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Information on EC 4.1.1.45 - aminocarboxymuconate-semialdehyde decarboxylase and Organism(s) Rattus norvegicus and UniProt Accession Q8R5M5

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     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.45 aminocarboxymuconate-semialdehyde decarboxylase
IUBMB Comments
Product rearranges non-enzymically to picolinate.
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This record set is specific for:
Rattus norvegicus
UNIPROT: Q8R5M5
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
acmsd, aminocarboxymuconate-semialdehyde decarboxylase, alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase, picolinic carboxylase, acmsdase, hacmsd, 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase, acmsd i, acms decarboxylase, alpha-amino-beta-carboxymuconic-epsilon-semialdehyde decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
-
alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase
-
picolinic carboxylase
-
3-(3-oxoprop-2-enyl)-2-aminobut-2-endioate carboxy-lyase
-
-
-
-
ACMSD
ACMSDase
-
-
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
-
-
Amino-carboxymuconate-semialdehyde decarboxylase
-
-
-
-
Decarboxylase, aminocarboxymuconate semialdehyde
-
-
-
-
Picolinic acid carboxylase
-
-
-
-
Picolinic acid decarboxylase
-
-
-
-
Picolinic decarboxylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
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.
CAS REGISTRY NUMBER
COMMENTARY hide
37289-47-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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-6-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-6-semialdehyde + CO2
show the reaction diagram
-
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
?
show the reaction diagram
additional information
?
-
-
key enzyme in NAD biosynthesis from tryptophan
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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-6-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
?
show the reaction diagram
additional information
?
-
-
key enzyme in NAD biosynthesis from tryptophan
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
p-chloromercuribenzoate
-
eicosapentaenoic acid
-
ACMSD mRNA levels in primary hepatocytes are decreased by the incubation with high concentrations of eicosapentaenoic acid
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-n-butyl phthalate
-
20% inhibition of ACMSD activity in the presence of 3 mmol/l mono-n-butyl phthalate
mono-n-hexyl phthalate
-
60% inhibition of ACMSD activity in the presence of 3 mmol/l mono-n-hexyl phthalate
WY-14,643
-
ACMSD mRNA levels in primary hepatocytes are decreased by the incubation with high concentrations of WY-14,643
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
hepatic ACMSD activity is increased in streptozotocin-induced diabetic rats
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013 - 0.014
2-amino-3-carboxymuconate-6-semialdehyde
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme plays a key role in NAD+ biosynthesis from tryptophan. The enzyme is associated with cholesterol metabolism
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACMSD_RAT
336
0
38091
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38090
deduced from cDNA
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 60
activity is decreased by 25% after 5 min at 40°C, but thereafter is stable for up to 30 min, activity is completely lost by incubation at 60°C for 30 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA cloning, ACMSD ORF is inserted into a mammalian expression vector and transfected into human hepatoma HepG2 cells
cDNA cloning
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene expression is positively regulated by SREBP-2 in the hypercholesterolemic rat and rat primary hepatocytes
the enzyme activity in hypercholesterolemic rats is decreased in liver but not in kidney
enzyme mRNA expression and activity is decreased by phytol in a dose-dependent manner (80% at 0.1 mM)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Homo sapiens (Q8TDX5), Homo sapiens, Mus musculus (Q8R519), Mus musculus ICR (Q8R519), Rattus norvegicus (Q8R5M5), Sus scrofa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team