Information on EC 4.1.1.45 - Aminocarboxymuconate-semialdehyde decarboxylase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
4.1.1.45
-
RECOMMENDED NAME
GeneOntology No.
Aminocarboxymuconate-semialdehyde decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate = 2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate = 2-aminomuconate semialdehyde + CO2
show the reaction diagram
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
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
decarboxylation
-
-
PATHWAY
KEGG Link
MetaCyc Link
2-amino-3-carboxymuconate semialdehyde degradation to 2-oxopentenoate
-
2-amino-3-carboxymuconate semialdehyde degradation to glutaryl-CoA
-
2-nitrobenzoate degradation I
-
Metabolic pathways
-
Tryptophan metabolism
-
SYSTEMATIC NAME
IUBMB Comments
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate carboxy-lyase (2-aminomuconate-semialdehyde-forming)
Product rearranges non-enzymically to picolinate.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-amino 3-carboxymuconate 6-semialdehyde decarboxylase
-
-
2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
Q83V25
-
2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
Pseudomonas fluorescens KU-7
Q83V25
-
-
2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
-
-
3-(3-oxoprop-2-enyl)-2-aminobut-2-endioate carboxy-lyase
-
-
-
-
ACMS decarboxylase
-
-
ACMSD
-
-
-
-
ACMSD
-
-
ACMSD
Q8TDX5
-
ACMSD
Q8R519
-
ACMSD
Mus musculus ICR
Q8R519
-
-
ACMSD
-
member of the metal-dependent amidohydrolase superfamily of the (beta/alpha)8 TIM barrel fold
ACMSD
Q8R5M5
-
ACMSD
-
-
ACMSD I
-
enzymatically active form
alpha-amino beta-carboxymuconate epsilon-semialdehyde decarboxylase
-
-
alpha-Amino-beta-carboxymuconate-epsilon-semialdehade decarboxylase
-
-
-
-
alpha-Amino-beta-carboxymuconate-epsilon-semialdehyde beta-decarboxylase
-
-
-
-
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase
-
-
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase
-
-
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase
Q8TDX5
-
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase
-
-
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase
-
-
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase
-
-
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase
-
-
alpha-amino-beta-carboxymuconic-epsilon-semialdehyde decarboxylase
-
-
Amino-carboxymuconate-semialdehyde decarboxylase
-
-
-
-
Decarboxylase, aminocarboxymuconate semialdehyde
-
-
-
-
hACMSD
Q8TDX5
-
NbaD enzyme
Q83V25
-
NbaD enzyme
Pseudomonas fluorescens KU-7
Q83V25
-
-
Picolinic acid carboxylase
-
-
-
-
Picolinic acid decarboxylase
-
-
-
-
Picolinic decarboxylase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37289-47-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
human
-
-
Manually annotated by BRENDA team
human
SwissProt
Manually annotated by BRENDA team
mouse
-
-
Manually annotated by BRENDA team
mouse, ICR strain
SwissProt
Manually annotated by BRENDA team
Mus musculus ICR
mouse, ICR strain
SwissProt
Manually annotated by BRENDA team
strain KU-7
SwissProt
Manually annotated by BRENDA team
Pseudomonas fluorescens KU-7
strain KU-7
SwissProt
Manually annotated by BRENDA team
rat, Wistar; Wistar strain
SwissProt
Manually annotated by BRENDA team
Wistar rat
-
-
Manually annotated by BRENDA team
Wistar strain and Sprague Dawley strain
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
Wistar strain
SwissProt
Manually annotated by BRENDA team
hog
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
Q8R5M5
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
-
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
-
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
Q8R519
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
Q8R5M5
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
-, Q83V25
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
-, Q8TDX5
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
-, Q8TDX5
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
-, Q83V25
2-nitrobenzoate degradation pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
Q8R5M5
important enzyme regulating tryptophan-niacin metabolism
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
-
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
Q8R519
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
Q8R5M5
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
-, Q8TDX5
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
Pseudomonas fluorescens KU-7
Q83V25
-, 2-nitrobenzoate degradation pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
Mus musculus ICR
Q8R519
-, tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
directly related to the concentration of blood muconate
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
show the reaction diagram
-
key enzyme of niacin synthesis from Trp
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
show the reaction diagram
-
key enzyme of niacin synthesis from Trp
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
show the reaction diagram
-
enzyme is involved in the metabolism of the benzene ring
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
show the reaction diagram
-
effect of various dietary fatty acids on enzyme activity
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
show the reaction diagram
-
40% casein diet, nicotinic acid-free, significantly reduces enzyme activity
-
-
-
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
-
-
-
-
?
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
-
-
-
-
?
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
-
-
-
-
?
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
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
show the reaction diagram
-, Q8TDX5
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
-, Q83V25
2-nitrobenzoate degradation pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
Q8R5M5
important enzyme regulating tryptophan-niacin metabolism
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
-
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
Q8R519
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
Q8R5M5
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
-, Q8TDX5
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
directly related to the concentration of blood muconate
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
show the reaction diagram
-
key enzyme of niacin synthesis from Trp
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
show the reaction diagram
-
key enzyme of niacin synthesis from Trp
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
show the reaction diagram
-
enzyme is involved in the metabolism of the benzene ring
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
show the reaction diagram
-
effect of various dietary fatty acids on enzyme activity
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
show the reaction diagram
-
40% casein diet, nicotinic acid-free, significantly reduces enzyme activity
-
-
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
Pseudomonas fluorescens KU-7
Q83V25
2-nitrobenzoate degradation pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
Mus musculus ICR
Q8R519
tryptophan-niacine pathway
-
?
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cd2+
-
activates
Cd2+
-
requires transition metal divalent cations for substrate activation
Co2+
-
activates
Co2+
-
requires transition metal divalent cations for substrate activation
Co2+
-
1.0 mM, increases activity to 130%
Co2+
-
after purification, Co2+-reconstituted ACMSD exhibits the highest activity and the greatest stability
Co2+
-
Co-substituted ACMSD shows a comparable activity to the native enzyme
Fe2+
-
activates
Fe2+
-
requires transition metal divalent cations for substrate activation
Fe2+
-
0.1 mM, increases activity to 124%
MgCl2
-
slightly stimulates
Mn2+
-
activates
Mn2+
-
requires transition metal divalent cations for substrate activation
Zn2+
-
requires transition metal divalent cations for substrate activation
Zn2+
-
native active site metal
Zn2+
-
essential cofactor
Zn2+
-, Q8TDX5
-
additional information
-
Fe3+, Cu2+ not activating
additional information
-
not influenced by 1 mM Mg2+, Mn2+, Ni2+ or Ca2+; the pure enzyme is 100% active in the absence of any metal ion
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,3-dihydroxyacetonephosphate
-, Q8TDX5
-
2-hydroxymuconate 6-semialdehyde
-
-
Cd2+
-
0.5 mM, reduces the enzymatic activity to 25%
Cr3+
-
0.5 mM, reduces the enzymatic activity to 35%
diethyldicarbonate
-
-
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%
-
iodoacetamide
-
-
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
-
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
N-Acetylimidazole
-
-
p-chloromercuribenzoate
Q8TDX5
-
p-chloromercuribenzoate
Q8R519
-
p-chloromercuribenzoate
Q8R5M5
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoic acid
-
-
PCMB
-
inhibition is prevented by either reduced glutathione or caseine
peroxisome proliferator-activated receptor alpha
-
gene expression is downregulated by activation of peroxisome proliferator-activated receptor alpha
-
Picolinic acid
-
1 mM, 47% residual activity
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
Monoiodoacetic acid
-
-
additional information
-
not inhibited by monoethyl phthalate
-
additional information
-
MK886 does not influence the suppressive effects of polyunsaturated fatty acids on ACMSD activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
hepatocyte nuclear factor 4alpha
-
gene expression is activated by hepatocyte nuclear factor 4alpha
-
additional information
-
hepatic ACMSD activity is increased in streptozotocin-induced diabetic rats
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.001
-
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
-
-
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 25C
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 22C
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 22C
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 22C
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 22C
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 22C
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 22C
0.013
-
2-amino-3-carboxymuconate-6-semialdehyde
Q8R5M5
pH 6.0, 25C, kidney enzyme
0.014
-
2-amino-3-carboxymuconate-6-semialdehyde
Q8R5M5
pH 6.0, 25C, 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+
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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 22C
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 22C
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 22C
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 22C
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 22C
1
-
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
in 50 mM 4-morpholinepropanesulfonic acid, pH 6.0, at 25C
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 22C
7.3
-
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
in 25 mM HEPES buffer pH 7.0, the enzyme contains Co2+
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+
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.006
-
-
crude cell extract, in 50 mM 4-morpholinepropanesulfonic acid, pH 6.0, at 25C
0.36
-
-
enzyme assay performed at 25C, pH 8.0 and 50 mmol/l Tris-acetate buffer
0.8
-
-
25 mM Hepes buffer at pH 7.0 and 25C, under not saturating conditions. ACSMD loaded with 1 molar equivalent Mn2+
1.39
-
-
after 231fold purification, in 50 mM 4-morpholinepropanesulfonic acid, pH 6.0, at 25C
1.7
-
-
25 mM Hepes buffer at pH 7.0 and 25C, under not saturating conditions. ACSMD loaded with 1 molar equivalent Cd2+
2.9
-
-
25 mM Hepes buffer at pH 7.0 and 25C, under not saturating conditions. ACSMD loaded with 1 molar equivalent Fe2+
3.789
-
-
-
5.9
-
-
25 mM Hepes buffer at pH 7.0 and 25C, under not saturating conditions. ACSMD loaded with 1 molar equivalent Co2+
6
-
-
in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22C
8.07
-
Q8R5M5
in kidney
8.82
-
Q8R5M5
in liver
additional information
-
-
-
additional information
-
-
ACMSD assay at pH 7.0 and in 50 mM potassium phosphate buffer. ACMSD activity is suppressed 20fold and 4fold after feeding of rats with linoleic acid concentrations of 20% and 10% respectively compared to 40 micromol/h/g protein without feeding of linoleic acid. Palmitic acid, stearic acid and oleic acid do not suppress ACMSD activity. N-3 fatty acids suppress ACMSD activity even at only 2% in diets.
additional information
-
-
3.07 micromol/h/g kidney, enzyme assay performed at 25C, pH 8.0 and 50 mmol/l Tris-acetate buffer
additional information
-
-
9.3 micromol/h/g liver, enzyme assay performed at 25C, pH 8.0 and in 50 mmol/l Tris-acetate buffer
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
6.5
Q8R5M5
-
6
9.5
-
-
6.5
8
-
-
7.5
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9
-
pH 6: about 40% of maximal activity, pH 9.0: about 35% of maximal activity
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37140
-
Q83V25
deduced from DNA sequence
38090
-
Q8R5M5
deduced from cDNA
38700
-
Q83V25
recombinant protein, SDS-PAGE
39000
-
Q8R5M5
SDS-PAGE
39000
-
-
SDS-PAGE
40000
-
-
SDS-PAGE
50000
-
-
gel filtration
58000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
x-ray crystallography
monomer
-
1 * 41000, SDS-PAGE
monomer
-
-
monomer or dimer
-
the protein exists in solution as a mixture of both monomer and dimer forms
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
vapour diffusion technique in hanging drop, crystal structure of human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase in complex with the glycolytic intermediate 1,3-dihydroxyacetonephosphate (DHAP), refined to an R-factor of 0.19, 1 mM DHAP, 2% poly(ethylene glycol) (PEG 400), 0.1 M Na/Hepes pH 7.5, 2.0 M ammonium sulphate, mixed with the same amount of a protein solution at a concentration of 12.7 mg/ml, and equilibrated against 500 microL of the reservoir solution, at 20C
-, Q8TDX5
hanging drop vapour diffusion method with 0.1 M Tris (pH 8.75), 15% PEG 5000, and 0.2 M MgCl2, at 20C
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9.5
-
stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
-20
-
-
the purified protein is sensitive to freezing at -20C
40
60
Q8R5M5
activity is decreased by 25% after 5 min at 40C, but thereafter is stable for up to 30 min, activity is completely lost by incubation at 60C for 30 min
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable for several months
-
4C, 10 mM Tris-HCl, pH 8.0, 0.13 m NaCl, several weeks, remains stable
-
-20C, 50 mM potassium phosphate buffer, pH 7.0, 0.14 M KCl, 5 mM 2-mercaptoethanol, 1 mM dithiothreitol, 1 mM EDTA, 20% glycerol, stable for at least 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
-, Q8TDX5
hydroxyapatite column chromatography, MonoQ column chromatography and Superose 12 gel filtration
-
partial
Q8TDX5
-
Q8R519
Ni-NTA superflow resin chromatography and HisPrep FF column chromatography
-
Q-Sepharose HP column chromatography, Phenyl Sepharose column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
-, Q8TDX5
cDNA cloning
-
cDNA cloning, expressed in COS7 cells
Q8TDX5
expressed in Pichia pastoris GS115 cells
-
expression in COS-7 cells
-
cDNA cloning
-
expressed in Escherichia coli BL21(DE3) cells
-
nbaD gene overexpressed in Escherichia coli
Q83V25
cDNA cloning
-
cDNA cloning, ACMSD ORF is inserted into a mammalian expression vector and transfected into human hepatoma HepG2 cells
Q8R5M5
cDNA cloning
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
H6A
-
activity decreases by about 82%
H8A
-
activity decreases by about 50%
D294E
-
the mutation causes a dramatic loss of enzyme activity, substantial reduction of the metal-binding ability, and an altered metallocenter electronic structure
H177A
-
similar properties like the wild type enzyme
H177A
-
the mutation causes a dramatic loss of enzyme activity, substantial reduction of the metal-binding ability, and an altered metallocenter electronic structure
H228A
-
the mutation causes a dramatic loss of enzyme activity, substantial reduction of the metal-binding ability, and an altered metallocenter electronic structure
H228E
-
the mutation causes a dramatic loss of enzyme activity, substantial reduction of the metal-binding ability, and an altered metallocenter electronic structure
H9E
-
the mutation causes a dramatic loss of enzyme activity, substantial reduction of the metal-binding ability, and an altered metallocenter electronic structure
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
-, Q8TDX5
inhibition of alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase should be explored as a possible novel therapeutic avenue for the treatment of diabetes
medicine
Q8TDX5
quinolinate, non-enzymatically derived from 2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate is a potent endogenous excitotoxin of neuronal cells, whose elevation in brain is implicated in the pathogenesis of various neurodegenerative disorders, ACMSD is the only known enzyme that can process ACMS to a benign catabolite and thus prevent the accumulation of quinolinate
medicine
-
the enzyme is an therapeutic target for treating disorders associated with increased levels of tryptophan metabolites
medicine
Q8R519
quinolinate, non-enzymatically derived from 2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate is a potent endogenous excitotoxin of neuronal cells, whose elevation in brain is implicated in the pathogenesis of various neurodegenerative disorders, ACMSD is the only known enzyme that can process ACMS to a benign catabolite and thus prevent the accumulation of quinolinate
medicine
Mus musculus ICR
-
quinolinate, non-enzymatically derived from 2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate is a potent endogenous excitotoxin of neuronal cells, whose elevation in brain is implicated in the pathogenesis of various neurodegenerative disorders, ACMSD is the only known enzyme that can process ACMS to a benign catabolite and thus prevent the accumulation of quinolinate
-
medicine
Q8R5M5
during the metabolism of tryptophan, ACMSD is able to influence directly the production of quinolinate, a potent endogenous excitotoxin, have roles in the pathogenesiof epilepsy, Huntington's disease, Alzheimer's disease and demetia resulting from AIDS, and picolinate which may influence the immune system in macrophages and apoptosis in human leukaemia cell lines
medicine
Q8R5M5
quinolinate, non-enzymatically derived from 2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate is a potent endogenous excitotoxin of neuronal cells, whose elevation in brain is implicated in the pathogenesis of various neurodegenerative disorders, ACMSD is the only known enzyme that can process ACMS to a benign catabolite and thus prevent the accumulation of quinolinate
medicine
-
quinolinate, non-enzymatically derived from 2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate is a potent endogenous excitotoxin of neuronal cells, whose elevation in brain is implicated in the pathogenesis of various neurodegenerative disorders, ACMSD is the only known enzyme that can process ACMS to a benign catabolite and thus prevent the accumulation of quinolinate