Studies on coenzyme B12-dependent D-Ornithine 4,5-aminomutase from Clostridium sticklandii
碩士 === 國立臺北科技大學 === 生物科技研究所 === 96 === D-Ornithine aminomutase from Clostridium sticklandii catalyzes the 1,2-rearrangement reaction of D-Ornithine to (2R,4S)-2,4-diaminopentanoic acid. The enzyme comprises two subunits, OraS and OraE. Previous studies have shown that OraSE and OraE protein possess...
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| Format: | Others |
| Language: | zh-TW |
| Published: |
2008
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| Online Access: | http://ndltd.ncl.edu.tw/handle/dfxj96 |
| Summary: | 碩士 === 國立臺北科技大學 === 生物科技研究所 === 96 === D-Ornithine aminomutase from Clostridium sticklandii catalyzes the 1,2-rearrangement reaction of D-Ornithine to (2R,4S)-2,4-diaminopentanoic acid. The enzyme comprises two subunits, OraS and OraE. Previous studies have shown that OraSE and OraE protein possess proteolytic activities in the presence of certain metal ions. The enzymatic assay method for this activity is established in this study. Site-directed mutagenesis studies of putative metal-binding are also carried out. My results confirm that OraSE belongs to a families of metalloprotease, and its substrate specificity is also investigated. Finally, I first show that the enzyme posseses novell activities toward D-a-Lysine. That Kcat and Km value for D-A_Lysine is also determind.
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