Purification, characterization, and cloning of trimethylamine dehydrogenase fromMethylophaga sp. strain SK1 |
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| Authors: | Hee Gon Kim Yan Kim Heon Man Lim Hyun-Jae Shin Si Wouk Kim |
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| Institution: | (1) Department of Biomaterials Engineering, Chosun University, 501-759 Gwangju, Korea;(2) Department of Biology, Chungnam National University, 305-764 Daejon, Korea;(3) Department of Chemical Engineering, Chosun University, 501-759 Gwangju, Korea;(4) Department of Environmental Engineering, BK21 Team for Biohydrogen Production, Chosun University, 501-759 Gwangju, Korea |
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| 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 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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| Keywords: | trimethylamine trimethylamine dehydrogenase tmd gene Methylophaga sp strain SK1 |
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