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Gene Review

speA  -  biosynthetic arginine decarboxylase, PLP...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK2933, JW2905
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Disease relevance of speA


High impact information on speA


Chemical compound and disease context of speA


Biological context of speA


Anatomical context of speA

  • These results suggest that it may be possible to use an arginine decarboxylase inhibitor in conjunction with known inhibitors of ornithine decarboxylase to block all putrescine biosynthesis in prokaryotic cells and thus to study the effects of such inhibition in these organisms [13].
  • Selective disruption of the cell envelope and an assessment of ADC activity or immunoprecipitable ADC in various fractions demonstrated its location between the cytoplasmic membrane and peptidoglycan layer [14].

Associations of speA with chemical compounds


Analytical, diagnostic and therapeutic context of speA

  • Peptide mapping experiments with V8 protease, trypsin, and alpha-chymotrypsin demonstrated that the two species of ADC were very similar except for a minor difference [14].
  • The diminished ornithine and arginine decarboxylase activities are shown to result from reversible post-translational inhibition since the enzymes could be reactivated to normal levels upon titration of the inhibitors [17].
  • We report here the crystallization of arginine decarboxylase from E. coli [18].
  • High-performance liquid chromatography method with radiochemical detection for measurement of nitric oxide synthase, arginase, and arginine decarboxylase activities [19].


  1. Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli. Moore, R.C., Boyle, S.M. J. Bacteriol. (1990) [Pubmed]
  2. Cyclic AMP inhibits and putrescine represses expression of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli. Moore, R.C., Boyle, S.M. J. Bacteriol. (1991) [Pubmed]
  3. Identification of the putrescine biosynthetic genes in Pseudomonas aeruginosa and characterization of agmatine deiminase and N-carbamoylputrescine amidohydrolase of the arginine decarboxylase pathway. Nakada, Y., Itoh, Y. Microbiology (Reading, Engl.) (2003) [Pubmed]
  4. Ornithine decarboxylase, S-adenosyl-L-methionine decarboxylase and arginine decarboxylase from Mycobacterium bovis (BCG). Paulin, L., Brander, E., Pösö, H. Experientia (1987) [Pubmed]
  5. Transcriptional effects of polyamines on ribosomal proteins and on polyamine-synthesizing enzymes in Escherichia coli. Huang, S.C., Panagiotidis, C.A., Canellakis, E.S. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  6. Biosynthesis of polyamines in ornithine decarboxylase, arginine decarboxylase, and agmatine ureohydrolase deletion mutants of Escherichia coli strain K-12. Panagiotidis, C.A., Blackburn, S., Low, K.B., Canellakis, E.S. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  7. Construction of lac fusions to the inducible arginine- and lysine decarboxylase genes of Escherichia coli K12. Auger, E.A., Redding, K.E., Plumb, T., Childs, L.C., Meng, S.Y., Bennett, G.N. Mol. Microbiol. (1989) [Pubmed]
  8. Analysis of enzyme kinetics by using integrated rate equations. Arginine decarboxylase. Cox, T.T., Boeker, E.A. Biochem. J. (1987) [Pubmed]
  9. Nucleotide sequence of the adi gene, which encodes the biodegradative acid-induced arginine decarboxylase of Escherichia coli. Stim, K.P., Bennett, G.N. J. Bacteriol. (1993) [Pubmed]
  10. Cloning and characterization of human agmatinase. Iyer, R.K., Kim, H.K., Tsoa, R.W., Grody, W.W., Cederbaum, S.D. Mol. Genet. Metab. (2002) [Pubmed]
  11. Arginine decarboxylase from a Pseudomonas species. Rosenfeld, H.J., Roberts, J. J. Bacteriol. (1976) [Pubmed]
  12. Crystallization and preliminary X-ray crystallographic analysis of a putative agmatinase from Deinococcus radiodurans. Lee, J.A., Ahn, H.J., Ha, J.Y., Shim, S.M., Kim, K.H., Kim, H.K., Suh, S.W. Acta Crystallogr. D Biol. Crystallogr. (2004) [Pubmed]
  13. DL-alpha-(Difluoromethyl)arginine: a potent enzyme-activated irreversible inhibitor of bacterial decarboxylases. Kallio, A., McCann, P.P., Bey, P. Biochemistry (1981) [Pubmed]
  14. Biosynthetic arginine decarboxylase in Escherichia coli is synthesized as a precursor and located in the cell envelope. Buch, J.K., Boyle, S.M. J. Bacteriol. (1985) [Pubmed]
  15. Expression, crystallization and preliminary X-ray crystallographic analysis of human agmatinase. Kim, K.H., Ahn, H.J., Kim, d.o. .J., Lee, H.H., Ha, J.Y., Kim, H.K., Yoon, H.J., Suh, S.W. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2005) [Pubmed]
  16. Arginine decarboxylase from Escherichia coli B: mechanism of dissociation from the decamer to the dimer. Boeker, E.A. Biochemistry (1978) [Pubmed]
  17. Relationship of the expression of the S20 and L34 ribosomal proteins to polyamine biosynthesis in Escherichia coli. Panagiotidis, C.A., Huang, S.C., Canellakis, E.S. Int. J. Biochem. Cell Biol. (1995) [Pubmed]
  18. Crystallization of biosynthetic arginine decarboxylase from Escherichia coli. Rodrigez, B.R., Carroll, D.W., Mitchell, D., Momany, C., Hackert, M.L. Acta Crystallogr. D Biol. Crystallogr. (1994) [Pubmed]
  19. High-performance liquid chromatography method with radiochemical detection for measurement of nitric oxide synthase, arginase, and arginine decarboxylase activities. Volke, A., Wegener, G., Vasar, E., Volke, V. Methods and findings in experimental and clinical pharmacology. (2006) [Pubmed]
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