Tyrosinase is a widespread, highly studied and important enzyme involved in processes ranging from the browning of mushrooms to roles in mammalian cancer. The enzyme suffers from a noticeable lag phase while the enzyme generates all necessary cofactors from available substrates. There have not been significant studies of the effect on lag from moving through a family of substituted substrates. This thesis reports the results of one such study using a family of N-acyltyramines.
The selection of N-acyltyramines was ideal because the substrates in this reaction may be related to synthesis of N-acyldopamines, which serve many important physiological functions. It was concluded that the product formed from N-acetyltyramine is 1-acetyl-2,3-dihydro-1H-indole-6,7-dione, a quinone.
| Identifer | oai:union.ndltd.org:USF/oai:scholarcommons.usf.edu:etd-1012 |
| Date | 31 March 2009 |
| Creators | Shafer, Jacob A |
| Publisher | Scholar Commons |
| Source Sets | University of South Flordia |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Graduate Theses and Dissertations |
| Rights | default |
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