| Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2011: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2010: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2009: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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| Research Abstract |
Peptide C-terminalα-amide groups essential for the full biological activity of many peptide hormones are produced by a bifunctional peptidylglycineα-amidating enyme(PAM). PAM consists of peptidylglycineα-hydroxylating monooxygenase(PHM) and peptidylamidoglycolate lyase(PAL). The purposes of this study are the clarification of the roles of the metals in PAM for understanding its reaction mechanism. We prepared Apo-PAM/PAL and Metal(s)-substituted enzymes. Apo-enzymes are remarkably diminished the PHM and PAL activities. But the Cu-substituted PAM restored the PHM activity, the Zn-substituted PAL restored the PAL activity, and the Cu, Zn-substituted PAM fully restored the PAM(PHM and PAL) activity. In addition, the effects of a series of divalent metals on the PAM activity were determined. Based on the findings, we will discuss the roles of the enzyme-bound metals in the PAM reaction.
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