KEGG   ENZYME: 1.13.11.39
Entry
EC 1.13.11.39               Enzyme                                 
Name
biphenyl-2,3-diol 1,2-dioxygenase;
2,3-dihydroxybiphenyl dioxygenase;
biphenyl-2,3-diol dioxygenase;
bphC (gene name);
biphenyl-2,3-diol:oxygen 1,2-oxidoreductase (decyclizing)
Class
Oxidoreductases;
Acting on single donors with incorporation of molecular oxygen (oxygenases);
With incorporation of two atoms of oxygen
Sysname
biphenyl-2,3-diol:oxygen 1,2-oxidoreductase (ring-opening)
Reaction(IUBMB)
biphenyl-2,3-diol + O2 = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate [RN:R03462]
Reaction(KEGG)
R03462;
(other) R05245 R07827
Substrate
biphenyl-2,3-diol [CPD:C02526];
O2 [CPD:C00007]
Product
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate [CPD:C01273]
Comment
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.
History
EC 1.13.11.39 created 1989
Pathway
ec00361  Chlorocyclohexane and chlorobenzene degradation
ec00621  Dioxin degradation
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K00462  biphenyl-2,3-diol 1,2-dioxygenase
Genes
PSDDSC_09355
BXEBxe_C1191(bphC)
BXBDR64_8614(bphC)
ACKC380_15945(bphC)
CTESO987_08235
ABREpbN1_20550(bphC)
CAULKCG34_11050
GJFM493_00030(bphC)
PNPIJ22_06970
SIVSSIL_3694
SSILSOLI23_19585
RHARHA1_ro08055(bphC1)
ROPROP_pROB02-01620(bnzC)
RKOJWS14_43435
ROZCBI38_14170
SSOII1A49_09540
AGRAAGRA3207_003621
CWOCwoe_0444
 » show all
Reference
1  [PMID:8428946]
  Authors
Eltis LD, Hofmann B, Hecht HJ, Lunsdorf H, Timmis KN
  Title
Purification and crystallization of 2,3-dihydroxybiphenyl 1,2-dioxygenase.
  Journal
J Biol Chem 268:2727-32 (1993)
  Sequence
[bxe:Bxe_C1191]
Reference
2  [PMID:11293547]
  Authors
Uragami Y, Senda T, Sugimoto K, Sato N, Nagarajan V, Masai E, Fukuda M, Mitsu Y
  Title
Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase.
  Journal
J Inorg Biochem 83:269-79 (2001)
DOI:10.1016/S0162-0134(00)00172-0
  Sequence
Reference
3  [PMID:12672826]
  Authors
Hatta T, Mukerjee-Dhar G, Damborsky J, Kiyohara H, Kimbara K
  Title
Characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from a polychlorinated biphenyl- and naphthalene-degrading Bacillus sp. JF8.
  Journal
J Biol Chem 278:21483-92 (2003)
DOI:10.1074/jbc.M210240200
  Sequence
Reference
4  [PMID:15715866]
  Authors
Wesche J, Hammer E, Becher D, Burchhardt G, Schauer F
  Title
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.
  Journal
J Appl Microbiol 98:635-45 (2005)
DOI:10.1111/j.1365-2672.2004.02489.x
Reference
5  [PMID:12728990]
  Authors
Iwata K, Nojiri H, Shimizu K, Yoshida T, Habe H, Omori T
  Title
Expression, purification, and characterization of 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase from carbazole-degrader Pseudomonas resinovorans strain CA10.
  Journal
Biosci Biotechnol Biochem 67:300-7 (2003)
DOI:10.1271/bbb.67.300
Other DBs
ExplorEnz - The Enzyme Database: 1.13.11.39
IUBMB Enzyme Nomenclature: 1.13.11.39
ExPASy - ENZYME nomenclature database: 1.13.11.39
UM-BBD (Biocatalysis/Biodegradation Database): 1.13.11.39
BRENDA, the Enzyme Database: 1.13.11.39
CAS: 103679-58-9

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