Skip to main content
PMC home page
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1995 Aug;61(8):3169–3171. doi: 10.1128/aem.61.8.3169-3171.1995

Cloning, nucleotide sequencing, and expression of an opine dehydrogenase gene from Arthrobacter sp. strain 1C.

T Dairi 1, Y Asano 1
PMCID: PMC167592  PMID: 7487048

Abstract

The gene coding for opine dehydrogenase from Arthrobacter sp. strain 1C was cloned onto plasmid pBluescript KS(-), and the nucleotide sequence of the 1,077-bp open reading frame consisting of 359 codons was identified as the odh gene. Transformed Escherichia coli cells overproduced NAD+-dependent opine dehydrogenase under control of the promoter of the lac gene on pBluescript KS(-).

Full Text

The Full Text of this article is available as a PDF (257.0 KB).

Selected References

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

  1. Asano Y., Nakazawa A., Endo K. Novel phenylalanine dehydrogenases from Sporosarcina ureae and Bacillus sphaericus. Purification and characterization. J Biol Chem. 1987 Jul 25;262(21):10346–10354. [PubMed] [Google Scholar]
  2. Asano Y., Yamaguchi K., Kondo K. A new NAD+-dependent opine dehydrogenase from Arthrobacter sp. strain 1C. J Bacteriol. 1989 Aug;171(8):4466–4471. doi: 10.1128/jb.171.8.4466-4471.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Britton K. L., Baker P. J., Engel P. C., Rice D. W., Stillman T. J. Evolution of substrate diversity in the superfamily of amino acid dehydrogenases. Prospects for rational chiral synthesis. J Mol Biol. 1993 Dec 20;234(4):938–945. doi: 10.1006/jmbi.1993.1647. [DOI] [PubMed] [Google Scholar]
  4. Britton K. L., Baker P. J., Rice D. W., Stillman T. J. Structural relationship between the hexameric and tetrameric family of glutamate dehydrogenases. Eur J Biochem. 1992 Nov 1;209(3):851–859. doi: 10.1111/j.1432-1033.1992.tb17357.x. [DOI] [PubMed] [Google Scholar]
  5. De Greve H., Dhaese P., Seurinck J., Lemmers M., Van Montagu M., Schell J. Nucleotide sequence and transcript map of the Agrobacterium tumefaciens Ti plasmid-encoded octopine synthase gene. J Mol Appl Genet. 1982;1(6):499–511. [PubMed] [Google Scholar]
  6. Depicker A., Stachel S., Dhaese P., Zambryski P., Goodman H. M. Nopaline synthase: transcript mapping and DNA sequence. J Mol Appl Genet. 1982;1(6):561–573. [PubMed] [Google Scholar]
  7. Donkersloot J. A., Thompson J. Cloning, expression, sequence analysis, and site-directed mutagenesis of the Tn5306-encoded N5-(carboxyethyl)ornithine synthase from Lactococcus lactis K1. J Biol Chem. 1995 May 19;270(20):12226–12234. doi: 10.1074/jbc.270.20.12226. [DOI] [PubMed] [Google Scholar]
  8. Feeney R., Clarke A. R., Holbrook J. J. A single amino acid substitution in lactate dehydrogenase improves the catalytic efficiency with an alternative coenzyme. Biochem Biophys Res Commun. 1990 Jan 30;166(2):667–672. doi: 10.1016/0006-291x(90)90861-g. [DOI] [PubMed] [Google Scholar]
  9. Firmin J. L., Stewart I. M., Wilson K. E. N2-(1-carboxyethyl)methionine. A 'pseudo-opine' in octopine-type crown-gall tumours. Biochem J. 1985 Dec 1;232(2):431–434. doi: 10.1042/bj2320431. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Garmyn D., Ferain T., Bernard N., Hols P., Delcour J. Cloning, nucleotide sequence, and transcriptional analysis of the Pediococcus acidilactici L-(+)-lactate dehydrogenase gene. Appl Environ Microbiol. 1995 Jan;61(1):266–272. doi: 10.1128/aem.61.1.266-272.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Okazaki N., Hibino Y., Asano Y., Ohmori M., Numao N., Kondo K. Cloning and nucleotide sequencing of phenylalanine dehydrogenase gene of Bacillus sphaericus. Gene. 1988 Mar 31;63(2):337–341. doi: 10.1016/0378-1119(88)90537-9. [DOI] [PubMed] [Google Scholar]
  12. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Schrell A., Schröder J. Characterization of a nopaline-induced gene for a 40 kDa protein in the nopaline catabolic (noc) region of Ti plasmid pTiC58. Biochim Biophys Acta. 1993 Sep 23;1174(3):303–304. doi: 10.1016/0167-4781(93)90204-q. [DOI] [PubMed] [Google Scholar]
  14. Takada H., Yoshimura T., Ohshima T., Esaki N., Soda K. Thermostable phenylalanine dehydrogenase of Thermoactinomyces intermedius: cloning, expression, and sequencing of its gene. J Biochem. 1991 Mar;109(3):371–376. doi: 10.1093/oxfordjournals.jbchem.a123388. [DOI] [PubMed] [Google Scholar]
  15. Thompson J., Donkersloot J. A. N-(carboxyalkyl)amino acids: occurrence, synthesis, and functions. Annu Rev Biochem. 1992;61:517–557. doi: 10.1146/annurev.bi.61.070192.002505. [DOI] [PubMed] [Google Scholar]
  16. Thompson J., Miller S. P. N5-(1-carboxyethyl)ornithine and related [N-carboxyalkyl]-amino acids: structure, biosynthesis, and function. Adv Enzymol Relat Areas Mol Biol. 1991;64:317–399. doi: 10.1002/9780470123102.ch7. [DOI] [PubMed] [Google Scholar]
  17. Thompson J. N5-(L-1-carboxyethyl)-L-ornithine:NADP+ oxidoreductase from Streptococcus lactis. Purification and partial characterization. J Biol Chem. 1989 Jun 5;264(16):9592–9601. [PubMed] [Google Scholar]

Articles from Applied and Environmental Microbiology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES