pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
key enzyme in the regulation of the tryptophan-nicotinamide adenine dinucleotide pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
key enzyme in the regulation of the tryptophan-nicotinamide adenine dinucleotide pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
key enzyme in the regulation of the tryptophan-nicotinamide adenine dinucleotide pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
key enzyme in the regulation of the tryptophan-nicotinamide adenine dinucleotide pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
2-nitrobenzoate degradation pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
2-nitrobenzoate degradation pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
important enzyme regulating tryptophan-niacin metabolism
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
important enzyme regulating tryptophan-niacin metabolism
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
-
enzyme is involved in the metabolism of the benzene ring
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
-
suppression of the enzyme activity by linoleic acid in relation to its induction by glucocorticoids and dietary protein
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
-
expression level of EC 4.1.1.45 might by modulated by linoleic acid or its metabolites
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
-
effect of dietary protein and soybean oil which contains about 85% unsaturated fatty acids
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
-
directly related to the concentration of blood muconate
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
-
key enzyme of niacin synthesis from Trp
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
-
effect of various dietary fatty acids on enzyme activity
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
-
40% casein diet, nicotinic acid-free, significantly reduces enzyme activity
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
-
key enzyme of niacin synthesis from Trp
-
-
?
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
-
-
-
?
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
-
-
-
?
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
-
-
-
?
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
the decarboxylation occurs first to generate an unstable alpha-aminomuconate-epsilon-semialdehyde intermediate, which then undergoes a relatively slow release from the enzyme and a much slower cyclization to yield the final product
-
-
?
additional information
?
-
-
plays a key role in tryptophan catabolism, the enzyme regulates NAD biosynthesis from the amino acid, directly affecting quinolinate and picolinate formation
-
-
?
additional information
?
-
-
key enzyme in NAD biosynthesis from tryptophan
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
additional information
?
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
key enzyme in the regulation of the tryptophan-nicotinamide adenine dinucleotide pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
key enzyme in the regulation of the tryptophan-nicotinamide adenine dinucleotide pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
key enzyme in the regulation of the tryptophan-nicotinamide adenine dinucleotide pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
key enzyme in the regulation of the tryptophan-nicotinamide adenine dinucleotide pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
-
key enzyme in the regulation of the tryptophan-nicotinamide adenine dinucleotide pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
2-nitrobenzoate degradation pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
2-nitrobenzoate degradation pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
important enzyme regulating tryptophan-niacin metabolism
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
important enzyme regulating tryptophan-niacin metabolism
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
-
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
-
enzyme is involved in the metabolism of the benzene ring
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
-
suppression of the enzyme activity by linoleic acid in relation to its induction by glucocorticoids and dietary protein
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
-
expression level of EC 4.1.1.45 might by modulated by linoleic acid or its metabolites
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
-
effect of dietary protein and soybean oil which contains about 85% unsaturated fatty acids
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
-
directly related to the concentration of blood muconate
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
-
key enzyme of niacin synthesis from Trp
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
-
effect of various dietary fatty acids on enzyme activity
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
-
40% casein diet, nicotinic acid-free, significantly reduces enzyme activity
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
-
key enzyme of niacin synthesis from Trp
-
-
?
additional information
?
-
-
plays a key role in tryptophan catabolism, the enzyme regulates NAD biosynthesis from the amino acid, directly affecting quinolinate and picolinate formation
-
-
?
additional information
?
-
-
key enzyme in NAD biosynthesis from tryptophan
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,3-dihydroxyacetonephosphate
-
2-hydroxymuconate 6-semialdehyde
-
-
3-[[[5-cyano-1,6-dihydro-6-oxo-4-(2-thienyl)-2-pyrimidinyl]thio]methyl]phenylacetic acid
potent and selective inhibitor. Treatment of primary hepatocytes significantly increases intracellular NAD+ levels. compound exhibits good solubility with low permeability of cells and no inhibition of cytochrome P450s
Cd2+
-
0.5 mM, reduces the enzymatic activity to 25%
Cr3+
-
0.5 mM, reduces the enzymatic activity to 35%
eicosapentaenoic acid
-
ACMSD mRNA levels in primary hepatocytes are decreased by the incubation with high concentrations of eicosapentaenoic acid
Fe3+
-
0.1 mM, reduces the enzymatic activity to 15%
Kynurenic acid
-
1 mM, 59% residual activity
linoleic acid
-
ACMSD mRNA levels in primary hepatocytes are decreased by the incubation with high concentrations of linoleic acid
mono (2-ethyl hexyl) phthalate
-
90% inhibition of ACMSD activity in the presence of 3 mmol/l mono (2-ethyl hexyl) phthalate, inhibition is reversible
mono (2-ethylhexyl) phthalate
p-chloromercuribenzoic acid
-
-
peroxisome proliferator-activated receptor alpha
-
gene expression is downregulated by activation of peroxisome proliferator-activated receptor alpha
-
Picolinic acid
-
1 mM, 47% residual activity
pyridine-2,6-dicarboxylic acid
-
competitive
quinolinic acid
-
1 mM, 61% residual activity
WY-14,643
-
ACMSD mRNA levels in primary hepatocytes are decreased by the incubation with high concentrations of WY-14,643
Zn2+
-
0.1 mM, reduces the enzymatic activity to 6%
[4-chloro-6-(2,3-xylidino)-2-pyrimidinylthio]acetic acid
-
suppresses ACMSD activity
mono (2-ethylhexyl) phthalate
-
92% inhibition of ACMSD activity in the presence of 3 mmol/l mono (2-ethyl hexyl) phthalate, inhibition is reversible
mono (2-ethylhexyl) phthalate
-
93% inhibition of ACMSD activity in the presence of 3 mmol/l mono (2-ethyl hexyl) phthalate
mono-n-butyl phthalate
-
18% inhibition of ACMSD activity in the presence of 3 mmol/l mono-n-butyl phthalate
mono-n-butyl phthalate
-
15% inhibition of ACMSD activity in the presence of 3 mmol/l mono-n-butyl phthalate
mono-n-butyl phthalate
-
20% inhibition of ACMSD activity in the presence of 3 mmol/l mono-n-butyl phthalate
mono-n-hexyl phthalate
-
84% inhibition of ACMSD activity in the presence of 3 mmol/l mono-n-hexyl phthalate
mono-n-hexyl phthalate
-
64% inhibition of ACMSD activity in the presence of 3 mmol/l mono-n-hexyl phthalate
mono-n-hexyl phthalate
-
60% inhibition of ACMSD activity in the presence of 3 mmol/l mono-n-hexyl phthalate
p-chloromercuribenzoate
-
p-chloromercuribenzoate
-
p-chloromercuribenzoate
-
p-chloromercuribenzoate
-
-
PCMB
-
inhibition is prevented by either reduced glutathione or caseine
additional information
-
not inhibited by monoethyl phthalate
-
additional information
not inhibitory: EDTA, 1,10-phenanthroline or 8-hydroxyquinoline-5-sulfonic acid
-
additional information
-
not inhibited by monoethyl phthalate
-
additional information
-
not inhibited by monoethyl phthalate
-
additional information
-
MK886 does not influence the suppressive effects of polyunsaturated fatty acids on ACMSD activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.001 - 0.0161
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
0.0065 - 0.0672
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
0.013 - 0.014
2-amino-3-carboxymuconate-6-semialdehyde
0.0033
2-aminomuconate semialdehyde
Cu-substituted enzyme, pH 7.0, temperature not specified in the publication
0.0049 - 0.0921
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde
0.001
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
-
-
0.0096
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
-
wild type enzyme, at pH 7.0 and 37°C
0.0161
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
-
-
0.0065
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
in 50 mM 4-morpholinepropanesulfonic acid, pH 6.0, at 25°C
0.0075
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
mutant enzyme H228A, in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22°C
0.0096
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
in 25 mM HEPES buffer pH 7.0, the enzyme contains Zn2+
0.0123
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
mutant enzyme H177A, in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22°C
0.0167
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
wild type enzyme, in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22°C
0.0232
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
in 25 mM HEPES buffer pH 7.0, the enzyme contains Co2+
0.0241
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
mutant enzyme H9E, in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22°C
0.0662
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
mutant enzyme H228E, in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22°C
0.0672
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
mutant enzyme D294E, in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22°C
0.013
2-amino-3-carboxymuconate-6-semialdehyde
pH 6.0, 25°C, kidney enzyme
0.014
2-amino-3-carboxymuconate-6-semialdehyde
pH 6.0, 25°C, liver enzyme
0.0049
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde
-
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase loaded with 1 molar equivalent Cd2+
0.0067
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde
-
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase loaded with 1 molar equivalent Mn2+
0.0232
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde
-
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase loaded with 1 molar equivalent Co2+
0.0921
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde
-
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase loaded with 1 molar equivalent Fe2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6.5
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
-
wild type enzyme, at pH 7.0 and 22°C
0.019 - 7.3
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
0.1 - 4.8
2-aminomuconate semialdehyde
1.4 - 10.2
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde
0.019
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
mutant enzyme H228E, in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22°C
0.025
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
mutant enzyme H9E, in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22°C
0.08
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
mutant enzyme D294E, in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22°C
0.11
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
mutant enzyme H228A, in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22°C
0.28
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
mutant enzyme H177A, in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22°C
1
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
in 50 mM 4-morpholinepropanesulfonic acid, pH 6.0, at 25°C
6.5
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
in 25 mM HEPES buffer pH 7.0, the enzyme contains Zn2+
6.65
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
wild type enzyme, in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22°C
7.3
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
in 25 mM HEPES buffer pH 7.0, the enzyme contains Co2+
0.1
2-aminomuconate semialdehyde
Cu-substituted enzyme, pH 7.0, temperature not specified in the publication
4.8
2-aminomuconate semialdehyde
enzyme with 64.4% zinc ion occupancy, pH 7.0, temperature not specified in the publication
1.4
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde
-
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase loaded with 1 molar equivalent Mn2+
1.7
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde
-
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase loaded with 1 molar equivalent Cd2+
7.3
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde
-
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase loaded with 1 molar equivalent Co2+
10.2
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde
-
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase?loaded with 1 molar equivalent Fe2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Shibata, K.
Tryptophan-niacin metabolism in alloxan diabetic rats and partial prevention of alloxan diabetes by nicotinamide
Agric. Biol. Chem.
51
811-816
1987
Rattus norvegicus
-
brenda
Shibata, K.; Hayakawa, T.; Iwai, K.
Comparison of the enzyme activities in the tryptophan-NAD pathway between the Wistar and Sprague Dawley strains of rats
Agric. Biol. Chem.
50
1643-1644
1986
Rattus norvegicus
-
brenda
Shibata, K.; Murata, K.
Comparison of the activity of the tryptophan-NAD pathway between rats fed a fat-free diet and a fat diet
Agric. Biol. Chem.
49
2899-2904
1985
Rattus norvegicus
-
brenda
Nishizuka, Y.; Ichiyama, A.; Hayaishi, O.
II. Picolinic carboxylase (cat liver) (alpha-amino-beta-carboxymuconic-epsilon-semialdehyde beta-decarboxylase)
Methods Enzymol.
17A
471-476
1970
Felis catus
-
brenda
Ichiyama, A.; Nakamura, S.; Kawai, H.; Honjo, T.; Nishizuka, Y.; Hayaishi, O.; Senoh, S.
Studies on the metabolism of the benzene ring of tryptophan in mammalian tissues II. Enzymic formation of alpha-aminomuconic acid from 3-hydroxyanthranilic acid
J. Biol. Chem.
240
740-749
1965
Felis catus
brenda
Egashira, Y.; Tanabe, A.; Ohta, T.; Sanada, H.
Dietary linoleic acid alters alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD), a key enzyme of niacin synthesis from tryptophan, in the process of protein expression in rat liver
J. Nutr. Sci. Vitaminol.
44
129-136
1998
Rattus norvegicus
brenda
Egashira, Y.; Kouhashi, H.; Ohta, T.; Sanada, H.
Purification and properties of alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD), key enzyme of niacin synthesis from tryptophan, from hog kidney
J. Nutr. Sci. Vitaminol.
42
173-183
1996
Sus scrofa
brenda
Sanada, H.; Takahashi, T.; Miyazaki, M.
Effects of dietary fat and protein on the activity of alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase and the urinary excretion of niacin metabolites in rats
J. Nutr. Sci. Vitaminol.
37
39-51
1991
Rattus norvegicus
brenda
Egashira, Y.; Ogawara, R.; Ohta, T.; Sanada, H.
Suppression of rat hepatic alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD) activity by linoleic acid in relation to its induction by glucocorticoids and dietary protein
Biosci. Biotechnol. Biochem.
58
339-343
1994
Rattus norvegicus
-
brenda
Egashira, Y.; Yamamiya, Y.; Sanada, H.
Effects of various dietary fatty acids on alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase activity in rat liver
Biosci. Biotechnol. Biochem.
56
2015-2019
1992
Rattus norvegicus
-
brenda
Fukuoka, S.; Tanabe, A.; Egashira, Y.; Sanada, H.; Shin, M.; Shibata, K.
Identification of cDNAs encoding alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSDase)
Adv. Exp. Med. Biol.
467
615-618
1999
Caenorhabditis elegans, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
brenda
Muraki, T.; Taki, M.; Hasegawa, Y.; Iwaki, H.; Lau, P.C.
Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7
Appl. Environ. Microbiol.
69
1564-1572
2003
Pseudomonas fluorescens (Q83V25), Pseudomonas fluorescens, Pseudomonas fluorescens KU-7 (Q83V25)
brenda
Tanabe, A.; Egashira, Y.; Fukuoka, S.; Shibata, K.; Sanada, H.
Purification and molecular cloning of rat 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
Biochem. J.
361
567-575
2002
Rattus norvegicus (Q8R5M5), Rattus norvegicus Wistar (Q8R5M5)
brenda
Fukuoka, S.; Ishiguro, K.; Yanagihara, K.; Tanabe, A.; Egashira, Y.; Sanada, H.; Shibata, K.
Identification and expression of a cDNA encoding human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD). A key enzyme for the tryptophan-niacine pathway and "quinolinate hypothesis"
J. Biol. Chem.
277
35162-35167
2002
Sus scrofa, Mus musculus (Q8R519), Rattus norvegicus (Q8R5M5), Homo sapiens (Q8TDX5), Homo sapiens, Mus musculus ICR (Q8R519)
brenda
Egashira, Y.; Murotani, G.; Tanabe, A.; Saito, K.; Uehara, K.; Morise, A.; Sato, M.; Sanada, H.
Differential effects of dietary fatty acids on rat liver alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase activity and gene expression
Biochim. Biophys. Acta
1686
118-124
2004
Rattus norvegicus
brenda
Li, T.; Walker, A.L.; Iwaki, H.; Hasegawa, Y.; Liu, A.
Kinetic and spectroscopic characterization of ACMSD from Pseudomonas fluorescens reveals a pentacoordinate mononuclear metallocofactor
J. Am. Chem. Soc.
127
12282-12290
2005
Pseudomonas fluorescens
brenda
Fukuwatari, T.; Ohsaki, S.; Fukuoka, S.; Sasaki, R.; Shibata, K.
Phthalate esters enhance quinolinate production by inhibiting alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD), a key enzyme of the tryptophan pathway
Toxicol. Sci.
81
302-308
2004
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Liu, A.; Zhang, H.
Transition metal-catalyzed nonoxidative decarboxylation reactions
Biochemistry
45
10407-10411
2006
Pseudomonas fluorescens
brenda
Martynowski, D.; Eyobo, Y.; Li, T.; Yang, K.; Liu, A.; Zhang, H.
Crystal structure of alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase: insight into the active site and catalytic mechanism of a novel decarboxylation reaction
Biochemistry
45
10412-10421
2006
Pseudomonas fluorescens
brenda
Li, T.; Iwaki, H.; Fu, R.; Hasegawa, Y.; Zhang, H.; Liu, A.
Alpha-amino-beta-carboxymuconic-epsilon-semialdehyde decarboxylase (ACMSD) is a new member of the amidohydrolase superfamily
Biochemistry
45
6628-6634
2006
Pseudomonas fluorescens
brenda
Pucci, L.; Perozzi, S.; Cimadamore, F.; Orsomando, G.; Raffaelli, N.
Tissue expression and biochemical characterization of human 2-amino 3-carboxymuconate 6-semialdehyde decarboxylase, a key enzyme in tryptophan catabolism
FEBS J.
274
827-840
2007
Homo sapiens
brenda
Li, T.; Ma, J.K.; Hosler, J.P.; Davidson, V.L.; Liu, A.
Detection of transient intermediates in the metal-dependent nonoxidative decarboxylation catalyzed by alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase
J. Am. Chem. Soc.
129
9278-9279
2007
Pseudomonas fluorescens
brenda
Shin, M.; Kim, I.; Inoue, Y.; Kimura, S.; Gonzalez, F.J.
Regulation of mouse hepatic alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase, a key enzyme in the tryptophan-nicotinamide adenine dinucleotide pathway, by hepatocyte nuclear factor 4alpha and peroxisome proliferator-activated receptor alpha
Mol. Pharmacol.
70
1281-1290
2006
Mus musculus
brenda
Gaetjens, J.; Mullins, C.S.; Kampf, J.W.; Thuery, P.; Pecoraro, V.L.
Corroborative cobalt and zinc model compounds of alpha-amino-beta-carboxymuconic-epsilon-semialdehyde decarboxylase (ACMSD)
Dalton Trans.
2009
51-62
2009
Pseudomonas fluorescens
brenda
Sasaki, N.; Egashira, Y.; Sanada, H.
Down-regulation of alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase by polyunsaturated fatty acids in hepatocytes is not mediated by PPARalpha
Eur. J. Nutr.
47
80-86
2008
Rattus norvegicus
brenda
Sasaki, N.; Egashira, Y.; Sanada, H.
Production of L-tryptophan-derived catabolites in hepatocytes from streptozotocin-induced diabetic rats
Eur. J. Nutr.
48
145-153
2009
Rattus norvegicus
brenda
Garavaglia, S.; Perozzi, S.; Galeazzi, L.; Raffaelli, N.; Rizzi, M.
The crystal structure of human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase in complex with 1,3-dihydroxyacetonephosphate suggests a regulatory link between NAD synthesis and glycolysis
FEBS J.
276
6615-6623
2009
Homo sapiens (Q8TDX5), Homo sapiens
brenda
Huo, L.; Fielding, A.J.; Chen, Y.; Li, T.; Iwaki, H.; Hosler, J.P.; Chen, L.; Hasegawa, Y.; Que, L.; Liu, A.
Evidence for a dual role of an active site histidine in alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase
Biochemistry
51
5811-5821
2012
Pseudomonas fluorescens (Q83V25), Pseudomonas fluorescens
brenda
Matsuda, H.; Gomi, R.T.; Hirai, S.; Egashira, Y.
Effect of dietary phytol on the expression of alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase, a key enzyme of tryptophan-niacin metabolism, in rats
Biosci. Biotechnol. Biochem.
77
1416-1419
2013
Rattus norvegicus
brenda
Matsuda, H.; Sato, M.; Yakushiji, M.; Koshiguchi, M.; Hirai, S.; Egashira, Y.
Regulation of rat hepatic alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase, a key enzyme in the tryptophan-NAD pathway, by dietary cholesterol and sterol regulatory element-binding protein-2
Eur. J. Nutr.
53
469-477
2014
Rattus norvegicus (Q8R5M5)
brenda
Huo, L.; Davis, I.; Chen, L.; Liu, A.
The power of two: arginine 51 and arginine 239* from a neighboring subunit are essential for catalysis in alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase
J. Biol. Chem.
288
30862-30871
2013
Pseudomonas fluorescens
brenda
Pellicciari, R.; Liscio, P.; Giacche, N.; De Franco, F.; Carotti, A.; Robertson, J.; Cialabrini, L.; Katsyuba, E.; Raffaelli, N.; Auwerx, J.
alpha-Amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD) inhibitors as novel modulators of de novo nicotinamide adenine dinucleotide (NAD+) biosynthesis
J. Med. Chem.
61
745-759
2018
Homo sapiens (Q8TDX5)
brenda
Huo, L.; Liu, F.; Iwaki, H.; Li, T.; Hasegawa, Y.; Liu, A.
Human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD) a structural and mechanistic unveiling
Proteins
83
178-187
2015
Homo sapiens (Q8TDX5)
brenda
Brundin, L.; Sellgren, C.; Lim, C.; Grit, J.; Palsson, E.; Landen, M.; Samuelsson, M.; Lundgren, K.; Brundin, P.; Fuchs, D.; Postolache, T.; Traskman-Bendz, L.; Guillemin, G.; Erhardt, S.
An enzyme in the kynurenine pathway that governs vulnerability to suicidal behavior by regulating excitotoxicity and neuroinflammation
Transl. Psychiatry
6
e865
2016
Homo sapiens (Q8TDX5), Homo sapiens
brenda