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Literature summary for 1.14.12.18 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
Search for more literature for 1.14.12.18

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Comamonas testosteroni Q46372 alpha-subunit of biphenyl dioxygenase; B-356
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
4,4'-dichlorobiphenyl + NADH + H+ + O2
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 Comamonas testosteroni 2,3-dihydroxy-4,4'-dichlorobiphenyl + NAD+
-
 ?
biphenyl + NADH + H+ + O2
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 Comamonas testosteroni 2,3-dihydro-dihydroxybiphenyl + NAD+
-
 ?

Subunits

Subunits Comment Organism
? 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

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

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Comamonas testosteroni