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Identification of Two Superoxide Dismutases (FeSOD and NiSOD) from Streptomyces peucetius ATCC 27952
Kanth, Bashistha Kumar,Oh, Tae-Jin,Sohng, Jae-Kyung 한국생물공학회 2010 Biotechnology and Bioprocess Engineering Vol.15 No.5
In this study, the whole genome of Streptomyces peucetius ATCC 27952 was analyzed and two superoxide dismutases (SODs), named sp-sod1 and sp-sod2, were identified. The sp-sod1 is a putative Fe-Zn sod that is 636 bp in length. The sp-sod2 is a putative NiSOD that is 396 bp in length. The deduced amino acid sequence of sp-sod1 shared approximately 85 ~ 90% identity with the iron sod of S. griseus, S. coelicolor A3(2), and S. avermitilis MA-4680 whereas sp-sod2 shared approximately 87 ~ 94% identity with S. avermitilis, S. coelicolor A3(2) and S. seoulensis. The sp-sod1 was characterized to be FeSOD in the sod mutant E. coli QC871. The N-terminal deleted sp-sod2 along with a putative signal peptidase sp-sodX, which was immediately downstream, was co-expressed in E. coli. This recombinant E. coli strain did not produce the processed mature Sp-SOD2 unlike S. coelicolor Muller. However, Sp-SOD2 was confirmed to be NiSOD in S. lividans TK24.
Streptomyces peucetius ATCC 27952 에서 Cytochrome P450 CYP107P3 의 컴퓨터 모델링
바시스터 水原大學校 2016 論文集 Vol.30 No.-
Streptomyces peucetius ATCC 27952 에서 CYP107P3는 7-ethoxycumarin를 putidaredoxin reductase 및 putidaredoxin의 합성으로 E. coli 안에서 7 hydroxycumarin으로 변환한다. CYP107P3의 동성 모델 은 템플릿 1EGY (CYP107A1), CV9 (CYP105A1), 2VZ7 (CYP107L1) 및 2WM4 (CYP124) 를 선택에 의 해 만들어진. 1EGY (CYP107A1), 3CV9 (CYP105A1), 2VZ7 (CYP107L1) 및 2WM4 (CYP124) CYP107P3 와 35 %, 34 %, 38 %, 36 %의 정체성 각각을 공유한다. 그 모델 7-ethoxycumarin과의 상호 작용을 연구하는데 사용될 수 있도록 모델화 CYP107P3는 품질 평가했다.
백승필,전소영,( Bashistha Kumar Kanth ),민기하,이창현 한국공업화학회 2014 한국공업화학회 연구논문 초록집 Vol.2014 No.1
Carbonic anhydrase (CA) has recently been considered as an efficient biocatalyst applicable for CO<sub>2</sub> capture process. We constructed codonoptimized sequence of PP-zCA and set up its expression/purification system using E. coli host. Subsequently, we characterized various properties of novel PP-zCA. PP-zCA was most active at ~50°C and pH 8.0 in 50 mM Tris/SO<sub>4</sub> buffer, and retained 70 % of its activity after incubation at 70°C for 15 min. We also demonstrated that PP-zCA enzyme can catalyze the conversion of CO<sub>2</sub> to CaCO<sub>3</sub>. SEM image revealed rhombohedral calcite crystals. XRD analysis of precipitated CaCO<sub>3</sub> indicates formation of a calcite phase. The 2θ diffraction peaks occurred at 29.5, 36.1, 39.5, and 43.3°, corresponding to the calcite crystal faces (104), (110), (113), and (202), respectively and the representative crystal surface of calcite was 2θ = 29.42.