Document Detail


Architecture and characterization of sarcosine oxidase from Thermococcus kodakarensis KOD1.
MedLine Citation:
PMID:  22083128     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Sarcosine oxidase (SOX) catalyzes the oxidation of the methyl group in sarcosine and transfer of the oxidized methyl group into the one-carbon metabolic pool. Here, we separately cloned and expressed α and β subunit of SOX from Thermococcus kodakarensis KOD1 (TkSOX) in Escherichia coli and the recombinant proteins were purified to homogeneity. Gel filtration chromatography and transmission electron microscopy analysis showed that the α subunit formed a dimeric structure and behaved as an NADH dehydrogenase; β subunit was a tetramer that had sarcosine oxidase and L: -proline dehydrogenase activity. The TkSOX complex assembled into the hetero-octameric (αβ)(4) form and had NADH dehydrogenase activity. Gold-label analysis indicated that α and β subunits were oriented in the alternative form. Based on these results, we suggested that TkSOX was a multifunctional enzyme and that each subunit and (αβ)(4) complex may separately exist as a function enzyme in different conditions.
Authors:
Sangmin Lee; Baolei Jia; Bang Phuong Pham; Yongqi Shao; Jae Myeong Kwak; Gang-Won Cheong
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-11-15
Journal Detail:
Title:  Extremophiles : life under extreme conditions     Volume:  -     ISSN:  1433-4909     ISO Abbreviation:  -     Publication Date:  2011 Nov 
Date Detail:
Created Date:  2011-11-15     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9706854     Medline TA:  Extremophiles     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Division of Applied Life Sciences (BK21 Program), Gyeongsang National University, Jinju, 660-701, Korea.
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