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Aminocarboxymuconate semialdehyde decarboxylase

aminocarboxymuconate-semialdehyde decarboxylase, 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
The neuronal excitotoxin quinolinate is an intermediate in the de novo synthesis pathway of NAD from tryptophan, and has been implicated in the pathogenesis of several neurodegenerative disorders. Quinolinate is derived from alpha-amino-beta-carboxy-muconate-epsilon-semialdehyde (ACMS). ACMSD (ACMS decarboxylase; EC 4.1.1.45) can divert ACMS to a benign catabolite and thus prevent the accumulation of quinolinate from ACMS.[supplied by OMIM, Oct 2004] (from NCBI)
Top mentioned proteins: kynureninase, ACID, tryptophan 2,3-dioxygenase, CAN, Indo
Papers on aminocarboxymuconate-semialdehyde decarboxylase
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.
GeneRIF
Rizzi et al., Novara, Italy. In Febs J, 2009
Data report a crystal structure of human ACMSD in complex with the glycolytic intermediate 1,3-dihydroxyacetonephosphate (DHAP),suggesting a regulatory link between NAD synthesis and glycolysis.
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.
GeneRIF
Gonzalez et al., Bethesda, United States. In Mol Pharmacol, 2006
Acmsd gene expression was found to be under the control of both hepatocyte nuclear factor 4alpha (HNF4alpha) and peroxisome proliferator-activated receptor alpha (PPARalpha).
The effect of age on the enzyme activities of tryptophan metabolism along the kynurenine pathway in rats.
Allegri et al., Padova, Italy. In Clin Chim Acta, 2005
The liver aminocarboxymuconate-semialdehyde decarboxylase activity increased up to 12 months of age, then tended to decrease at 18 months, while in the kidneys, in which the activity was higher than in the liver at all the considered ages, the activity remained constantly elevated from 2-3 months to 18 months of age.
Tryptophan-NAD+ pathway metabolites as putative biomarkers and predictors of peroxisome proliferation.
Waterfield et al., Ware, United Kingdom. In Arch Toxicol, 2005
These compounds also reduced mRNA expression for aminocarboxymuconate-semialdehyde decarboxylase (ACMSDase, EC 4.1.1.45),
The necessity of niacin in rats fed on a high protein diet.
Shibata et al., Japan. In Biosci Biotechnol Biochem, 2005
This phenomenon was attributed to the supposition that liver aminocarboxymuconate-semialdehyde decarboxylase activities increased according with the dietary casein levels.
Changes in quinolinic acid production and its related enzymes following D-galactosamine and lipopolysaccharide-induced hepatic injury.
Seishima et al., Gifu, Japan. In Arch Biochem Biophys, 2004
D-Galactosamine treatment significantly decreased activities of hepatic aminocarboxymuconate-semialdehyde decarboxylase (ACMSDase) resulting in increased QUIN concentrations in serum and tissues.
Development of a multivariate statistical model to predict peroxisome proliferation in the rat, based on urinary 1H-NMR spectral patterns.
Haselden et al., Ware, United Kingdom. In Biomarkers, 2004
The inference from these results was that the tryptophan-nicotinamide adenine dinucleotide (NAD(+)) pathway was altered in correlation with peroxisome proliferation, a hypothesis subsequently confirmed by TaqMan analysis of the relevant genes encoding two key enzymes in the pathway, aminocarboxymuconate-semialdehyde decarboxylase (EC 4.1.1.45)
Enzyme activities of tryptophan metabolism along the kynurenine pathway in various species of animals.
Ragazzi et al., Padova, Italy. In Farmaco Prat, 2003
Liver tryptophan 2,3-dioxygenase, small intestine indole 2,3-dioxygenase, liver and kidney kynurenine 3-monooxygenase, kynureninase, kynurenine-oxoglutarate transaminase, 3-hydroxyanthranilate 3,4-dioxygenase and aminocarboxymuconate-semialdehyde decarboxylase were analysed.
Enzyme activities along the kynurenine pathway in mice.
Costa et al., Padova, Italy. In Adv Exp Med Biol, 2002
The following enzymes were assayed: liver tryptophan 2,3-dioxygenase, small intestine indole 2,3-dioxygenase, liver and kidney kynurenine 3-monooxygenase, kynureninase, kynurenine-oxoglutarate transaminase, 3-hydroxyanthranilate 3,4-dioxygenase, and aminocarboxymuconate-semialdehyde decarboxylase.
Tryptophan metabolism in rabbits.
Costa et al., Padova, Italy. In Adv Exp Med Biol, 2002
3-Hydroxyanthranilate 3,4-dioxygenase and aminocarboxymuconate-semialdehyde decarboxylase activities were higher in kidney than in liver.
Tryptophan metabolism along the kynurenine pathway in rats.
Rocchi et al., Padova, Italy. In Adv Exp Med Biol, 2002
Enzyme activities along the kynurenine pathway, liver tryptophan 2,3-dioxygenase, small intestine indole 2,3-dioxygenase, liver and kidney kynurenine 3-monooxygenase, kynureninase, kynurenine-oxoglutarate transaminase, 3-hydroxyanthranilate 3,4-dioxygenase, and aminocarboxymuconate-semialdehyde decarboxylase, involved in the catabolism of tryptophan, were studied in male adult Wistar albino rats.
Kynurenine pathway enzymes in different species of animals.
Ragazzi et al., Padova, Italy. In Adv Exp Med Biol, 2002
Kynurenine pathway enzyme activities, liver tryptophan 2,3-dioxygenase (TDO), small intestine indole 2,3-dioxygenase (IDO), liver and kidney kynurenine 3-monooxygenase, kynurenine-oxoglutarate transaminase, kynureninase, 3-hydroxyanthranilate 3,4-dioxygenase and aminocarboxymuconate-semialdehyde decarboxylase, were assayed in rabbits, rats, mice and guinea pigs.
Metabolism of tryptophan along the kynurenine pathway in alloxan diabetic rabbits.
Costa et al., Padova, Italy. In Adv Exp Med Biol, 2002
Instead, aminocarboxymuconate-semialdehyde decarboxylase (picolinic carboxylase) activity was significantly higher in diabetic-hyperlipidermic rabbits in comparison with hyperlypidemic and control rabbits.
The kynurenine pathway enzymes in healthy and hyperlipidemic rabbits.
Vanin et al., Padova, Italy. In Adv Exp Med Biol, 2002
The activities of liver tryptophan 2,3-dioxygenase small intestine indole 2,3-dioxygenase, liver and kidney kynurenine 3-monooxygenase, kynurenine-oxoglutarate transaminase, kynureninase, 3-hydroxyanthranilate 3,4-dioxygenase and aminocarboxymuconate semialdehyde decarboxylase (picolinic carboxylase) were determined.
Kynurenine pathway enzymes in guinea pigs.
Biasiolo et al., Padova, Italy. In Adv Exp Med Biol, 2002
3-Hydroxyanthranilate 3,4-dioxygenase gave similar, but very high, values in both liver and kidney, whereas aminocarboxymuconate-semialdehyde decarboxylase activity was double in kidney with respect to liver, but much lower than that of 3-hydroxyanthranilate 3,4-dioxygenase.
Enzyme activities along the tryptophan-nicotinic acid pathway in alloxan diabetic rabbits.
Allegri et al., Padova, Italy. In Biochim Biophys Acta, 2002
The enzymes assayed were: liver tryptophan 2,3-dioxygenase (TDO), intestine indoleamine 2,3-dioxygenase (IDO), liver and kidney kynurenine 3-monooxygenase, kynurenine-oxoglutarate transaminase, kynureninase, 3-hydroxyanthranilate 3,4-dioxygenase and aminocarboxymuconate-semialdehyde decarboxylase.TDO showed a reduction of specific activity in liver of diabetic-hyperlipidemic and hyperlipidemic rabbits compared to controls.
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