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Title 

Structural and fuctional characterization of S-adenosylmethionine (SAM) synthetase from Pichia ciferrii

 

Pichia ciferrii의 S-adenosylmethionine (SAM) synthetase에 대한 구조 및 기능적 특성

Authors 

S YoonW LeeMin-Soo KimT D KimY Ryu

Publisher 

Springer Verlag (Germany)

Issue Date 

2012

Citation 

Bioprocess and Biosystems Engineering, vol. 35, no. 1, pp. 173-181

Abstract 

S-adenosylmethionine synthetase (SAM-s) catalyzes the synthesis of S-adenosylmethionine (SAM), which is essential for methylation, transcription, proliferation, and production of secondary metabolites. Here SAM-s from Pichia ciferrii were selectively cloned using RNA CapFishing and rapid amplification of cDNA ends (RACE). The putative full-length cDNA of SAM-s encoded a 383 amino acid protein (42.6 kDa), which has highly conserved metal binding sites, a phosphate-binding site, and functionally important motifs. The corresponding enzyme was over-expressed in a heterologous host of Pichia pastoris, and then purified to a homogenous form. Enzyme kinetics, immunoblotting, circular dichroism (CD), high performance liquid chromatography (HPLC), and molecular modeling were conducted to characterize the SAM-s from P. ciferrii. Structural and functional studies of SAM-s will provide important insights for industrial applications.

ISSN 

1615-7591

Link 

http://dx.doi.org/10.1007/s00449-011-0640-x

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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