biphenyl-2,3-diol 1,2-dioxygenase [EC:1.13.11.39]

PMID:8428946

Eltis LD, Hofmann B, Hecht HJ, Lunsdorf H, Timmis KN

Purification and crystallization of 2,3-dihydroxybiphenyl 1,2-dioxygenase.

J Biol Chem 268:2727-32 (1993)

[bxe:Bxe_C1191]

PMID:17142386

Vezina J, Barriault D, Sylvestre M

Family shuffling of soil DNA to change the regiospecificity of Burkholderia xenovorans LB400 biphenyl dioxygenase.

J Bacteriol 189:779-88 (2007)
DOI:10.1128/JB.01267-06

Oxidoreductases;
Acting on single donors with incorporation of molecular oxygen (oxygenases);
With incorporation of two atoms of oxygen

biphenyl-2,3-diol:oxygen 1,2-oxidoreductase (ring-opening)

biphenyl-2,3-diol + O2 = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate [RN:R03462]

R03462;
(other) R05245 R07827

biphenyl-2,3-diol [CPD:C02526];
O2 [CPD:C00007]

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.

EC 1.13.11.39 created 1989

1  [PMID:8428946]

Eltis LD, Hofmann B, Hecht HJ, Lunsdorf H, Timmis KN

Purification and crystallization of 2,3-dihydroxybiphenyl 1,2-dioxygenase.

J. Biol. Chem. 268 (1993) 2727-32.

[bxe:Bxe_C1191]

2  [PMID:11293547]

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 (2001) 269-79.

[ack:C380_15945]

3  [PMID:12672826]

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 (2003) 21483-92.

[ag:BAC23089]

4  [PMID:15715866]

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 (2005) 635-45.

5  [PMID:12728990]

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 (2003) 300-7.