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Chemical Compound Review

Dienelactone     (2Z)-2-(5-oxo-2- furylidene)ethanoic acid

Synonyms: AC1NQXEN, SureCN891606, CHEBI:38107, C12838, 22752-92-7, ...
 
 
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Disease relevance of Dienelactone

 

High impact information on Dienelactone

  • Except for the cap domain the structure resembles that of the dienelactone hydrolase in spite of any significant sequence homology [3].
  • Three critical enzymes catechol oxygenase II (chlorocatechol dioxygenase), muconate cycloisomerase II, and dienelactone hydrolase, are involved in the degradation of chlorocatechols, which are obligatory intermediates in the catabolism of chlorinated aromatic compounds [4].
  • Furthermore, a gene for a dichlorophenol hydroxylase (tfdB), a putative regulatory gene (cadR), two genes for dichlorocatechol 1,2-dioxygenases (dccA(I/II)), two for dienelactone hydrolases (dccD(I/II)), part of a gene for maleylacetate reductase (dccE), and one gene for a potential phenoxyalkanoic acid permease were isolated [5].
  • As judged by sequence similarity and correspondence of predicted N termini with those of purified enzymes, the open reading frames correspond to genes for a second chlorocatechol 1,2-dioxygenase (ClcA2), a second chloromuconate cycloisomerase (ClcB2), a second dienelactone hydrolase (ClcD2), and a muconolactone isomerase-related enzyme (ClcF) [6].
  • The dienelactone hydrolase and the 3-oxoadipate enol-lactone hydrolase from Pseudomonas cepacia have now been purified to apparent homogeneity and characterized with respect to molecular mass and amino acid composition [7].
 

Chemical compound and disease context of Dienelactone

 

Biological context of Dienelactone

 

Associations of Dienelactone with other chemical compounds

 

Gene context of Dienelactone

  • Substrate-induced activation of dienelactone hydrolase: an enzyme with a naturally occurring Cys-His-Asp triad [11].
  • In this paper, using the disulfide proteome, we examined rice bran and identified fragments of embryo-specific protein and dienelactone hydrolase as putative targets of thioredoxin [12].
 

Analytical, diagnostic and therapeutic context of Dienelactone

References

  1. Crystallization and preliminary x-ray crystallographic data of dienelactone hydrolase from Pseudomonas sp. B13. Ollis, D.L., Ngai, K.L. J. Biol. Chem. (1985) [Pubmed]
  2. Identification and sequencing of pyrG, the CTP synthetase gene of Azospirillum brasilense Sp7. Zimmer, W., Hundeshagen, B. FEMS Microbiol. Lett. (1994) [Pubmed]
  3. Crystal structure of haloalkane dehalogenase: an enzyme to detoxify halogenated alkanes. Franken, S.M., Rozeboom, H.J., Kalk, K.H., Dijkstra, B.W. EMBO J. (1991) [Pubmed]
  4. Organization and nucleotide sequence determination of a gene cluster involved in 3-chlorocatechol degradation. Frantz, B., Chakrabarty, A.M. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  5. Genetic analysis of phenoxyalkanoic acid degradation in Sphingomonas herbicidovorans MH. Müller, T.A., Byrde, S.M., Werlen, C., van der Meer, J.R., Kohler, H.P. Appl. Environ. Microbiol. (2004) [Pubmed]
  6. A new modified ortho cleavage pathway of 3-chlorocatechol degradation by Rhodococcus opacus 1CP: genetic and biochemical evidence. Moiseeva, O.V., Solyanikova, I.P., Kaschabek, S.R., Gröning, J., Thiel, M., Golovleva, L.A., Schlömann, M. J. Bacteriol. (2002) [Pubmed]
  7. Dienelactone hydrolase from Pseudomonas cepacia. Schlömann, M., Ngai, K.L., Ornston, L.N., Knackmuss, H.J. J. Bacteriol. (1993) [Pubmed]
  8. Nucleotide sequence and expression of clcD, a plasmid-borne dienelactone hydrolase gene from Pseudomonas sp. strain B13. Frantz, B., Ngai, K.L., Chatterjee, D.K., Ornston, L.N., Chakrabarty, A.M. J. Bacteriol. (1987) [Pubmed]
  9. Different types of dienelactone hydrolase in 4-fluorobenzoate-utilizing bacteria. Schlömann, M., Schmidt, E., Knackmuss, H.J. J. Bacteriol. (1990) [Pubmed]
  10. Thiol protease-like active site found in the enzyme dienelactone hydrolase: localization using biochemical, genetic, and structural tools. Pathak, D., Ashley, G., Ollis, D. Proteins (1991) [Pubmed]
  11. Substrate-induced activation of dienelactone hydrolase: an enzyme with a naturally occurring Cys-His-Asp triad. Cheah, E., Austin, C., Ashley, G.W., Ollis, D. Protein Eng. (1993) [Pubmed]
  12. Disulfide proteome yields a detailed understanding of redox regulations: a model study of thioredoxin-linked reactions in seed germination. Yano, H., Kuroda, M. Proteomics (2006) [Pubmed]
  13. Following directed evolution with crystallography: structural changes observed in changing the substrate specificity of dienelactone hydrolase. Kim, H.K., Liu, J.W., Carr, P.D., Ollis, D.L. Acta Crystallogr. D Biol. Crystallogr. (2005) [Pubmed]
 
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