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Literature summary for extracted from

  • Hülsmeyer, M.; Hecht, H.J.; Niefind, K.; Hofer, B.; Eltis, L.D.; Timmis, K.N.; Schomburg, D.
    Crystal structure of cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase from a PCB degrader at 2.0 A resolution (1998), Protein Sci., 7, 1286-1293.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
the crystal structure of the NAD+-enzyme complex is determined by molecular replacement and refined to an R-value of 17.9% at 2.0 A Pseudomonas sp.


Organism UniProt Comment Textmining
Pseudomonas sp. P47227


Reaction Comment Organism Reaction ID
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ = biphenyl-2,3-diol + NADH + H+ a two-step reaction mechanism is proposed Pseudomonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ modeling studies indicate that the substrate is bound in a deep hydrophobic cleft close to the nicotinamide moiety of the NAD+ cofactor. These studies further suggest that Asn143 is a key determinant of substrate specificity Pseudomonas sp. biphenyl-2,3-diol + NADH + H+


Synonyms Comment Organism
Pseudomonas sp.
Pseudomonas sp.

General Information

General Information Comment Organism
physiological function the enzyme is involved in the aerobic biodegradation of polychlorinated biphenyls Pseudomonas sp.