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Literature summary extracted from

  • Baig, M.S.; Manickam, N.
    Homology modeling and docking studies of Comamonas testosteroni B-356 biphenyl-2,3-dioxygenase involved in degradation of polychlorinated biphenyls (2010), Int. J. Biol. Macromol., 46, 47-53.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.12.18 Fe2+ coordination geometry of Fe-ion along with the oxygen and different polychlorinated biphenyl congeners Comamonas testosteroni

Organism

EC Number Organism UniProt Comment Textmining
1.14.12.18 Comamonas testosteroni Q46372 alpha-subunit of biphenyl dioxygenase; B-356
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.12.18 3,3'-dichlorobiphenyl + NADH + H+ + O2
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Comamonas testosteroni 5,6-dihydroxy-1-phenylcyclohexa-1,3-diene + 4,5-dihydroxy-1-phenylcyclohexa-1,2-diene + NAD+ + HCl
-
?
1.14.12.18 4,4'-dichlorobiphenyl + NADH + H+ + O2
-
Comamonas testosteroni 2,3-dihydroxy-4,4'-dichlorobiphenyl + NAD+
-
?
1.14.12.18 biphenyl + NADH + H+ + O2
-
Comamonas testosteroni 2,3-dihydro-dihydroxybiphenyl + NAD+
-
?

Subunits

EC Number Subunits Comment Organism
1.14.12.18 ? construction of a three-dimensional model of alpha-subunit of biphenyl dioxygenase (BphA). BphA active site is composed of two domains, the catalytic domain (residues 1-58 and 176-457) and the Rieske domain (residues 59–166). The active site pocket, which is lined mostly by hydrophobic residues (Phe227, Trp390, Phe 376, Asp386, Phe382 and Ala234) is located between the core beta-sheet and alpha-helices in the catalytic domain of the alpha-subunit Comamonas testosteroni

Synonyms

EC Number Synonyms Comment Organism
1.14.12.18 biphenyl dioxygenase
-
Comamonas testosteroni
1.14.12.18 biphenyl-2,3-dioxygenase
-
Comamonas testosteroni
1.14.12.18 BPDO
-
Comamonas testosteroni
1.14.12.18 BphA
-
Comamonas testosteroni

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.12.18 NADH
-
Comamonas testosteroni