Mechanistic and structural studies of nitroalkane oxidase from Fusarium oxysporum /
a ping pong mechanism. The pH dependence of the V/K data are
| Main Author: | |
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| Format: | Thesis eBook |
| Language: | English |
| Published: |
[Place of publication not identified] :
[publisher not identified] ;
1995.
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| Subjects: | |
| Online Access: | Link to OAKTrust copy |
| Summary: | a ping pong mechanism. The pH dependence of the V/K data are aidehyde or ketone. The enzyme was purified by using a three carbon position. The enzyme activity is dependent on added consistent with the enzyme having an ionizable group which denitrification of a nitroalkane to the corresponding mechanistic studies of nitroalkane oxidase from Fusarium must be deprotonated for activity with a pKa of 6.8 and a N-terminus has been determined. nitroethane, 1 -nitropropane, and 1 -nitropentane, all fit to oxidized flavin. In addition, the amino acid sequence of the oxysponim. Nitroalkane oxidase catalyzes the oxidative perform many analyses. The substrates used to date, requirement for the substrate to be protonated in the a step purification scheme in large enough quantities to This thesis describes the purification and the initial |
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| Item Description: | "Major subject: Biochemistry". Vita. |
| Physical Description: | x, 31 leaves : illustrations ; 28 cm. Also available online. Issued also on microfiche from Lange Micrographics. |
| Bibliography: | Includes bibliographical references. |