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Information on EC 4.1.1.45 - aminocarboxymuconate-semialdehyde decarboxylase and Organism(s) Mus musculus and UniProt Accession Q8R519

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EC Tree
     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:
Mus musculus
UNIPROT: Q8R519
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The taxonomic range for the selected organisms is: Mus musculus
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, alpha-amino-beta-carboxymuconic-epsilon-semialdehyde decarboxylase, acms decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-(3-oxoprop-2-enyl)-2-aminobut-2-endioate carboxy-lyase
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-
-
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ACMSD
ACMSDase
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alpha-Amino-beta-carboxymuconate-epsilon-semialdehade decarboxylase
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-
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alpha-Amino-beta-carboxymuconate-epsilon-semialdehyde beta-decarboxylase
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-
-
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alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase
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Amino-carboxymuconate-semialdehyde decarboxylase
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-
-
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Decarboxylase, aminocarboxymuconate semialdehyde
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-
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Picolinic acid carboxylase
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-
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Picolinic acid decarboxylase
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Picolinic decarboxylase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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-
-
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PATHWAY SOURCE
PATHWAYS
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-, -, -
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
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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-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-2-enyl)-but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
-
-
-
-
?
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-6-semialdehyde + CO2
show the reaction diagram
tryptophan-niacine pathway
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
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key enzyme in the regulation of the tryptophan-nicotinamide adenine dinucleotide pathway
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
p-chloromercuribenzoate
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mono (2-ethylhexyl) phthalate
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93% inhibition of ACMSD activity in the presence of 3 mmol/l mono (2-ethyl hexyl) phthalate
mono-n-butyl phthalate
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15% inhibition of ACMSD activity in the presence of 3 mmol/l mono-n-butyl phthalate
mono-n-hexyl phthalate
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64% inhibition of ACMSD activity in the presence of 3 mmol/l mono-n-hexyl phthalate
peroxisome proliferator-activated receptor alpha
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gene expression is downregulated by activation of peroxisome proliferator-activated receptor alpha
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[4-chloro-6-(2,3-xylidino)-2-pyrimidinylthio]acetic acid
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suppresses ACMSD activity
additional information
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not inhibited by monoethyl phthalate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hepatocyte nuclear factor 4alpha
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gene expression is activated by hepatocyte nuclear factor 4alpha
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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3.07 micromol/h/g kidney, enzyme assay performed at 25°C, pH 8.0 and 50 mmol/l Tris-acetate buffer
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
mouse, ICR strain
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACMSD_MOUSE
336
0
38027
Swiss-Prot
other Location (Reliability: 1)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA cloning
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
Manually annotated by BRENDA team