1.3.1.56: cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase
This is an abbreviated version!
For detailed information about cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase, go to the full flat file.
Word Map on EC 1.3.1.56
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1.3.1.56
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biphenyls
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dioxygenase
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polychlorinated
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testosteroni
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comamonas
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pnomenusa
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burkholderia
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pandoraea
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chlorinated
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chlorobiphenyls
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congener
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dehydrogenation
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toluene
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bpha1a2a3a4
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cis-dihydrodiols
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cepacia
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meta-cleavage
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dehydrogenases
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ortho-substituted
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putida
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2,2\',5,5\'-tetrachlorobiphenyl
- 1.3.1.56
- biphenyls
- dioxygenase
-
polychlorinated
- testosteroni
-
comamonas
- pnomenusa
-
burkholderia
-
pandoraea
-
chlorinated
-
chlorobiphenyls
-
congener
-
dehydrogenation
- toluene
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bpha1a2a3a4
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cis-dihydrodiols
- cepacia
-
meta-cleavage
- dehydrogenases
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ortho-substituted
- putida
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2,2\',5,5\'-tetrachlorobiphenyl
Reaction
Synonyms
2,3-dihydro-2,3-dehydroxybiphenyl-2,3-dehydrogenase, 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase, 2,3-dihydroxy-4-phenylhexa-4,6-diene dehydrogenase, B2,3D, BephB, biphenyl dehydrogenase, biphenyl dihydrodiol dehydrogenase, Biphenyl-2,3-dihydro-2,3-diol dehydrogenase, biphenyl-2,3-dihydrodiol 2,3-dehydrogenase, biphenyl-2,3-dihydrodiol-2,3-dehydrogenase, Biphenyl-cis-diol dehydrogenase, BphB, BphBB-356, BphBB356, cis-2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase, cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase, More, NAD-dependent cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase
ECTree
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Crystallization
Crystallization on EC 1.3.1.56 - cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase
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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
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
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