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Literature summary for 1.3.1.56 extracted from

  • Piccoli, S.; Musiani, F.; Giorgetti, A.
    Dynamic characterization and substrate binding of cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase - an enzyme used in bioremediation (2014), J. Mol. Model., 20, 2531 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis of PpBphB, PDB ID 3ZV5, overview Pandoraea pnomenusa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ Pandoraea pnomenusa
-
biphenyl-2,3-diol + NADH + H+
-
?
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ Pandoraea pnomenusa B-356
-
biphenyl-2,3-diol + NADH + H+
-
?

Organism

Organism UniProt Comment Textmining
Pandoraea pnomenusa
-
-
-
Pandoraea pnomenusa B-356
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
Pandoraea pnomenusa biphenyl-2,3-diol + NADH + H+
-
?
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
Pandoraea pnomenusa B-356 biphenyl-2,3-diol + NADH + H+
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 29400, functional form Pandoraea pnomenusa
More three-dimensional enzyme structure analysis, crystal structure analysis of PpBphB, PDB ID 3ZV5, molecular dynamics simulations, overview Pandoraea pnomenusa

Synonyms

Synonyms Comment Organism
BphB
-
Pandoraea pnomenusa
NAD-dependent cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase
-
Pandoraea pnomenusa

Cofactor

Cofactor Comment Organism Structure
NAD+ dependent on Pandoraea pnomenusa

General Information

General Information Comment Organism
evolution PbBphB is a member of the short-chain dehydrogenase/reductase (SRD) family Pandoraea pnomenusa
metabolism NAD-dependent cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase (BphB) catalyzes the second step of the PCB catabolic pathway in bacteria Pandoraea pnomenusa
additional information the pocket between strand beta6 and helix alpha8 is the substrate-binding region and corresponds to a disordered region (Leu199-Ser206) in the structures of the apo and binary forms, dynamic behavior of the substrate binding loop. In the holo form, BPY stabilizes the conformation of the binding loop by interacting through the aromatic rings of reaction product 2,3-dihydroxybiphenyl with Val207 and Pro208 residues. Ile204 makes a hydrophobic interaction with the NAD+ cofactor only in the holo simulation. The lack of the latter interaction in the apo and in the binary forms explains the extended mobility of this region in the other two binding states of the protein Pandoraea pnomenusa
physiological function the enzyme is the key enzyme in the biphenyl/polychlorinated biphenyl catabolic pathway Pandoraea pnomenusa