2001
DOI: 10.1006/bbrc.2001.5449
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Molecular Characterization of the 56-kDa CYP153 from Acinetobacter sp. EB104

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Cited by 124 publications
(103 citation statements)
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References 35 publications
(18 reference statements)
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“…EB104 (Fig. 3b), which catalyzes the terminal oxidation of alkanes 22 . Thus, the three P450 systems are likely to account for an important part of the expanded hydrocarbon degradation capacity of A. borkumensis SK2.…”
Section: Genomic Islands and Mobile Genetic Elementsmentioning
confidence: 99%
“…EB104 (Fig. 3b), which catalyzes the terminal oxidation of alkanes 22 . Thus, the three P450 systems are likely to account for an important part of the expanded hydrocarbon degradation capacity of A. borkumensis SK2.…”
Section: Genomic Islands and Mobile Genetic Elementsmentioning
confidence: 99%
“…EB104 [205]. In contrast to the eukaryotic membrane-bound P450 systems, the CYP153 appeared to occur as a soluble protein [206] like other bacterial P450s involved in other Chapter 1 -General Introduction 33 metabolic pathways.…”
Section: Cytochrome P450 Alkane Hydroxylasesmentioning
confidence: 99%
“…In contrast to the eukaryotic membrane-bound P450 systems, the CYP153 appeared to occur as a soluble protein [206] like other bacterial P450s involved in other Chapter 1 -General Introduction 33 metabolic pathways. This purified P450 exhibited n-alkane-oxidizing activity in the presence of ferredoxin and ferredoxin reductase isolated from the same bacterium [207] and it seemed to be induced by a variety of hydrocarbons [205,207]. Subsequently, highly degenerate primers were designed based on conserved sequence motifs in CYP153A1 and two CYP153…”
Section: Cytochrome P450 Alkane Hydroxylasesmentioning
confidence: 99%
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