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Gene Review

metC  -  cystathionine beta-lyase

Escherichia coli UTI89

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Disease relevance of metC


High impact information on metC

  • While the enzyme showed high gamma-lyase activity toward L-cystathionine (Km = 0.5 mM, Vmax = 2.5 units/mg) with an optimum pH of 8.2, no residual cystathionine beta-lyase behavior and only marginal reactivity toward L-cystine and L-cysteine were detected [6].
  • Aminoethoxyvinylglycine showed slow and tight binding characteristics with a Ki of 10.5 microM, comparable with its effect on cystathionine beta-lyase [6].
  • The region upstream of the beta-cystathionase (metC) gene in B. avium 197 lacked regulatory sequences ("Met boxes") described for metC in enteric species, and enzyme production was not repressed by methionine [7].
  • The three-dimensional structure of cystathionine beta-lyase from Arabidopsis was determined by Patterson search techniques, using the structure of tobacco (Nicotiana tabacum) cystathionine gamma-synthase as starting point [8].
  • The three-dimensional structure of cystathionine beta-lyase from Arabidopsis and its substrate specificity [8].

Chemical compound and disease context of metC


Biological context of metC

  • The chloramphenicol resistance determinant of a plasmid integrated at the ISP-I locus was mapped by PBS1 transduction and was found to be closely linked to metC (99.5%) [10].
  • Also, the overexpression of plasmid-encoded metC did not affect mal gene expression, nor did the deduced amino acid sequence of MetC show homology to that of MalY [11].
  • The encoded CmbR protein is homologous to the LysR family of regulator proteins and is an activator of the metC-cysK operon [4].
  • Other sulfur sources tested showed no significant effect on metC-cysK gene expression [4].
  • These mutations were mapped to a locus designated ctaA, located at 127 degrees between pyrD and metC on the B. subtilis chromosome [12].

Anatomical context of metC


Associations of metC with chemical compounds

  • In addition we found that O-acetyl-l-serine, the substrate of cysteine synthase, was an inducer of the metC-cysK operon [4].
  • The structure of the catalytic dimer and mode of PLP binding in Tnase resemble those found in aspartate amino-transferase, TPL, omega-amino acid pyruvate aminotransferase, dialkylglycine decarboxylase (DGD), cystathionine beta-lyase and ornithine decarboxylase [14].
  • Cystathionine beta-lyase (CBL) is a member of the gamma-family of pyridoxal-5'-phosphate (PLP)-dependent enzymes (Alexander et al., 1994) that cleave C(beta,gamma)-S bonds of a broad variety of substrates [15].

Analytical, diagnostic and therapeutic context of metC

  • Cloning, purification, and crystallization of Escherichia coli cystathionine beta-lyase [16].
  • A SDS-PAGE analysis identified a putative cystathionine beta-lyase band with approximate Mr of 41,000 that consisted of 368 amino acids encoded from ORF1 [3].


  1. Two transsulfurylation pathways in Klebsiella pneumoniae. Seiflein, T.A., Lawrence, J.G. J. Bacteriol. (2006) [Pubmed]
  2. Changes in active transport, intracellular adenosine 5'-triphosphate levels, macromolecular syntheses, and glycolysis in an energy-uncoupled mutant of Escherichia coli. Lieberman, M.A., Hong, J.S. J. Bacteriol. (1976) [Pubmed]
  3. Properties of the Corynebacterium glutamicum metC gene encoding cystathionine beta-lyase. Kim, J.W., Kim, H.J., Kim, Y., Lee, M.S., Lee, H.S. Mol. Cells (2001) [Pubmed]
  4. Regulation of the metC-cysK operon, involved in sulfur metabolism in Lactococcus lactis. Fernández, M., Kleerebezem, M., Kuipers, O.P., Siezen, R.J., van Kranenburg, R. J. Bacteriol. (2002) [Pubmed]
  5. Isolation of the patC gene encoding the cystathionine beta-lyase of Lactobacillus delbrueckii subsp. bulgaricus and molecular analysis of inter-strain variability in enzyme biosynthesis. Aubel, D., Germond, J.E., Gilbert, C., Atlan, D. Microbiology (Reading, Engl.) (2002) [Pubmed]
  6. Kinetics and inhibition of recombinant human cystathionine gamma-lyase. Toward the rational control of transsulfuration. Steegborn, C., Clausen, T., Sondermann, P., Jacob, U., Worbs, M., Marinkovic, S., Huber, R., Wahl, M.C. J. Biol. Chem. (1999) [Pubmed]
  7. Toxicity of Bordetella avium beta-cystathionase toward MC3T3-E1 osteogenic cells. Gentry-Weeks, C.R., Keith, J.M., Thompson, J. J. Biol. Chem. (1993) [Pubmed]
  8. The three-dimensional structure of cystathionine beta-lyase from Arabidopsis and its substrate specificity. Breitinger, U., Clausen, T., Ehlert, S., Huber, R., Laber, B., Schmidt, F., Pohl, E., Messerschmidt, A. Plant Physiol. (2001) [Pubmed]
  9. Accumulation of L-cystathionine by an Escherichia coli mutant deficient in cystathionine beta-lyase. Nishi, T., Tanaka, K., Tanaka, Y., Araki, K., Furihata, K., Onodera, M., Toda, K. J. Biosci. Bioeng. (2002) [Pubmed]
  10. Cloning and sequencing of the major intracellular serine protease gene of Bacillus subtilis. Koide, Y., Nakamura, A., Uozumi, T., Beppu, T. J. Bacteriol. (1986) [Pubmed]
  11. MalY of Escherichia coli is an enzyme with the activity of a beta C-S lyase (cystathionase). Zdych, E., Peist, R., Reidl, J., Boos, W. J. Bacteriol. (1995) [Pubmed]
  12. Isolation and sequence of ctaA, a gene required for cytochrome aa3 biosynthesis and sporulation in Bacillus subtilis. Mueller, J.P., Taber, H.W. J. Bacteriol. (1989) [Pubmed]
  13. Identification of odoriferous sulfanylalkanols in human axilla secretions and their formation through cleavage of cysteine precursors by a C-S lyase isolated from axilla bacteria. Natsch, A., Schmid, J., Flachsmann, F. Chem. Biodivers. (2004) [Pubmed]
  14. Crystal structure of tryptophanase. Isupov, M.N., Antson, A.A., Dodson, E.J., Dodson, G.G., Dementieva, I.S., Zakomirdina, L.N., Wilson, K.S., Dauter, Z., Lebedev, A.A., Harutyunyan, E.H. J. Mol. Biol. (1998) [Pubmed]
  15. Mode of action of cystathionine beta-lyase. Clausen, T., Laber, B., Messerschmidt, A. Biol. Chem. (1997) [Pubmed]
  16. Cloning, purification, and crystallization of Escherichia coli cystathionine beta-lyase. Laber, B., Clausen, T., Huber, R., Messerschmidt, A., Egner, U., Müller-Fahrnow, A., Pohlenz, H.D. FEBS Lett. (1996) [Pubmed]
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