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Literature summary for extracted from

  • Patil, D.N.; Tomar, S.; Sylvestre, M.; Kumar, P.
    Expression, purification, crystallization and preliminary crystallographic studies of cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase from Pandoraea pnomenusa B-356 (2010), Acta Crystallogr. Sect. F, 66, 1517-1520.
    View publication on PubMedView publication on EuropePMC


Cloned (Comment) Organism
gene bphB, overexpression of N-terminally His-tagged BphB in Escherichia coli strain BL21 (DE3) Comamonas testosteroni

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant detagged BphB, sitting drop vapour diffusion method, 0.001 ml of 10 mg/ml protein in 20 mM HEPES, pH 8.0, 10% glycerol, and 300 mM NaCl, are mixed with 0.001 ml of reservoir solution containing 0.2 M sodium malonate, pH 6.0, and 20% PEG 3350, 20% glycerol is used as cryoprotectant, X-ray diffractiuon structure determination and analysis at 2.8 A resolution Comamonas testosteroni

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
x * 29400, about Comamonas testosteroni


Organism UniProt Comment Textmining
Comamonas testosteroni Q46381 gene bphB
Comamonas testosteroni B-356 Q46381 gene bphB

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged BphB from Escherichia coli strain BL21 (DE3) to homogeneity by niockel affinity chromatography, the His-tag is cleaved off followed by ultrafiltration and gel filtration Comamonas testosteroni


Subunits Comment Organism
? x * 29400, about Comamonas testosteroni


Synonyms Comment Organism
biphenyl dihydrodiol dehydrogenase
Comamonas testosteroni
Comamonas testosteroni
Comamonas testosteroni
Comamonas testosteroni
More the enzyme belongs to the short-chain alcohol dehydrogenase/reductase, SDR, family Comamonas testosteroni


Cofactor Comment Organism Structure
NAD+ required Comamonas testosteroni