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. 1979 Sep;38(3):359–364. doi: 10.1128/aem.38.3.359-364.1979

Stimulation of L-asparate beta-decarboxylase formation by L-glutamate in Pseudomonas dacunhae and Improved production of L-alanine.

T Shibatani, T Kakimoto, I Chibata
PMCID: PMC243499  PMID: 533269

Abstract

The formation of L-asparate beta-decarboxylase by Pseudomonas dacunhae was compared on media containing a variety of organic acids and amino acids as a carbon source. Although the enzyme was formed constitutively when the organism was grown on basal medium or on that containing tricarboxylic acid cycle intermediates, it was induced twofold by L-glutamate and repressed one-tenth by L-serine. L-Glutamine, L-proline, L-leucine, glycine, and L-threonine also showed induction effects lower than that of L-glutamate. L-Glutamate derepressed the serine effect. This glutamate effect was observed effect was observed with other microoganisms, e.g., Achromobacter pestifer and Achromobacter liquidum. Since the intermediates from L-glutamate metabolism had no effect, this induction effect was specific to L-glutamate. The formation of some glutamate-related enzymes was measured and is discussed in relation to the formation of L-asparate beta-decarboxylase. L-Asparate beta-decarboxylase was purified to an electrophoretically homogenous state from L-glutamate-grown cells of P. dacunhae, and some properties were compared with those of the enzyme from fumarate-grown cells. The two enzymes were identical in disc electrophoresis, molecular weight, and some enzymatic properties. The industrial production of L-alanine from L-aspartic acid acid was improved by using the culture broth with highly induced L-asparate beta-decarboxylase (9.4 U/ml of broth).

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BHEEMESWAR B. Studies on transaminase and decarboxylase catalysed by extracts of the silkworm, Bombyx mori L. Nature. 1955 Sep 17;176(4481):555–556. doi: 10.1038/176555b0. [DOI] [PubMed] [Google Scholar]
  2. CATTANEO-LACOMBE J., SENEZ J. C., BEAUMONT P. Sur la purification de la 4-aspartique décarboxylase de Desulfovibrio desulfuricans. Biochim Biophys Acta. 1958 Dec;30(3):458–465. doi: 10.1016/0006-3002(58)90090-8. [DOI] [PubMed] [Google Scholar]
  3. COOKSEY K. E., RAINBOW C. Metabolic patterns in acetic acid bacteria. J Gen Microbiol. 1962 Jan;27:135–142. doi: 10.1099/00221287-27-1-135. [DOI] [PubMed] [Google Scholar]
  4. CRAWFORD L. V. Studies on the aspartic decarboxylase of Nocardia globerula. Biochem J. 1958 Feb;68(2):221–225. doi: 10.1042/bj0680221. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Chibata I., Kakimoto T., Kato J. Enzymatic production of L-alanine by Pseudomonas dacunhae. Appl Microbiol. 1965 Sep;13(5):638–645. doi: 10.1128/am.13.5.638-645.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Chibata I., Kakimoto T., Kato J., Shibatani T., Nishimura N. On the activation mechanism of L-aspartate beta-decarboxylase from Pseudomonas dacunhae by alpha-ketoglutarate. Biochem Biophys Res Commun. 1968 Aug 13;32(3):375–379. doi: 10.1016/0006-291x(68)90670-0. [DOI] [PubMed] [Google Scholar]
  7. Gilles R., Schoffeniels E. Décarboxylation des acides aspartique et oxaloacétique chez le homard et l'écrevisse. Bull Soc Chim Biol (Paris) 1966;48(3):397–417. [PubMed] [Google Scholar]
  8. Kakimoto T., Kato J., Shibatani T., Nishimura N., Chibata I. Crystalline L-aspartate beta-decarboxylase of Pseudomonas dacunhae. I. Crystallization and some physiocochemical properties. J Biol Chem. 1969 Jan 25;244(2):353–358. [PubMed] [Google Scholar]
  9. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  10. MEISTER A., SOBER H. A., TICE S. V. Enzymatic decarboxylation of aspartic acid to alpha-alanine. J Biol Chem. 1951 Apr;189(2):577–590. [PubMed] [Google Scholar]
  11. NISHIMURA J. S., MANNING J. M., MEISTER A. Studies on the mechanism of activation acid beta-decarboxylase by alpha-keto acids and pyridoxal 5'-phosphate. Biochemistry. 1962 May 25;1:442–447. doi: 10.1021/bi00909a011. [DOI] [PubMed] [Google Scholar]
  12. NOVOGRODSKY A., MEISTER A. CONTROL OF ASPARTATE BETA-DECARBOXYLASE ACTIVITY BY TRANSAMINATION. J Biol Chem. 1964 Mar;239:879–888. [PubMed] [Google Scholar]
  13. O'Connor M. L., Hanson R. S. Serine transhydroxymethylase isoenzymes from a facultative methylotroph. J Bacteriol. 1975 Nov;124(2):985–996. doi: 10.1128/jb.124.2.985-996.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. SEAMAN G. R. Amino acid decarboxylases in a pseudomonad. J Bacteriol. 1960 Dec;80:830–836. doi: 10.1128/jb.80.6.830-836.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. SENEZ J. C., CATTANEO-LACOMBE J. Transformation de l'acide L-aspartique en alpha-alanine par des extraits de Desulfovibrio desulfuricans. C R Hebd Seances Acad Sci. 1956 Feb 13;242(7):941–943. [PubMed] [Google Scholar]
  16. SHUKUYA R., SCHWERT G. W. Glutamic acid decarboxylase. I. Isolation procedures and properties of the enzyme. J Biol Chem. 1960 Jun;235:1649–1652. [PubMed] [Google Scholar]
  17. Tate S. S., Meister A. Interaction of gamma-glutamyl transpeptidase with amino acids, dipeptides, and derivatives and analogs of glutathione. J Biol Chem. 1974 Dec 10;249(23):7593–7602. [PubMed] [Google Scholar]
  18. Tate S. S., Meister A. Regulation of the activity of L-aspartate beta-decarboxylase by a novel allosteric mechanism. Biochemistry. 1969 Apr;8(4):1660–1668. doi: 10.1021/bi00832a048. [DOI] [PubMed] [Google Scholar]
  19. Veronese F. M., Boccu E., Conventi L. Glutamate dehydrogenase from Escherichia coli: induction, purification and properties of the enzyme. Biochim Biophys Acta. 1975 Feb 19;377(2):217–228. doi: 10.1016/0005-2744(75)90304-6. [DOI] [PubMed] [Google Scholar]
  20. WARREN H. W., HORN M. J., BLUM A. E. Microbiological determination of alanine in proteins and foods. Anal Biochem. 1963 Jan;5:70–77. doi: 10.1016/0003-2697(63)90060-5. [DOI] [PubMed] [Google Scholar]
  21. WILSON E. M. Crystalline L-aspartate 4-carboxy-lyase. Biochim Biophys Acta. 1963 Feb 12;67:345–348. doi: 10.1016/0006-3002(63)91840-7. [DOI] [PubMed] [Google Scholar]
  22. WILSON E. M., KORNBERG H. L. PROPERTIES OF CRYSTALLINE L-ASPARTATE 4-CARBOXY-LYASE FROM ACHROMOBACTER SP. Biochem J. 1963 Sep;88:578–587. doi: 10.1042/bj0880578. [DOI] [PMC free article] [PubMed] [Google Scholar]

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