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.

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	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3,3'-dichlorobiphenyl + NADH + H+ + O2	-	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	-	Comamonas testosteroni	2,3-dihydroxy-4,4'-dichlorobiphenyl + NAD+	-	?
biphenyl + NADH + H+ + O2	-	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 59166). 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	-	Comamonas testosteroni
BphA	-	Comamonas testosteroni

Cofactor

Cofactor	Comment	Organism	Structure
NADH	-	Comamonas testosteroni

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)