Literature summary for 1.3.1.56 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.

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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

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

Subunits	Comment	Organism
tetramer	-	Comamonas testosteroni

Synonyms

Synonyms	Comment	Organism
biphenyl dehydrogenase	-	Comamonas testosteroni
BphBB-356	-	Comamonas testosteroni

Cofactor

Cofactor	Comment	Organism	Structure
NADH	-	Comamonas testosteroni

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Release 2023.1 (January 2023)