Structural and fuctional characterization of S-adenosylmethionine (SAM) synthetase from Pichia ciferrii = Pichia ciferrii의 S-adenosylmethionine (SAM) synthetase에 대한 구조 및 기능적 특성

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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
Author(s)
S Yoon; W Lee; Min-Soo Kim; T D Kim; Y Ryu
Bibliographic Citation
Bioprocess and Biosystems Engineering, vol. 35, no. 1, pp. 173-181
Publication Year
2012
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.
Keyword
S-adenosylmethionineSAM synthetasePichia ciferriiRNA CapFishingRapid amplification of cDNA ends
ISSN
1615-7591
Publisher
Springer
DOI
http://dx.doi.org/10.1007/s00449-011-0640-x
Type
Article
Appears in Collections:
Jeonbuk Branch Institute > Microbial Biotechnology Research Center > 1. Journal Articles
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