<em>N</em>-Acyltyramines as Substrates for Tyrosinase: Enzymatic Lag and Dopamine Precursor

• Main Author: Shafer, Jacob A
• Format: Others
• Published: Scholar Commons 2009
• Subjects: Kinetics; Enzyme; Quinone; Mushroom; Oxygen electrode; American Studies; Arts and Humanities
• Online Access: https://scholarcommons.usf.edu/etd/13; https://scholarcommons.usf.edu/cgi/viewcontent.cgi?article=1012&amp;context=etd

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.