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Literature summary for extracted from

  • Dhindwal, S.; Patil, D.N.; Mohammadi, M.; Sylvestre, M.; Tomar, S.; Kumar, P.
    Biochemical studies and ligand-bound structures of biphenyl dehydrogenase from Pandoraea pnomenusa strain B-356 reveal a basis for broad specificity of the enzyme (2011), J. Biol. Chem., 286, 37011-37022.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
the crystal structures of the apoenzyme, the binary complex with NAD+, and the ternary complexes with NAD-2,3-dihydroxybiphenyl and NAD+-4,4'-dihydroxybiphenyl are determined at 2.2-, 2.5-, 2.4-, and 2.1 A resolutions, respectively. A series of conformational changes in the substrate binding loop that occur during ligand binding are identified Comamonas testosteroni


Organism UniProt Comment Textmining
Comamonas testosteroni Q46381

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3,4-dihydro-3,4-dihydroxy-2,2',5,5'-tetrachlorobiphenyl + NAD+
Comamonas testosteroni 3,4-dihydroxy-2,2',5,5'-tetrachlorobiphenyl + NADH


Subunits Comment Organism
Comamonas testosteroni


Synonyms Comment Organism
biphenyl dehydrogenase
Comamonas testosteroni
Comamonas testosteroni


Cofactor Comment Organism Structure
Comamonas testosteroni