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Purification, Characterization, and Cloning of Trimethylamine Dehydrogenase from Methylophaga sp. Strain SK1  

Kim, Hee-Gon (Department of Biomaterials Engineering, Chosun University)
Kim, Yan (Department of Biomaterials Engineering, Chosun University)
Lim, Heon-Man (Department of Biology, Chungnam National University)
Shin, Hyun-Jae (Department of Chemical Engineering, Chosun University)
Kim, Si-Wouk (Department of Biomaterials Engineering, Chosun University)
Publication Information
Biotechnology and Bioprocess Engineering:BBE / v.11, no.4, 2006 , pp. 337-343 More about this Journal
Abstract
Trimethylamine dehydrogenase (TMADH, EC 1.5.99.7), an iron-sulfur flavoprotein that catalyzes the oxidative demethylation of trimethylamine to form dimethylamine and formaldehyde, was purified from Methylophaga sp. strain SK1. The active TMADH was purified 12.3-fold through three purification steps. The optimal pH and temperature for enzyme activity was determined to be 8.5 and $55^{\circ}C$, respectively. The $V_{max}\;and\;K_m$ values were 7.9 nmol/min/mg protein and 1.5 mM. A genomic DNA of 2,983 bp from Methylophaga sp. strain SK1 was cloned, and DNA sequencing revealed the open reading frame (ORF) of the gene coding for TMADH. The ORF contained 728 amino acids with extensive identity (82%) to that of Methylophilus methylotrophus $W_3A_1$.
Keywords
trimethylamine; trimethylamine dehydrogenase; tmd gene; Methylophaga sp. strain SK1;
Citations & Related Records
Times Cited By KSCI : 1  (Citation Analysis)
Times Cited By Web Of Science : 4  (Related Records In Web of Science)
Times Cited By SCOPUS : 4
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