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IUBMB Comments Catalyses the second step in the biphenyl degradation pathway in bacteria.
The taxonomic range for the selected organisms is: Comamonas testosteroni The enzyme appears in selected viruses and cellular organisms
Synonyms
biphenyl-2,3-dihydrodiol-2,3-dehydrogenase, b2,3d, cis-2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase, cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase, 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase, biphenyl dehydrogenase, 2,3-dihydroxy-4-phenylhexa-4,6-diene dehydrogenase, biphenyl-2,3-dihydrodiol 2,3-dehydrogenase, nad-dependent cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase,
more
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biphenyl dihydrodiol dehydrogenase
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cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase
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2,3-dihydro-2,3-dehydroxybiphenyl-2,3-dehydrogenase
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2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase
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2,3-dihydroxy-4-phenylhexa-4,6-diene dehydrogenase
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Biphenyl-2,3-dihydro-2,3-diol dehydrogenase
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biphenyl-2,3-dihydrodiol-2,3-dehydrogenase
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Biphenyl-cis-diol dehydrogenase
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cis-2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase
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additional information
the enzyme belongs to the short-chain alcohol dehydrogenase/reductase, SDR, family
additional information
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enzyme belongs to the short-chain alcohol dehydrogenase/reductase family
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cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ = biphenyl-2,3-diol + NADH + H+
catalytic triad is formed by the conserved residues SEr142, Tyr153, and Lys159
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cis-3-phenylcyclohexa-3,5-diene-1,2-diol:NAD+ oxidoreductase
Catalyses the second step in the biphenyl degradation pathway in bacteria.
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3,4-dihydro-3,4-dihydroxy-2,2',5,5'-tetrachlorobiphenyl + NAD+
3,4-dihydroxy-2,2',5,5'-tetrachlorobiphenyl + NADH
cis-1,2-dihydro-1,2-dihydroxynaphthalene + NAD+
? + NADH
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cis-2,3-dihydro-2,3-dihydroxybiphenyl + NAD+
2,3-dihydroxybiphenyl + NADH
2,2',5,5'-tetrachlorobiphenyl + NAD+
2,2',5,5'-tetrachloro-3,4-dihydroxybiphenyl + NADH
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cis-2,3-dihydro-2,3-dihydroxybiphenyl + NAD(P)+
2,3-dihydroxybiphenyl + NAD(P)H
cis-2,3-dihydro-2,3-dihydroxybiphenyl + NAD+
2,3-dihydroxybiphenyl + NADH
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
biphenyl-2,3-diol + NADH
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additional information
?
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3,4-dihydro-3,4-dihydroxy-2,2',5,5'-tetrachlorobiphenyl + NAD+
3,4-dihydroxy-2,2',5,5'-tetrachlorobiphenyl + NADH
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3,4-dihydro-3,4-dihydroxy-2,2',5,5'-tetrachlorobiphenyl + NAD+
3,4-dihydroxy-2,2',5,5'-tetrachlorobiphenyl + NADH
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cis-2,3-dihydro-2,3-dihydroxybiphenyl + NAD+
2,3-dihydroxybiphenyl + NADH
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cis-2,3-dihydro-2,3-dihydroxybiphenyl + NAD+
2,3-dihydroxybiphenyl + NADH
biphenyl degradation pathway
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cis-2,3-dihydro-2,3-dihydroxybiphenyl + NAD(P)+
2,3-dihydroxybiphenyl + NAD(P)H
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cis-2,3-dihydro-2,3-dihydroxybiphenyl + NAD(P)+
2,3-dihydroxybiphenyl + NAD(P)H
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second step of the metabolic pathway for the bacterial degradation of biphenyl
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cis-2,3-dihydro-2,3-dihydroxybiphenyl + NAD+
2,3-dihydroxybiphenyl + NADH
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cis-2,3-dihydro-2,3-dihydroxybiphenyl + NAD+
2,3-dihydroxybiphenyl + NADH
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biphenyl degradation pathway
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additional information
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enzyme catalyzes the second step in the biphenyl catabolic degradation pathway, substrate spectrum of the organism in vivo, overview
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additional information
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enzyme shows a broad substrate specificity
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3,4-dihydro-3,4-dihydroxy-2,2',5,5'-tetrachlorobiphenyl + NAD+
3,4-dihydroxy-2,2',5,5'-tetrachlorobiphenyl + NADH
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cis-1,2-dihydro-1,2-dihydroxynaphthalene + NAD+
? + NADH
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cis-2,3-dihydro-2,3-dihydroxybiphenyl + NAD+
2,3-dihydroxybiphenyl + NADH
biphenyl degradation pathway
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cis-2,3-dihydro-2,3-dihydroxybiphenyl + NAD(P)+
2,3-dihydroxybiphenyl + NAD(P)H
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second step of the metabolic pathway for the bacterial degradation of biphenyl
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cis-2,3-dihydro-2,3-dihydroxybiphenyl + NAD+
2,3-dihydroxybiphenyl + NADH
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biphenyl degradation pathway
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cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
biphenyl-2,3-diol + NADH
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additional information
?
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enzyme catalyzes the second step in the biphenyl catabolic degradation pathway, substrate spectrum of the organism in vivo, overview
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?
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additional information
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NADP+ is a poor cofactor, probably due to Asp at position 36
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NAD+
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NAD+
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essential cofactor for His-taggged enzyme
NAD+
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260fold preferred over NADP+
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1.5
3,4-dihydro-3,4-dihydroxy-2,2',5,5'-tetrachlorobiphenyl
with 2.5 mM NAD+
0.28
cis-1,2-dihydro-1,2-dihydroxynaphthalene
with 2.5 mM NAD+
0.0039
cis-2,3-dihydro-2,3-dihydroxybiphenyl
with 2.5 mM NAD+
0.073
2,3-dihydro-2,3,-dihydroxybiphenyl
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activity measured with 1 micromol NAD+ in the reaction mixture at pH 9.5 and 37°C
0.0031
cis-2,3-dihydro-2,3-dihydroxybiphenyl
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at pH 9 and 25°C
0.00024
NAD(P)+
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at pH 9 and 25°C
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0.123
3,4-dihydro-3,4-dihydroxy-2,2',5,5'-tetrachlorobiphenyl
with 2.5 mM NAD+
0.9
cis-1,2-dihydro-1,2-dihydroxynaphthalene
with 2.5 mM NAD+
0.38
cis-2,3-dihydro-2,3-dihydroxybiphenyl
with 2.5 mM NAD+
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17.4
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after purification at 25°C and pH 9
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9.5
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recombinant His-tagged enzyme
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UniProt
brenda
gene bphB
UniProt
brenda
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BPHB_COMTE
281
0
29350
Swiss-Prot
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123000
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native protein, gel filtration
29400
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4 * 29400, electrospray mass spectrometry
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tetramer
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tetramer
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4 * 29400, electrospray mass spectrometry
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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
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-20°C stable in 50% glycerol for months
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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
ammonium sulfate precipitation, DEAE-Sepharose chromatography, yield about 50 mg of enzyme/l of cell culture
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gene bphB, overexpression of N-terminally His-tagged BphB in Escherichia coli strain BL21 (DE3)
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Vedadi, M.; Barriault, D.; Sylvestre, M; Powlowski, J.
Active site residues of cis-2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase from Comamonas testosteroni strain B-356
Biochemistry
39
5028-5034
2000
Comamonas testosteroni
brenda
Sylvestre, M.; Hurtubise, Y.; Barriault, D.; Bergeron, J.; Ahmad, D.
Characterization of active recombinant 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase from Comamonas testosteroni B-356 and sequence of the encoding gene (bphB)
Appl. Environ. Microbiol.
62
2710-2715
1996
Comamonas testosteroni
brenda
Barriault, D.; Vedadi, M.; Powlowski, J.; Sylvestre, M.
cis-2,3-Dihydro-2,3-dihydroxybiphenyl dehydrogenase and cis-1,2-dihydro-1,2-dihydroxynaphathalene dehydrogenase catalyze dehydrogenation of the same range of substrates
Biochem. Biophys. Res. Commun.
260
181-187
1999
Burkholderia cepacia, Burkholderia cepacia LB400, Comamonas testosteroni (Q46381), Comamonas testosteroni
brenda
Sylvestre, M.
Genetically modified organisms to remediate polychlorinated biphenyls. Where do we stand?
Int. Biodeter. Biodegrad.
54
153-162
2004
Burkholderia sp., Burkholderia sp. LB400, Comamonas testosteroni
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brenda
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
Acta Crystallogr. Sect. F
66
1517-1520
2010
Comamonas testosteroni (Q46381), Comamonas testosteroni B-356 (Q46381)
brenda
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
J. Biol. Chem.
286
37011-37022
2011
Comamonas testosteroni (Q46381)
brenda