65
Views
0
CrossRef citations to date
0
Altmetric
Original Articles

Occurrence of a Novel Lyase Catalyzing β-Elimination Reaction toward threo-3-Chloro-L-aspartate in Pseudomonas putida TPU 7151

&
Pages 435-437 | Received 12 Jul 2000, Accepted 07 Oct 2000, Published online: 22 May 2014

  • 1) Arfin, S.M. and Koziell, D.A., Inhibition of growth of Salmonella typhimurium and of threonine deaminase and transaminase B by β-chloroalanine. J. Bacteriol., 105, 519-522 (1971).
  • 2) Tate, S.S., Relyea, N.M., and Meister, A., Interaction of L-aspartate-β-decarboxylase with β-chloro-L-alanine. β-Elimination reaction and active-site labelling. Biochemistry, 8, 5016-5021 (1969).
  • 3) Badet, B., Roise, D., and Walsh, C.T., Inactivation of the dadB Salmonella typhimurium alanine racemase by D and L isomers of β-substituted alanines: kinetics, stoichiometry, active site peptide sequencing, and reaction mechanism. Biochemistry, 23, 5188-5194 (1984).
  • 4) Henderson, L.L. and Johenston, R.B., Inhibition studies of the enantiomers of β-chloroalanine on purified alanine racemase from B. subtilis. Biochem. Biophys. Res. Commun., 68, 793-798 (1976).
  • 5) Kumagai, H., Suzuki, H., Shigematsu, H., and Tochikura, T., S Carboxymethylcysteine synthase from Escherichia coli. Agric. Biol. Chem., 53, 2481-2487 (1989).
  • 6) Nagasawa, T. and Yamada, H., Enzymatic transformations of 3-chloroalanine into useful amino acids. Appl. Biochem. Biotech., 13, 147-165 (1986).
  • 7) Asano, Y. and Kato, Y., Occurrence of 3-methylaspartate ammonia-lyase in facultative anaerobes and their application to synthesis of 3-substituted (S)-aspartic acids. Biosci. Biotechnol. Biochem., 58, 223-224 (1994).
  • 8) Kato, Y. and Asano, Y., Purification and properties of crystalline 3-methylaspartase from two facultative anaerobes, Citrobacter sp. strain YG-0504 and Morganella morganii strain YG-0601. Biosci. Biotechnol. Biochem., 59, 93-99 (1995).
  • 9) Kato, Y. and Asano, Y., 3-Methylaspartate ammonia-lyase from a facultative anaerobe, strain YG-1002. Appl. Microbiol. Biotech., 43, 901-907 (1995).
  • 10) Kato, Y. and Asano, Y., 3-Methylaspartate ammonia-lyase as a marker enzyme of the mesaconate pathway for (S)-glutamate fermentation in Enterobacteriaceae. Arch. Microbiol., 168, 457-463 (1997).
  • 11) Kato, Y. and Asano, Y., Cloning, nucleotide sequencing, and expression of 3-methylaspartate ammonia-lyase gene from Citrobacter amalonaticus strain YG-1002. Appl. Microbiol. Biotech., 50, 468-474 (1998).
  • 12) Friedmann, T.E. and Haugen, G.E., Pyruvic acid II. The determination of keto acids in blood and urine. J. Biol. Chem., 147, 415-442 (1943).
  • 13) Guilbault, G.G., XLIII. Oxaloacetate and oxoglutarate. In “Handbook of enzymatic method analysis” eds. Guilbault, G.G., Marcel Dekker, Inc., New York, pp. 309-310 (1976).
  • 14) Guilbault, G.G. VI. (L- and D-) alanine. In “Handbook of enzymatic method analysis” eds. Guilbault, G.G., Marcel Dekker, Inc., New York, pp. 208-210 (1976).
  • 15) Fawcett, J.K. and Scott, J.E., A rapid and precise method for the determination of urea. J. Clin. Path., 13, 156-159 (1960).
  • 16) Bergmann, J.G. and Sanik, J. Jr., Determination of trace amounts of chlorine in naphtha. Anal. Chem., 29, 241-243 (1957).
  • 17) Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
  • 18) Asano, Y., A Japanese screening approach-selection of an opine dehydrogenase and alkaline D-peptidase-. In “Studies in Organic Chemistry 53, New frontiers in screening for microbial biocatalysts”, eds. Kieslich, K., van der Beek, C.P., de Bont, J.A.M., and van den Tweel, W.J.J., Elsevier, Amsterdam., pp. 19-28 (1998).
  • 19) Asano, Y., Ueda, M., and Yamada, H., Microbial production of D-malate from maleate. Appl. Environ. Microbiol., 59, 1110-1113 (1993).
  • 20) Palleroni, N., Family I. Pseudomonadaceae. In “Bergey’s manual of systematic bacteriology Vol. I”, eds. Krieg, N.R. and Holt, J.G., Williams & Wilkins, Baltimore. pp. 141-218 (1984).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.