Graduation Year
2009
Document Type
Thesis
Degree
M.S.
Degree Granting Department
Chemistry
Major Professor
David J. Merkler, Ph.D.
Committee Member
G. King Farrington, Ph.D.
Committee Member
Roman Manetsch, Ph.D.
Committee Member
Mark L. McLaughlin, Ph.D.
Keywords
Kinetics, Enzyme, Quinone, Mushroom, Oxygen electrode
Abstract
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.
Scholar Commons Citation
Shafer, Jacob A., "N-Acyltyramines as Substrates for Tyrosinase: Enzymatic Lag and Dopamine Precursor" (2009). Graduate Theses and Dissertations.
https://scholarcommons.usf.edu/etd/13