EC 1.13.11.39 - Biphenyl-2,3-diol 1,2-dioxygenase

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IntEnz Enzyme Nomenclature
EC 1.13.11.39

Names

Accepted name:
biphenyl-2,3-diol 1,2-dioxygenase
Other names:
2,3-dihydroxybiphenyl dioxygenase
biphenyl-2,3-diol dioxygenase
BphC
biphenyl-2,3-diol:oxygen 1,2-oxidoreductase (decyclizing)
Systematic name:
biphenyl-2,3-diol:oxygen 1,2-oxidoreductase (ring-opening)

Reaction

Cofactor

Comments:

Contains Fe2+ or Mn2+ [3]. This enzyme participates in the degradation pathway of biphenyl and PCB (poly chlorinated biphenyls), and catalyses the first ring cleavage step by incorporating two oxygen atoms into the catechol ring formed by EC 1.3.1.56, cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase. The enzyme from the bacterium Burkholderia xenovorans LB400 can also process catechol, 3-methylcatechol, and 4-methylcatechol, but less efficiently [1]. The enzyme from the carbazole-degrader Pseudomonas resinovorans strain CA10 also accepts 2'-aminobiphenyl-2,3-diol [5]. The enzyme from Ralstonia sp. SBUG 290 can also accept 1,2-dihydroxydibenzofuran and 1,2-dihydroxynaphthalene [4]. The enzyme is strongly inhibited by the substrate [1]. Not identical with EC 1.13.11.2 catechol 2,3-dioxygenase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UM-BBD , UniPathway
Protein domains and families: PROSITE:PDOC00078
Structural data: CSA , EC2PDB
Gene Ontology: GO:0018583
CAS Registry Number: 102784-29-2
UniProtKB/Swiss-Prot:

References

  1. Eltis, L. D., Hofmann, B., Hecht, H. J., Lunsdorf, H., Timmis, K. N.
    Purification and crystallization of 2,3-dihydroxybiphenyl 1,2-dioxygenase.
    J. Biol. Chem. 268: 2727-2732 (1993). [PMID: 8428946]
  2. Uragami, Y., Senda, T., Sugimoto, K., Sato, N., Nagarajan, V., Masai, E., Fukuda, M., Mitsu, Y.
    Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase.
    J. Inorg. Biochem. 83: 269-279 (2001). [PMID: 11293547]
  3. Hatta, T., Mukerjee-Dhar, G., Damborsky, J., Kiyohara, H., Kimbara, K.
    Characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from a polychlorinated biphenyl- and naphthalene-degrading Bacillus sp. JF8.
    J. Biol. Chem. 278: 21483-21492 (2003). [PMID: 12672826]
  4. Wesche, J., Hammer, E., Becher, D., Burchhardt, G., Schauer, F.
    The bphC gene-encoded 2,3-dihydroxybiphenyl-1,2-dioxygenase is involved in complete degradation of dibenzofuran by the biphenyl-degrading bacterium Ralstonia sp. SBUG 290.
    J. Appl. Microbiol. 98: 635-645 (2005). [PMID: 15715866]
  5. Iwata, K., Nojiri, H., Shimizu, K., Yoshida, T., Habe, H., Omori, T.
    Expression, purification, and characterization of 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase from carbazole-degrader Pseudomonas resinovorans strain CA10.
    Biosci. Biotechnol. Biochem. 67: 300-307 (2003). [PMID: 12728990]

[EC 1.13.11.39 created 1989, modified 2010]