J. Bacteriol., Sep 1996, 5249-5256, Vol 178, No. 17
Copyright © 1996, American Society for Microbiology

Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (MpcI): sequence analysis and biochemical properties of a third family of extradiol dioxygenases

EL Spence, M Kawamukai, J Sanvoisin, H Braven and TD Bugg
Department of Chemistry, University of Southampton, United Kingdom.

The nucleotide sequence of the Escherichia coli mhpB gene, encoding 2,3- dihydroxyphenylpropionate 1,2-dioxygenase, was determined by sequencing of a 3.1-kb fragment of DNA from Kohara phage 139. The inferred amino acid sequence showed 58% sequence identity with the sequence of an extradiol dioxygenase, MpcI, from Alcaligenes eutrophus and 10 to 20% sequence identity with protocatechuate 4,5-dioxygenase from Pseudomonas paucimobilis, with 3,4-dihydroxyphenylacetate 2,3-dioxygenase from E. coli, and with human 3-hydroxyanthranilate dioxygenase. Sequence similarity between the N- and C-terminal halves of this new family of dioxygenases was detected, with conserved histidine residues in the N- terminal domain. A model is proposed to account for the relationship between this family of enzymes and other extradiol dioxygenases. The A. eutrophus MpcI enzyme was expressed in E. coli, purified, and characterized as a protein with a subunit size of 33.8 kDa. Purified MhpB and MpcI showed similar substrate specificities for a range of 3- substituted catechols, and evidence for essential histidine and cysteine residues in both enzymes was obtained.

This article has been cited by other articles:

• Li, X., Guo, M., Fan, J., Tang, W., Wang, D., Ge, H., Rong, H., Teng, M., Niu, L., Liu, Q., Hao, Q. (2006). Crystal structure of 3-hydroxyanthranilic acid 3,4-dioxygenase from Saccharomyces cerevisiae: A special subgroup of the type III extradiol dioxygenases. Protein Sci. 15: 761-773 [Abstract] [Full Text]  
• Nogales, J., Canales, A., Jimenez-Barbero, J., Garcia, J. L., Diaz, E. (2005). Molecular Characterization of the Gallate Dioxygenase from Pseudomonas putida KT2440: THE PROTOTYPE OF A NEW SUBGROUP OF EXTRADIOL DIOXYGENASES. J. Biol. Chem. 280: 35382-35390 [Abstract] [Full Text]  
• Viggiani, A., Siani, L., Notomista, E., Birolo, L., Pucci, P., Di Donato, A. (2004). The Role of the Conserved Residues His-246, His-199, and Tyr-255 in the Catalysis of Catechol 2,3-Dioxygenase from Pseudomonas stutzeri OX1. J. Biol. Chem. 279: 48630-48639 [Abstract] [Full Text]  
• Ishida, T., Tanaka, H., Horiike, K. (2004). Quantitative Structure-Activity Relationship for the Cleavage of C3/C4-Substituted Catechols by a Prototypal Extradiol Catechol Dioxygenase with Broad Substrate Specificity. J Biochem 135: 721-730 [Abstract] [Full Text]  
• Vetting, M. W., Wackett, L. P., Que, L. Jr., Lipscomb, J. D., Ohlendorf, D. H. (2004). Crystallographic Comparison of Manganese- and Iron-Dependent Homoprotocatechuate 2,3-Dioxygenases. J. Bacteriol. 186: 1945-1958 [Abstract] [Full Text]  
• Christinet, L., Burdet, F. X., Zaiko, M., Hinz, U., Zryd, J.-P. (2004). Characterization and Functional Identification of a Novel Plant 4,5-Extradiol Dioxygenase Involved in Betalain Pigment Biosynthesis in Portulaca grandiflora. Plant Physiol. 134: 265-274 [Abstract] [Full Text]  
• Muraki, T., Taki, M., Hasegawa, Y., Iwaki, H., Lau, P. C. K. (2003). Prokaryotic Homologs of the Eukaryotic 3-Hydroxyanthranilate 3,4-Dioxygenase and 2-Amino-3-Carboxymuconate-6-Semialdehyde Decarboxylase in the 2-Nitrobenzoate Degradation Pathway of Pseudomonas fluorescens Strain KU-7. Appl. Environ. Microbiol. 69: 1564-1572 [Abstract] [Full Text]  
• Diaz, E., Ferrandez, A., Prieto, M. A., Garcia, J. L. (2001). Biodegradation of Aromatic Compounds by Escherichia coli. Microbiol. Mol. Biol. Rev. 65: 523-569 [Abstract] [Full Text]  
• Park, H.-S., Kim, H.-S. (2001). Genetic and Structural Organization of the Aminophenol Catabolic Operon and Its Implication for Evolutionary Process. J. Bacteriol. 183: 5074-5081 [Abstract] [Full Text]  
• Providenti, M. A., Mampel, J., MacSween, S., Cook, A. M., Wyndham, R. C. (2001). Comamonas testosteroni BR6020 possesses a single genetic locus for extradiol cleavage of protocatechuate. Microbiology 147: 2157-2167 [Abstract] [Full Text]  
• Donald, L. J., Hosfield, D. J., Cuvelier, S. L., Ens, W., Standing, K. G., Duckworth, H. W. (2001). Mass spectrometric study of the Escherichia coli repressor proteins, IcIR and GcIR, and their complexes with DNA. Protein Sci. 10: 1370-1380 [Abstract] [Full Text]  
• Arai, H., Yamamoto, T., Ohishi, T., Shimizu, T., Nakata, T., Kudo, T. (1999). Genetic organization and characteristics of the 3-(3-hydroxyphenyl)propionic acid degradation pathway of Comamonas testosteroni TA441. Microbiology 145: 2813-2820 [Abstract] [Full Text]  
• Riegert, U., Heiss, G., Kuhm, A. E., Müller, C., Contzen, M., Knackmuss, H.-J., Stolz, A. (1999). Catalytic Properties of the 3-Chlorocatechol-Oxidizing 2,3-Dihydroxybiphenyl 1,2-Dioxygenase from Sphingomonas sp. Strain BN6. J. Bacteriol. 181: 4812-4817 [Abstract] [Full Text]  
• Laurie, A. D., Lloyd-Jones, G. (1999). The phn Genes of Burkholderia sp. Strain RP007 Constitute a Divergent Gene Cluster for Polycyclic Aromatic Hydrocarbon Catabolism. J. Bacteriol. 181: 531-540 [Abstract] [Full Text]  
• Vaillancourt, F. H., Han, S., Fortin, P. D., Bolin, J. T., Eltis, L. D. (1998). Molecular Basis for the Stabilization and Inhibition of 2,3-Dihydroxybiphenyl 1,2-Dioxygenase by t-Butanol. J. Biol. Chem. 273: 34887-34895 [Abstract] [Full Text]  
• Ferrandez, A., Minambres, B., Garcia, B., Olivera, E. R., Luengo, J. M., Garcia, J. L., Diaz, E. (1998). Catabolism of Phenylacetic Acid in Escherichia coli. CHARACTERIZATION OF A NEW AEROBIC HYBRID PATHWAY. J. Biol. Chem. 273: 25974-25986 [Abstract] [Full Text]  
• Berlyn, M. K. B. (1998). Linkage Map of Escherichia coli K-12, Edition 10: The Traditional Map. Microbiol. Mol. Biol. Rev. 62: 814-984 [Abstract] [Full Text]  
• Peng, X., Egashira, T., Hanashiro, K., Masai, E., Nishikawa, S., Katayama, Y., Kimbara, K., Fukuda, M. (1998). Cloning of a Sphingomonas paucimobilis SYK-6 Gene Encoding a Novel Oxygenase That Cleaves Lignin-Related Biphenyl and Characterization of the Enzyme. Appl. Environ. Microbiol. 64: 2520-2527 [Abstract] [Full Text]  
• Díaz, E., Ferrández, A., García, J. L. (1998). Characterization of the hca Cluster Encoding the Dioxygenolytic Pathway for Initial Catabolism of 3-Phenylpropionic Acid in Escherichia coli K-12. J. Bacteriol. 180: 2915-2923 [Abstract] [Full Text]  
• Blattner, F. R., Plunkett III, G., Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). The Complete Genome Sequence of Escherichia coli K-12. Science 277: 1453-1462 [Abstract] [Full Text]  
• Takenaka, S., Murakami, S., Shinke, R., Hatakeyama, K., Yukawa, H., Aoki, K. (1997). Novel Genes Encoding 2-Aminophenol 1,6-Dioxygenase from Pseudomonas Species AP-3 Growing on 2-Aminophenol and Catalytic Properties of the Purified Enzyme. J. Biol. Chem. 272: 14727-14732 [Abstract] [Full Text]