Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1997 Apr;179(8):2761–2765. doi: 10.1128/jb.179.8.2761-2765.1997

Cloning, sequence, and properties of the soluble pyridine nucleotide transhydrogenase of Pseudomonas fluorescens.

C E French 1, B Boonstra 1, K A Bufton 1, N C Bruce 1
PMCID: PMC179029  PMID: 9098078

Abstract

The gene encoding the soluble pyridine nucleotide transhydrogenase (STH) of Pseudomonas fluorescens was cloned and expressed in Escherichia coli. STH is related to the flavoprotein disulfide oxidoreductases but lacks one of the conserved redox-active cysteine residues. The gene is highly similar to an E. coli gene of unknown function.

Full Text

The Full Text of this article is available as a PDF (636.4 KB).

Selected References

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

  1. Benen J. A., Van Berkel W. J., Van Dongen W. M., Müller F., De Kok A. Molecular cloning and sequence determination of the lpd gene encoding lipoamide dehydrogenase from Pseudomonas fluorescens. J Gen Microbiol. 1989 Jul;135(7):1787–1797. doi: 10.1099/00221287-135-7-1787. [DOI] [PubMed] [Google Scholar]
  2. Cohen P. T., Kaplan N. O. Purification and properties of the pyridine nucleotide transhydrogenase from Pseudomonas aeruginosa. J Biol Chem. 1970 Jun 10;245(11):2825–2836. [PubMed] [Google Scholar]
  3. Greer S., Perham R. N. Glutathione reductase from Escherichia coli: cloning and sequence analysis of the gene and relationship to other flavoprotein disulfide oxidoreductases. Biochemistry. 1986 May 6;25(9):2736–2742. doi: 10.1021/bi00357a069. [DOI] [PubMed] [Google Scholar]
  4. Gustafsson C., Warne S. R. Physical map of the oxyR-trmA region (minute 89.3) of the Escherichia coli chromosome. J Bacteriol. 1992 Dec;174(23):7878–7879. doi: 10.1128/jb.174.23.7878-7879.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Höjeberg B., Brodelius P., Rydström J., Mosbach K. Affinity chromatography and binding studies on immobilized 5'-monophosphate and adenosine 2',5'-bisphosphate of nicotinamide nucleotide transhydrogenase from Pseudomonas aeruginosa. Eur J Biochem. 1976 Jul 15;66(3):467–475. doi: 10.1111/j.1432-1033.1976.tb10571.x. [DOI] [PubMed] [Google Scholar]
  6. Jackson J. B. The proton-translocating nicotinamide adenine dinucleotide transhydrogenase. J Bioenerg Biomembr. 1991 Oct;23(5):715–741. doi: 10.1007/BF00785998. [DOI] [PubMed] [Google Scholar]
  7. Louie D. D., Kaplan N. O., McLean J. D. Allosteric effect of 2'-adenylic acid on the Pseudomonas pyridine nucleotide transhydrogenase. J Mol Biol. 1972 Oct 14;70(3):651–664. doi: 10.1016/0022-2836(72)90564-5. [DOI] [PubMed] [Google Scholar]
  8. McKie J. H., Douglas K. T. Evidence for gene duplication forming similar binding folds for NAD(P)H and FAD in pyridine nucleotide-dependent flavoenzymes. FEBS Lett. 1991 Feb 11;279(1):5–8. doi: 10.1016/0014-5793(91)80236-v. [DOI] [PubMed] [Google Scholar]
  9. Poole L. B., Claiborne A. The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid. J Biol Chem. 1989 Jul 25;264(21):12330–12338. [PubMed] [Google Scholar]
  10. Ross R. P., Claiborne A. Cloning, sequence and overexpression of NADH peroxidase from Streptococcus faecalis 10C1. Structural relationship with the flavoprotein disulfide reductases. J Mol Biol. 1991 Oct 5;221(3):857–871. doi: 10.1016/0022-2836(91)80180-3. [DOI] [PubMed] [Google Scholar]
  11. Voordouw G., van der Vies S. M., Eweg J. K., Veeger C., van Breemen J. F., van Bruggen E. F. Pyridine nucleotide transhydrogenase from Azotobacter vinelandii. Improved purification, physical properties and subunit arrangement in purified polymers. Eur J Biochem. 1980 Oct;111(2):347–355. doi: 10.1111/j.1432-1033.1980.tb04948.x. [DOI] [PubMed] [Google Scholar]
  12. Voordouw G., van der Vies S. M., Themmen A. P. Why are two different types of pyridine nucleotide transhydrogenase found in living organisms? Eur J Biochem. 1983 Apr 5;131(3):527–533. doi: 10.1111/j.1432-1033.1983.tb07293.x. [DOI] [PubMed] [Google Scholar]
  13. Wang Y., Moore M., Levinson H. S., Silver S., Walsh C., Mahler I. Nucleotide sequence of a chromosomal mercury resistance determinant from a Bacillus sp. with broad-spectrum mercury resistance. J Bacteriol. 1989 Jan;171(1):83–92. doi: 10.1128/jb.171.1.83-92.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Wermuth B., Kaplan N. O. Pyridine nucleotide transhydrogenase from Pseudomonas aeruginosa: purification by affinity chromatography and physicochemical properties. Arch Biochem Biophys. 1976 Sep;176(1):136–143. doi: 10.1016/0003-9861(76)90149-1. [DOI] [PubMed] [Google Scholar]
  15. Widmer F., Kaplan N. O. Pseudomonas aeruginosa transhydrogenase: affinity of substrates for the regulatory site and possible hysteretic behavior. Biochem Biophys Res Commun. 1977 Jun 20;76(4):1287–1292. doi: 10.1016/0006-291x(77)90995-0. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES