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
RBDALSL_1078
PFUWKF707C_16270(bphC)
PALLUYA_07070
MSHEMAALD49_00930
BXEBxe_C1191(bphC)
BXBDR64_8614(bphC)
PANXOYT13_24880(bphC)
PNAPnap_4146
ACKC380_15945(bphC)
CTESO987_08235
RBUPG1C_07515
ABREpbN1_20550(bphC)
AZIAzCIB_4412
AZDCDA09_21445
CAULKCG34_11050
THAACFI11_19390
SPFDSPYCA_3467(bphC1)
SPHYCHN51_18345
BKWBkAM31D_08390(bphC)
GJFM493_00030(bphC)
LYGC1N55_08055
PRDF7984_08665 F7984_12045
NDTL1999_08985 L1999_09010 L1999_17535
PNPIJ22_06970
SIVSSIL_3694
SSILSOLI23_19585
PLIQQWY22_10485
PSHEQWY16_10585
PSHXQWY21_10880
RHARHA1_ro08055(bphC1)
ROPROP_pROB02-01620(bnzC)
RKOJWS14_43435
ROZCBI38_14170
RPSKJWS13_01620(bphC)
RGORNMQ04_17790
RHOUKZJ41_10505
RHOWA4U64_15240
SSOII1A49_09540
AGRAAGRA3207_003621
ARHDVSH64_21275
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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