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Literature summary for 1.14.12.18 extracted from

  • Cao, Y.M.; Xu, L.; Jia, L.Y.
    Analysis of PCBs degradation abilities of biphenyl dioxygenase derived from Enterobacter sp. LY402 by molecular simulation (2011), New Biotechnol., 29, 90-98.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
biphenyl + NADH + H+ + O2 Enterobacter sp.
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(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
?
biphenyl + NADH + H+ + O2 Enterobacter sp. LY402
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(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
?
additional information Enterobacter sp. the strain LY402 shows polychlorinated biphenyls degradation abilities of BphA1, molecular simulation and ligand docking studies, overview ?
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?
additional information Enterobacter sp. LY402 the strain LY402 shows polychlorinated biphenyls degradation abilities of BphA1, molecular simulation and ligand docking studies, overview ?
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?

Organism

Organism UniProt Comment Textmining
Enterobacter sp.
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isolated from polluted soil
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Enterobacter sp. LY402
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isolated from polluted soil
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
biphenyl + NADH + H+ + O2
-
Enterobacter sp. (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
?
biphenyl + NADH + H+ + O2
-
Enterobacter sp. LY402 (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
?
additional information the strain LY402 shows polychlorinated biphenyls degradation abilities of BphA1, molecular simulation and ligand docking studies, overview Enterobacter sp. ?
-
?
additional information the strain LY402 shows polychlorinated biphenyls degradation abilities of BphA1, molecular simulation and ligand docking studies, overview Enterobacter sp. LY402 ?
-
?

Subunits

Subunits Comment Organism
More three-dimensional model of LY402-BphA1, overview Enterobacter sp.

Synonyms

Synonyms Comment Organism
BDO
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Enterobacter sp.
BphA1
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Enterobacter sp.

General Information

General Information Comment Organism
additional information the alpha-subunit of the iron-sulfur protein of biphenyl 2,3-dioxygenase directly influences catalytic activities and substrate specificity, three-dimensional model of LY402-BphA1, overview. The number and subposition of chlorine substituents influence the polychlorinated biphenyls binding ability of BphA1 significantly. Ser283, Val287, Gly321 and Tyr384 residues in the active site of LY402-BphA1 show high variability, and the space limitation of the active site of BphA1 have negative influence on the polychlorinated biphenyls binding affinity of the enzyme Enterobacter sp.