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Titolo:
Emergence of multifunctional oxygenase activities by random priming recombination
Autore:
Suenaga, H; Goto, M; Furukawa, K;
Indirizzi:
Kyushu Univ, Appl Microbiol Lab, Grad Sch Bioresource & Bioenvironm Sci, Fukuoka 8128581, Japan Kyushu Univ Fukuoka Japan 8128581 ioenvironm Sci, Fukuoka 8128581, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 25, volume: 276, anno: 2001,
pagine: 22500 - 22506
SICI:
0021-9258(20010622)276:25<22500:EOMOAB>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLYCHLORINATED BIPHENYL DEGRADATION; PSEUDOMONAS-PSEUDOALCALIGENES KF707; SITE-DIRECTED MUTAGENESIS; SP STRAIN LB400; NAPHTHALENE DIOXYGENASE; CHLORINE SUBSTITUTION; SUBSTRATE-SPECIFICITY; TOLUENE DIOXYGENASE; ALPHA-SUBUNIT; AMINO-ACIDS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Furukawa, K Kyushu Univ, Appl Microbiol Lab, Grad Sch Bioresource & Bioenvironm Sci, Hakozaki 6-10-1, Fukuoka 8128581, Japan Kyushu Univ Hakozaki 6-10-1 Fukuoka Japan 8128581 8581, Japan
Citazione:
H. Suenaga et al., "Emergence of multifunctional oxygenase activities by random priming recombination", J BIOL CHEM, 276(25), 2001, pp. 22500-22506

Abstract

Biphenyl dioxygenase (Bph Dox) is responsible for the initial dioxygenation of biphenyl, The large subunit (BphA1) of Bph Dox plays a crucial role indetermination of substrate specificity of biphenyl-related compounds including polychlorinated biphenyls (PCBs), Functional evolution of Bph Dox of Pseudomonas pseudoalcaligenes KF707 was accomplished by random priming recombination of the bphA1 gene, involving two rounds of in vitro recombination and mutation followed by selection for increased activity in vivo. Evolved Bph Dox acquired novel and multifunctional degradation capabilities not only for PCBs but also for dibenzofuran, dibenzo-p-dioxin, dibenzothiophene, and fluorene, the compounds scarcely attacked by the original KF707 Bph Dox. The modes of oxygenation were angular and lateral dioxygenation for dibenzofuran and dibenzo-p-dioxin, sulfoxidation for dibenzothiophene, and mono-oxygenation for fluorene, These enzymes also exhibited enhanced degradation abilities for PCB congeners, retaining 2,3-dioxygenase activity and gaining3,4-dioxygenase activity, depending on the chlorine substitution of PCB congeners. Further mutation analysis revealed that the amino acid at position376 in BphA1 is significantly involved in the acquisition of multifunctional oxygenase activities and mode of oxygenation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 03:47:40