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Gene Review

ACMSD  -  aminocarboxymuconate semialdehyde...

Homo sapiens

Synonyms: 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase, Picolinate carboxylase
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Disease relevance of ACMSD

  • Kinetic and spectroscopic characterization of ACMSD from Pseudomonas fluorescens reveals a pentacoordinate mononuclear metallocofactor [1].

High impact information on ACMSD

  • Ultimately, these results suggest for the first time that ACMSD is a metal-dependent enzyme that catalyzes a novel nonoxidative decarboxylation [1].
  • The enzyme alpha-amino-beta-carboxy-muconic-epsilon-semialdehyde decarboxylase (ACMSD) plays an important role in the biodegradation of 2-nitrobenzoic acid in microorganisms and in tryptophan catabolism in humans [1].
  • We report that the overexpressed ACMSD enzyme from Pseudomonas fluorescens requires a divalent metal, such as Co(II), Fe(II), Cd(II), or Mn(II), for catalytic activity and that neither a redox reagent nor an organic cofactor is required for the catalytic function [1].
  • The activity of ACMSD determines whether the metabolites in both pathways are converted to quinolinic acid for NAD biosynthesis or to acetyl-CoA for the citric acid cycle [2].
  • Progress in the biochemical and structural characterization of ACMSD not only sheds light on the active site of this protein family but also promises the elucidation of the detailed catalytic mechanism of these novel transition metal-dependent nonoxidative decarboxylation reactions [3].

Biological context of ACMSD

  • The cDNA encodes a unique open reading frame of 336 amino acids and displays little homology to any known enzymes or motifs in mammalian databases, suggesting that ACMSD may contain a new kind of protein fold [4].
  • Utilizing partial amino acid sequences obtained from highly purified porcine kidney ACMSD, a cDNA encoding human ACMSD was cloned and characterized [4].

Anatomical context of ACMSD


Associations of ACMSD with chemical compounds


Analytical, diagnostic and therapeutic context of ACMSD


  1. Kinetic and spectroscopic characterization of ACMSD from Pseudomonas fluorescens reveals a pentacoordinate mononuclear metallocofactor. Li, T., Walker, A.L., Iwaki, H., Hasegawa, Y., Liu, A. J. Am. Chem. Soc. (2005) [Pubmed]
  2. Crystal structure of alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase: insight into the active site and catalytic mechanism of a novel decarboxylation reaction. Martynowski, D., Eyobo, Y., Li, T., Yang, K., Liu, A., Zhang, H. Biochemistry (2006) [Pubmed]
  3. Transition metal-catalyzed nonoxidative decarboxylation reactions. Liu, A., Zhang, H. Biochemistry (2006) [Pubmed]
  4. Identification and expression of alpha cDNA encoding human 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase (ACMSD): a key enzyme for the tryptophan-niacine pathway and quinolinate hypothesis. Fukuoka, S., Ishiguro, K., Tanabe, A., Egashira, Y., Sanada, H., Fukuwatari, T., Shibata, K. Adv. Exp. Med. Biol. (2003) [Pubmed]
  5. Changes in quinolinic acid production and its related enzymes following D-galactosamine and lipopolysaccharide-induced hepatic injury. Ohashi, H., Saito, K., Fujii, H., Wada, H., Furuta, N., Takemura, M., Maeda, S., Seishima, M. Arch. Biochem. Biophys. (2004) [Pubmed]
  6. Phthalate esters enhance quinolinate production by inhibiting alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD), a key enzyme of the tryptophan pathway. Fukuwatari, T., Ohsaki, S., Fukuoka, S., Sasaki, R., Shibata, K. Toxicol. Sci. (2004) [Pubmed]
  7. Tryptophan-niacin metabolism in rat with puromycin aminonucleoside-induced nephrosis. Egashira, Y., Nagaki, S., Sanada, H. International journal for vitamin and nutrition research. Internationale Zeitschrift für Vitamin- und Ernährungsforschung. Journal international de vitaminologie et de nutrition. (2006) [Pubmed]
  8. Degradation of 2-Nitrobenzoate by Burkholderia terrae Strain KU-15. Iwaki, H., Hasegawa, Y. Biosci. Biotechnol. Biochem. (2007) [Pubmed]
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