- 1) Ornston, L. N., Regulation of catabolic pathways in Pseudomonas. Bacteriol. Rev., 35, 87–116 (1971).
- 2) Maruyama, K., Purification and properties of γ-oxalomesaconate hydratase from Pseudomonas ochraceae grown with phthalate. Biochem. Biophys. Res. Commun., 128, 271–277 (1985).
- 3) Hara, H., Masai, E., Miyauchi, K., Katayama, Y., and Fukuda, M., Characterization of the 4-carboxy-4-hydroxy-2-oxoadipate aldolase gene and operon structure of the protocatechuate 4,5-cleavage pathway genes in Sphingomonas paucimobilis SYK-6. J. Bacteriol., 185, 41–50 (2003).
- 4) Maruyama, K., Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae grown on phthalate. J. Biochem., 108, 327–333 (1990).
- 5) Maruyama, K., Activation of Pseudomonas ochraceae 4-hydroxy-4-methyl-2-oxoglutarate aldolase by inorganic phosphate. J. Biochem., 108, 334–340 (1990).
- 6) Pollard, J. R., and Bugg, T. D., Purification, characterisation and reaction mechanism of monofunctional 2-hydroxypentadienoic acid hydratase from Escherichia coli. Eur. J. Biochem., 251, 98–106 (1998).
- 7) Flint, D. H., Emptage, M. H., Finnegan, M. G., Fu, W., and Johnson, M. K., The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase. J. Biol. Chem., 268, 14732–14742 (1993).
- 8) Maruyama, K., Isolation and identification of the reaction product of α-hydroxy-γ-carboxymuconic ε-semialdehyde dehydrogenase. J. Biochem., 86, 1671–1677 (1979).
- 9) Kersten, P. J., Dagley, S., Whittaker, J. W., Arciero, D. M., and Lipscomb, J. D., 2-pyrone-4,6-dicarboxylic acid, a catabolite of gallic acids in Pseudomonas species. J. Bacteriol., 152, 1154–1162 (1982).
- 10) Maruyama, K., Purification and properties of 2-pyrone-4,6-dicarboxylate hydrolase. J. Biochem., 93, 557–565 (1983).
- 11) Hara, H., Masai, E., Katayama, Y., and Fukuda, M., The 4-oxalomesaconate hydratase gene, involved in the protocatechuate 4,5-cleavage pathway, is essential to vanillate and syringate degradation in Sphingomonas paucimobilis SYK-6. J. Bacteriol., 182, 6950–6957 (2000).
- 12) Providenti, M. A., Mampel, J., MacSween, S., Cook, A. M., and Wyndham, R. C., Comamonas testosteroni BR6020 possesses a single genetic locus for extradiol cleavage of protocatechuate. Microbiol., 147, 2157–2167 (2001).
- 13) Eaton, R. W., Plasmid-encoded phthalate catabolic pathway in Arthrobacter keyseri 12B. J. Bacteriol., 183, 3689–3703 (2001).
- 14) Wattiau, P., Bastiaens, L., van Herwijnen, R., Daal, L., Parsons, J. R., Renard, M.-E., Springael, D., and Cornelis, G. R., Fluorene degradation by Sphingomonas sp. LB126 proceeds through protocatechuic acid: a genetic analysis. Res. Microbiol., 152, 861–872 (2001).
- 15) Larimer, F. W., Chain, P., Hauser, L., Lamerdin, J., Malfatti, S., Do, L., Land, M. L., Pelletier, D. A., Beatty, J. T., Lang, A. S., Tabita, F. R., Gibson, J. L., Hanson, T. E., Bobst, C., Torres, J. L. T., Peres, C., Harrison, F. H., Gibson, J., and Harwood, C. S., Complete genome sequence of the metabolically versatile photosynthetic bacterium Rhodopseudomonas palustris. Nat. Biotechnol., 22, 55–61 (2004).
- 16) Maruyama, K., Miwa, M., Tsujii, N., Nagai, T., Tomita, N., Harada, T., Sobajima, H., and Sugisaki, H., Cloning, sequencing, and expression of the gene encoding 4-hydroxy-4-methy-2-oxoglutarate aldolase from Pseudomonas ochraceae NGJ1. Biosci. Biotechnol. Biochem., 65, 2701–2709 (2001).
- 17) Maruyama, K., Shibayama, T., Ichikawa, A., Sakou, Y., Yamada, S., and Sugisaki, H., Cloning and characterization of the genes encoding enzymes for protocatechuate meta-degradation pathway of Pseudomonas ochraceae NGJ1. Biosci. Biotechnol. Biochem., 68, 1434–1441 (2004).
- 18) Sambrook, J., Fritsch, E. F., and Maniatis, T., “Molecular Cloning, a Laboratory Manual” 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor (1989).
- 19) Pearson, W. R., and Lipman, D. J., Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA, 85, 2444–2448 (1988).
- 20) Altschul, S. F., Madden, T. L., Schaffer, A. A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D. J., Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acid Res., 25, 3389–3402 (1997).
- 21) Thompson, J. D., Higgins, D. G., and Gibson, T. J., CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673–4680 (1994).
- 22) Shine, J., and Dalgarno, L., The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc. Natl. Acad. Sci. USA, 71, 1342–1346 (1974).
- 23) Hashimoto-Gotoh, T., Mizuno, T., Ogasahara, Y., and Nakagawa, M., An oligodeoxyribonucleotide-directed dual amber method for site-directed mutagenesis. Gene, 152, 271–275 (1995).
- 24) Vesterburg, O., Isoelectric focusing of proteins. Methods Enzymol., 22, 389–412 (1971).
- 25) Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193, 265–275 (1951).
- 26) Bennet, T. P., Membrane filtration for determining protein in the presence of interfering substances. Nature, 18, 1131–1132 (1967).
- 27) Riddle, P. W., Blakeley, R. L., and Zerner, B., Elleman’s reagent: 5,5′-dithiobis(2-nitrobenzoic acid): a reexamination. Anal. Biochem., 94, 75–81 (1979).
- 28) Hunt, J. B., Neece, S. H., and Grinsburg, A., The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase. Anal. Biochem., 146, 150–157 (1985).
- 29) Davis, B. J., Disc electrophoresis. II. Method and application to human serum proteins. Ann. NY Acad. Sci., 121, 404–427 (1964).
- 30) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London), 227, 680–685 (1970).
- 31) Sussman, J. L., Harel, M., Frolow, F., Oefner, C., Goldman, A., Toker, L., and Silman, I., Atomic structure of acetylcholinesterase from Torpede californica: a prototypic acetylcholine-binding protein. Science, 253, 872–879 (1991).
- 32) Laurell, H., Contreras, J. A., Castan, I., Langin, D., and Holm, C., Analysis of the psychrotolerant property of hormone-sensitive lipase through site-directed mutagenesis. Protein Eng., 13, 711–717 (2000).
- 33) Dixon, M., The determination of enzyme inhibitor constants. Biochem. J., 55, 170–171 (1953).
- 34) Hill, R. L., and Teipel, J. W., Fumarase and crotonase. Enzymes, 5, 539–571 (1971).
- 35) Sheridan, R. P., and Allen, L. C., The active site electrostatic potential of human carbonic anhydrase. J. Am. Chem. Soc., 103, 1544–1550 (1981).
Full access
Role of Cysteine Residues in 4-Oxalomesaconate Hydratase from Pseudomonas ochraceae NGJ1
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.
Related research
People also read lists articles that other readers of this article have read.
Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.
Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.