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. 1989 Jul;55(7):1829–1834. doi: 10.1128/aem.55.7.1829-1834.1989

Molybdenum Involvement in Aerobic Degradation of 2-Furoic Acid by Pseudomonas putida Fu1

Kerstin Koenig 1, Jan Remmer Andreesen 1,*
PMCID: PMC202958  PMID: 16347977

Abstract

An organism identified as Pseudomonas putida was isolated from an enrichment culture with 2-furoic acid as its sole source of carbon and energy. The organism contained a 2-furoyl-coenzyme A (CoA) synthetase to form 2-furoyl-CoA and a 2-furoyl-CoA dehydrogenase to form 5-hydroxy-2-furoyl-CoA as the first two enzymes involved in the degradation. Tungstate, the specific antagonist of molybdate, decreased growth rate and consumption of 2-furoic acid but had no influence on growth with succinate. Correspondingly, the 2-furoyl-CoA dehydrogenase activity decreased when the organism was grown on 2-furoic acid in the presence of increasing amounts of tungstate. The addition of molybdate reversed the negative effect on 2-furoyl-CoA dehydrogenase activity, which points to the involvement of a molybdoenzyme in this reaction. Both enzymes studied were inducible. No plasmid was detected in this organism.

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Selected References

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  1. 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. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  2. Brune G., Schoberth S. M., Sahm H. Growth of a strictly anaerobic bacterium on furfural (2-furaldehyde). Appl Environ Microbiol. 1983 Nov;46(5):1187–1192. doi: 10.1128/aem.46.5.1187-1192.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Coughlan M. P., Johnson J. L., Rajagopalan K. V. Mechanisms of inactivation of molybdoenzymes by cyanide. J Biol Chem. 1980 Apr 10;255(7):2694–2699. [PubMed] [Google Scholar]
  4. Dilworth G. L. Occurrence of molybdenum in the nicotinic acid hydroxylase from Clostridium barkeri. Arch Biochem Biophys. 1983 Mar;221(2):565–569. doi: 10.1016/0003-9861(83)90176-5. [DOI] [PubMed] [Google Scholar]
  5. Dilworth G. L. Properties of the selenium-containing moiety of nicotinic acid hydroxylase from Clostridium barkeri. Arch Biochem Biophys. 1982 Nov;219(1):30–38. doi: 10.1016/0003-9861(82)90130-8. [DOI] [PubMed] [Google Scholar]
  6. EBERWEIN H., GRIES F. A., DECKER K. [On the decomposition of nicotine by bacterial enzymes. II. Isolation and characterization of a nicotine-splitting soil bacterium]. Hoppe Seylers Z Physiol Chem. 1961 May 3;323:236–248. doi: 10.1515/bchm2.1961.323.1.236. [DOI] [PubMed] [Google Scholar]
  7. ENSIGN J. C., RITTENBERG S. C. THE PATHWAY OF NICOTINIC ACID OXIDATION BY A BACILLUS SPECIES. J Biol Chem. 1964 Jul;239:2285–2291. [PubMed] [Google Scholar]
  8. GREENLEE L., HANDLER P. XANTHINE OXIDASE. VI. INFLUENCE OF PH ON SUBSTRATE SPECIFICITY. J Biol Chem. 1964 Apr;239:1090–1095. [PubMed] [Google Scholar]
  9. Genthner B. R., Davis C. L., Bryant M. P. Features of rumen and sewage sludge strains of Eubacterium limosum, a methanol- and H2-CO2-utilizing species. Appl Environ Microbiol. 1981 Jul;42(1):12–19. doi: 10.1128/aem.42.1.12-19.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. HIGGINS E. S., RICHERT D. A., WESTERFELD W. W. Molybdenum deficiency and tungstate inhibition studies. J Nutr. 1956 Aug 10;59(4):539–559. doi: 10.1093/jn/59.4.539. [DOI] [PubMed] [Google Scholar]
  11. HOCHSTEIN L. I., RITTENBERG S. C. The bacterial oxidation of nicotine. II. The isolation of the first oxidative product and its identification as (1)-6-hydroxynicotine. J Biol Chem. 1959 Jan;234(1):156–160. [PubMed] [Google Scholar]
  12. HUNT A. L., HUGHES D. E., LOWENSTEIN J. M. The hydroxylation of nicotinic acid by Pseudomonas fluorescens. Biochem J. 1958 Jun;69(2):170–173. doi: 10.1042/bj0690170. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hirschberg R., Ensign J. C. Oxidation of nicotinic acid by a Bacillus species: source of oxygen atoms for the hydroxylation of nicotinic acid and 6-hydroxynicotinic acid. J Bacteriol. 1971 Nov;108(2):757–759. doi: 10.1128/jb.108.2.757-759.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Holmes D. S., Quigley M. A rapid boiling method for the preparation of bacterial plasmids. Anal Biochem. 1981 Jun;114(1):193–197. doi: 10.1016/0003-2697(81)90473-5. [DOI] [PubMed] [Google Scholar]
  15. KAKINUMA A., YAMATODANI S. L-GLUTAMIC ACID FORMATION FROM 2-FUROIC ACID BY SOIL BACTERIA. Nature. 1964 Jan 25;201:420–421. doi: 10.1038/201420a0. [DOI] [PubMed] [Google Scholar]
  16. Kitcher J. P., Trudgill P. W., Rees J. S. Purification and properties of 2-furoyl-coenzyme A hydroxylase from Pseudomonas putida F2. Biochem J. 1972 Nov;130(1):121–132. doi: 10.1042/bj1300121. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Krenitsky T. A. Aldehyde oxidase and xanthine oxidase--functional and evolutionary relationships. Biochem Pharmacol. 1978;27(24):2763–2764. doi: 10.1016/0006-2952(78)90186-7. [DOI] [PubMed] [Google Scholar]
  18. Krenitsky T. A., Neil S. M., Elion G. B., Hitchings G. H. A comparison of the specificities of xanthine oxidase and aldehyde oxidase. Arch Biochem Biophys. 1972 Jun;150(2):585–599. doi: 10.1016/0003-9861(72)90078-1. [DOI] [PubMed] [Google Scholar]
  19. Krenitsky T. A., Tuttle J. V., Cattau E. L., Jr, Wang P. A comparison of the distribution and electron acceptor specificities of xanthine oxidase and aldehyde oxidase. Comp Biochem Physiol B. 1974 Dec 15;49(4):687–703. doi: 10.1016/0305-0491(74)90256-9. [DOI] [PubMed] [Google Scholar]
  20. Margolis J., Kenrick K. C. Polyacrylamide gel-electrophoresis across a molecular sieve gradient. Nature. 1967 Jun 24;214(5095):1334–1336. doi: 10.1038/2141334a0. [DOI] [PubMed] [Google Scholar]
  21. Meyer O., Rajagopalan K. V. Molybdopterin in carbon monoxide oxidase from carboxydotrophic bacteria. J Bacteriol. 1984 Feb;157(2):643–648. doi: 10.1128/jb.157.2.643-648.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Poels P. A., Groen B. W., Duine J. A. NAD(P)+-independent aldehyde dehydrogenase from Pseudomonas testosteroni. A novel type of molybdenum-containing hydroxylase. Eur J Biochem. 1987 Aug 3;166(3):575–579. doi: 10.1111/j.1432-1033.1987.tb13552.x. [DOI] [PubMed] [Google Scholar]
  23. Rajagopalan K. V., Handler P. Purification and properties of chicken liver xanthine dehydrogenase. J Biol Chem. 1967 Sep 25;242(18):4097–4107. [PubMed] [Google Scholar]
  24. Tate R. L., Ensign J. C. A new species of Arthrobacter which degrades picolinic acid. Can J Microbiol. 1974 May;20(5):691–694. doi: 10.1139/m74-105. [DOI] [PubMed] [Google Scholar]
  25. Tate R. L., Ensign J. C. Picolinic acid hydroxylase of Arthrobacter picolinophilus. Can J Microbiol. 1974 May;20(5):695–702. doi: 10.1139/m74-106. [DOI] [PubMed] [Google Scholar]
  26. Trudgill P. W. The metabolism of 2-furoic acid by Pseudomanas F2. Biochem J. 1969 Jul;113(4):577–587. doi: 10.1042/bj1130577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Turner N., Barata B., Bray R. C., Deistung J., Le Gall J., Moura J. J. The molybdenum iron-sulphur protein from Desulfovibrio gigas as a form of aldehyde oxidase. Biochem J. 1987 May 1;243(3):755–761. doi: 10.1042/bj2430755. [DOI] [PMC free article] [PubMed] [Google Scholar]

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