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Literature summary for 1.14.12.18 extracted from

  • Zielinski, M.; Backhaus, S.; Hofer, B.
    The principal determinants for the structure of the substrate-binding pocket are located within a central core of a biphenyl dioxygenase alpha subunit (2002), Microbiology, 148, 2439-2448.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
the construction of appropriate hybrid genes may be used as a general strategy to overcome problems in obtaining heterologous biphenyl dioxygenase activities in Escherichia coli or other host organisms Rhodococcus globerulus
the construction of appropriate hybrid genes may be used as a general strategy to overcome problems in obtaining heterologous biphenyl dioxygenase activities in Escherichia coli or other host organisms Burkholderia sp.

Protein Variants

Protein Variants Comment Organism
additional information generation of 8 chimeric enzyme systems that each consists of a hybrid hydroxylase alpha subunit (BphA1) containing segments from Burkholderia sp. strain LB400 and Rhodococcus globerulus P6, and of a hydroxylase beta subunit (BphA2), a ferredoxin (BphA3) and a ferredoxin reductase (BphA4) from strain LB400. All hybrid bphA1 genes are expressed at high levels. Seven of the resulting fusion subunits functionally interacts with the other polypeptides of the dioxygenase system to yield catalytically active enzymes.The construction of appropriate hybrid genes may be used as a general strategy to overcome problems in obtaining heterologous biphenyl dioxygenase activities in Escherichia coli or other host organisms Rhodococcus globerulus
additional information generation of 8 chimeric enzyme systems that each consists of a hybrid hydroxylase alpha subunit (BphA1) containing segments from Burkholderia sp. strain LB400 and Rhodococcus globerulus P6, and of a hydroxylase beta subunit (BphA2), a ferredoxin (BphA3) and a ferredoxin reductase (BphA4) from strain LB400. All hybrid bphA1 genes are expressed at high levels. Seven of the resulting fusion subunits functionally interacts with the other polypeptides of the dioxygenase system to yield catalytically active enzymes.The construction of appropriate hybrid genes may be used as a general strategy to overcome problems in obtaining heterologous biphenyl dioxygenase activities in Escherichia coli or other host organisms Burkholderia sp.

Organism

Organism UniProt Comment Textmining
Burkholderia sp.
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-
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Burkholderia sp. LB400
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-
-
Rhodococcus globerulus
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P6
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Rhodococcus globerulus P6
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P6
-