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Volumn 11, Issue 3, 2000, Pages 262-270

Engineering bacteria for bioremediation

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIUM; BIODEGRADATION; BIOENGINEERING; POLLUTION; PRIORITY JOURNAL; REVIEW; SOIL TREATMENT;

EID: 0034075043     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(00)00094-X     Document Type: Review
Times cited : (370)

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    • Broad host-range plasmids were constructed that contained the gene coding for haloalkane dehalogenase from Rhodococcus sp. strain M15-3, an enzyme capable of efficient transformation of trihalopropanes to dihalopropanols, under the control of different heterologous promoters. By introduction of these plasmids into Agrobacterium radiobacter AD1, which is capable of utilizing dihalogenated propanols for growth, recombinant organisms able to grow on trihalopropanes were obtained
    • Bosma T., Kruzinga E., Bruin E.J.D., Poelarends G.J., Janssen D.B. Utilization of trihalogenated propanes by Agrobacterium radiobacter AD1 through heterologous expression of the haloalkane dehalogenase from Rhodococcus sp. strain M15-3. Appl Environ Microbiol. 65:1999;4575-4581. Broad host-range plasmids were constructed that contained the gene coding for haloalkane dehalogenase from Rhodococcus sp. strain M15-3, an enzyme capable of efficient transformation of trihalopropanes to dihalopropanols, under the control of different heterologous promoters. By introduction of these plasmids into Agrobacterium radiobacter AD1, which is capable of utilizing dihalogenated propanols for growth, recombinant organisms able to grow on trihalopropanes were obtained.
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    • 2+ at the active site. By replacing Glu79 with histidine, a mutant enzyme was produced which binds the catalytic active iron more strongly. In addition, the mutant enzyme showed higher affinities for all substrates tested and a significant increase in the reaction rates with the majority of the substrates. Despite the higher iron binding affinity, however, the mutant enzyme was more sensitive to inactivation during substrate turnover.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.