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Chemical Compound Review

Allophanate     aminocarbonylcarbamic acid

Synonyms: CHEBI:9889, AG-G-29997, CTK2F4542, AKOS006340981, AC1L4543, ...
 
 
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High impact information on aminocarbonylcarbamic acid

  • Expression of the allantoin system genes in Saccharomyces cerevisiae is induced by allophanate or its analog, oxalurate [1].
  • Its expression was (i) induced by allophanate, (ii) sensitive to nitrogen catabolite repression, and (iii) responsive to mutation of the DAL80 and DAL81 loci, which have previously been shown to regulate the allantoin degradation system [2].
  • Comparable constitutive levels of activity were also observed in doubly mutant strains (durl dal80) which are unable to synthesize allophanate [3].
  • Production of the four enzymes and one of the active transport systems is inducible; allophanate, the last intermediate of the pathway, functions as the inducer [3].
  • Previous studies have shown that (i) Dal81p and Dal82p are required for allophanate-induced gene expression in Saccharomyces cerevisiae; (ii) the cis-acting element mediating the induced transcriptional response to allophanate is a dodecanucleotide, UIS(ALL); and (iii) Dal82p binds specifically to UIS(ALL) [4].
 

Biological context of aminocarbonylcarbamic acid

  • Only malonamate, which strongly inhibited allophanate hydrolysis, was an alternative substrate, with a greatly reduced k(cat)/K(m) of 21 s(-1) M(-1) [5].
  • The substrate specificity of the enzyme was strict, and analogs of allophanate were not hydrolyzed [6].
  • MPEG was grafted on PDMS-based PUs by two methods depending on the PU synthetic routes: esterification and allophanate reactions [7].
  • In light-synchronized cultures, allophanate lyase induction appeared to be limited to the light phase of the cell cycle, provided that culture samples were induced under ongoing illumination conditions (i.e. light induction of light phase cells and dark induction of dark phase cells) [8].
  • The relationship between allophanate lyase induction and gametogenesis is discussed [8].
 

Associations of aminocarbonylcarbamic acid with other chemical compounds

 

Gene context of aminocarbonylcarbamic acid

  • Dal82p binds to the UIS(ALL) sites of allophanate-induced genes of the allantoin-degradative pathway and functions synergistically with the GATA family Gln3p and Gat1p transcriptional activators that are responsible for nitrogen catabolite repression-sensitive gene expression [14].

References

  1. The DAL7 promoter consists of multiple elements that cooperatively mediate regulation of the gene's expression. Yoo, H.S., Cooper, T.G. Mol. Cell. Biol. (1989) [Pubmed]
  2. Identification of the ureidoglycolate hydrolase gene in the DAL gene cluster of Saccharomyces cerevisiae. Yoo, H.S., Genbauffe, F.S., Cooper, T.G. Mol. Cell. Biol. (1985) [Pubmed]
  3. Isolation and characterization of mutants that produce the allantoin-degrading enzymes constitutively in Saccharomyces cerevisiae. Chisholm, G., Cooper, T.G. Mol. Cell. Biol. (1982) [Pubmed]
  4. Functional domain mapping and subcellular distribution of Dal82p in Saccharomyces cerevisiae. Scott, S., Dorrington, R., Svetlov, V., Beeser, A.E., Distler, M., Cooper, T.G. J. Biol. Chem. (2000) [Pubmed]
  5. Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP. Shapir, N., Sadowsky, M.J., Wackett, L.P. J. Bacteriol. (2005) [Pubmed]
  6. Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP-dependent degradation pathway specific to urea. Kanamori, T., Kanou, N., Kusakabe, S., Atomi, H., Imanaka, T. FEMS Microbiol. Lett. (2005) [Pubmed]
  7. PDMS-based polyurethanes with MPEG grafts: mechanical properties, bacterial repellency, and release behavior of rifampicin. Park, J.H., Lee, K.B., Kwon, I.C., Bae, Y.H. Journal of biomaterials science. Polymer edition. (2001) [Pubmed]
  8. The induction of allophanate lyase during the vegetative cell cycle in light-synchronized cultures of Chlamydomonas reinhardi. Semler, B.L., Hodson, R.C., Williams SK, I.I., Howell, S.H. Biochim. Biophys. Acta (1975) [Pubmed]
  9. Sequence of molecular events involved in induction of allophanate hydrolase. Bossinger, J., Cooper, T.G. J. Bacteriol. (1976) [Pubmed]
  10. Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth. Shapir, N., Cheng, G., Sadowsky, M.J., Wackett, L.P. Appl. Environ. Microbiol. (2006) [Pubmed]
  11. A study on grafting and characterization of HMDI-modified calcium hydrogenphosphate. Dong, G.C., Sun, J.S., Yao, C.H., Jiang, G.J., Huang, C.W., Lin, F.H. Biomaterials (2001) [Pubmed]
  12. Lomofungin inhibition of allophanate hydrolase synthesis in Saccharomyces cerevisiae. Lawther, R.P., Phillips, S.L., Cooper, T.G. Mol. Gen. Genet. (1975) [Pubmed]
  13. Functional analysis of the regulatory region adjacent to the cargB gene of Saccharomyces cerevisiae. Nucleotide sequence, gene fusion experiments and cis-dominant regulatory mutation analysis. Degols, G. Eur. J. Biochem. (1987) [Pubmed]
  14. Synergistic operation of the CAR2 (Ornithine transaminase) promoter elements in Saccharomyces cerevisiae. Park, H.D., Scott, S., Rai, R., Dorrington, R., Cooper, T.G. J. Bacteriol. (1999) [Pubmed]
 
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