Purification, characterization, and cloning of trimethylamine dehydrogenase from Methylophaga sp. strain SK1
Biotechnology and Bioprocess Engineering, ISSN: 1226-8372, Vol: 11, Issue: 4, Page: 337-343
2006
- 7Citations
- 4Captures
Metric Options: Counts1 Year3 YearSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Article Description
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°C, respectively. The V and K 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 WA. ©KSBB.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33748507364&origin=inward; http://dx.doi.org/10.1007/bf03026250; http://link.springer.com/10.1007/BF03026250; http://link.springer.com/content/pdf/10.1007/BF03026250; http://link.springer.com/content/pdf/10.1007/BF03026250.pdf; http://link.springer.com/article/10.1007/BF03026250/fulltext.html; http://www.springerlink.com/index/pdf/10.1007/BF03026250; https://dx.doi.org/10.1007/bf03026250; https://link.springer.com/article/10.1007/BF03026250; http://www.springerlink.com/index/10.1007/BF03026250
Springer Science and Business Media LLC
Provide Feedback
Have ideas for a new metric? Would you like to see something else here?Let us know