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Title 

Purification and characterization of a cytochrome P-450 from pravastatin-producing Streptomyces sp. Y-110

Authors 

Joo Woong ParkJoo Kyung LeeTae Jong KwonDong Hee YiYong Il ParkSang Mo Kang

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

2001

Citation 

Journal of Microbiology and Biotechnology, vol. 11, no. 6, pp. 1011-1017

Keywords 

cytochrome P-450enzyme purificationhydroxylationhypercholesterolemiapravastatinstreptomyces sp. Y-1002 diethylaminoethanolalanineasparaginecarbon monoxide

Abstract 

Streptomyces sp. Y-110 cytochrome P-450, induced by the addition of compactin-Na into the culture medium, was purified from the cell extract to apparent homogeniety, mainly by DEAE-Sepharose, hydroxyapatite, and Mono Q column chromatography. The specific activity of purified enzyme on its substrate, compactin-Na, was determined to be 15 nmol of pravastatin per mg protein. The molecular mass of this enzyme on SDS-PAGE was 37±0.5 kDa, pI was 4.5, and its CO difference spectrum showed maximum absorption peaks at 452 and 550 nm, respectively. The N-terminal amino acid sequence was determined to be Met>Thr>Cys>Thr>Pro> 1.028 μM · min-1. The maximum substrate concentration (Ks) for reaction was 270 μM and thus 1/[Ks] was 3.7 μM. These physicochemical characteristics and kinetic behavior of this enzyme were compared and shown to be different from those of Streptomyces cytochrome P-450 enzymes reported, suggesting that this enzyme may be an additional member of the Streptomyces cytochrome P-450 family.

ISSN 

1017-7825

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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