Graduation Year
2003
Document Type
Thesis
Degree
M.S.
Degree Granting Department
Chemistry
Major Professor
David Merkler, Ph.D.
Committee Member
Randy Larsen, Ph.D.
Committee Member
Gloria Ferreira, Ph.D.
Keywords
enzyme, prostate, inhibition, 4-hpr, kinetics
Abstract
C-Terminal glycine-extended prohormones are enzymatically converted to á-amidated peptides, by peptidylglycine á-amidating monooxygenase (PAM). PAM is a bifunctional enzyme with two catalytic domains: peptidylglycine á-hydroxylating monooxygenase (PHM) and peptidylglycine peptidylglycineaminoglycolate lyase (PAL).
PAM has a significant role in the proliferation of androgen-independent prostate cancer. Thus, the inhibition of PAM could halt cancer growth. Hippurate and hippurate analogs were used as lead compounds for developing inhibitors for PAM. The hippurate analogs exhibiting the highest affinity to PAM (lowest inhibition constant) did inhibit the growth of human androgen-independent prostate cancer DU 145 cells.
Scholar Commons Citation
Chew, Geoffrey H., "Substrate-Based Inhibitors of Peptidylglycine á-Amidating Monooxygenase (PAM) as Anti-Proliferative Drugs for Cancer" (2003). USF Tampa Graduate Theses and Dissertations.
https://digitalcommons.usf.edu/etd/1341
