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KMID : 1094720060110040337
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Biotechnology and Bioprocess Engineering
2006 Volume.11 No. 4 p.337 ~ p.343
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Purification, characterization, and cloning of trimethylamine dehydrogenase from Methylophaga sp. strain SK1
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Kim Hee-Gon
Kim Yan
Lim Heon-Man
Shin Hyun-Jae
Kim Si-Wouk
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Abstract
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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 fromMethylophaga 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°C, respectively. TheV max andK m values were 7.9 nmol/min/mg protein and 1.5 mM. A genomic DNA of 2,983 bp fromMethylophaga 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 ofMethylophilus methylotrophus W3A1.
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KEYWORD
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trimethylamine, trimethylamine dehydrogenase, tmd gene, Methylophaga sp. strain SK1
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