Literature summary 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.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.14.12.18	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
1.14.12.18	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

EC Number	Protein Variants	Comment	Organism
1.14.12.18	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
1.14.12.18	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

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

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Release 2023.1 (January 2023)