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Gene Review

BNA5  -  kynureninase

Saccharomyces cerevisiae S288c

Synonyms: Biosynthesis of nicotinic acid protein 5, Kynureninase, L-kynurenine hydrolase, L8083.14, YLR231C
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Disease relevance of BNA5

  • Cloning, sequence, and expression of kynureninase from Pseudomonas fluorescens [1].
  • The resultant plasmid was used to transform E. coli DH5alpha F', and these cells overexpressed kynureninase to about 37% of total soluble protein [1].

High impact information on BNA5

  • We have identified the genes that encode the enzymes of the kynurenine pathway and for BNA5 (YLR231c) and BNA6 (YFR047c) confirmed that they encode kynureninase and quinolinate phosphoribosyl transferase respectively [2].
  • Based on this alignment, we predict that Lys227 and Asp212 in P. fluorescens kynureninase are involved in pyridoxal-5'-phosphate binding [1].
  • Alignment of the four sequences shows a highly conserved region which corresponds to the pyridoxal-5'-phosphate (PLP) binding site of rat kynureninase [1].
  • P. fluorescens kynureninase also exhibits significant homology to the nifS gene product, cysteine desulfurase, and to eucaryotic serine/pyruvate aminotransferases, suggesting that it is a member of subgroup IV of the aminotransferase family of PLP-dependent enzymes [1].
  • Hemin added to the medium enhanced total niacin production by increasing the amount of tryptophan metabolized via the kynureninase flux [3].

Associations of BNA5 with chemical compounds

  • 2-3H liberation increased dose-dependently at tryptophan concentration higher than 10(-5)M, while the kynureninase flux reached its plateau at 10(-5)M [4].
  • Of kynurenine (0.05 mM) added to the medium, 55% went through the transaminase flux (2-H liberation), 20% through the kynureninase flux, but none through the acetyl-CoA flux [5].


  1. Cloning, sequence, and expression of kynureninase from Pseudomonas fluorescens. Koushik, S.V., Sundararaju, B., McGraw, R.A., Phillips, R.S. Arch. Biochem. Biophys. (1997) [Pubmed]
  2. Aerobic and anaerobic NAD+ metabolism in Saccharomyces cerevisiae. Panozzo, C., Nawara, M., Suski, C., Kucharczyka, R., Skoneczny, M., Bécam, A.M., Rytka, J., Herbert, C.J. FEBS Lett. (2002) [Pubmed]
  3. Effects of exogenous hemin on the niacin content of aerobically grown Saccharomyces uvarum. Shin, M., Sano, K., Umezawa, C. FEMS Microbiol. Lett. (1991) [Pubmed]
  4. Metabolic fates of L-tryptophan in Saccharomyces uvarum (Saccharomyces carlsbergensis). Shin, M., Shinguu, T., Sano, K., Umezawa, C. Chem. Pharm. Bull. (1991) [Pubmed]
  5. Metabolism of tryptophan to niacin in Saccharomyces uvarum. Shin, M., Sano, K., Umezawa, C. J. Nutr. Sci. Vitaminol. (1991) [Pubmed]
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